NCBI Conserved Domain Search

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 106.53 E-value: 7.60e-27

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809    288 CDPDWTPFNRKCYKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRDENASET-WIGLSSNKIPVSFEWSSGS 366
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYyWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 568915809    367 S-VIFTNWYPLEPrilPNRRQLCVSAEESDGRWKVKDCKERLFYICK 412
Cdd:smart00034   81 GpVSYSNWAPGEP---NNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 98.06 E-value: 7.03e-24

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809   1161 WIKFKGNCYSFSTvlDSRSFEDAHEFCKSEGSNLLAIRDAAENSFLLeELLAFGSSVQMVWLNAQFDNNNKTLRWFDGTP 1240
Cdd:smart00034    5 WISYGGKCYKFST--EKKTWEDAQAFCQSLGGHLASIHSEAENDFVA-SLLKNSGSSDYYWIGLSDPDSNGSWQWSDGSG 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 568915809   1241 TEQ-SNWglrKPDMDHLKPHPCVVLRIPEGIWHFTPCEDKKGFICK 1285
Cdd:smart00034   82 PVSySNW---APGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 96.92 E-value: 1.64e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  153 CYQFNLlSSLSWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVVKE-VWIGLNQLDEKAGWQWSDGTP-LSYLNWSQE 230
Cdd:cd00037     2 CYKFST-EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568915809  231 iTPGPFVEHHCGTLEVVSAA-WRSRDCESTLPYICKR 266
Cdd:cd00037    81 -EPNPGGSEDCVVLSSSSDGkWNDVSCSSKLPFICEK 116

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 96.90 E-value: 1.91e-23

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809    140 CDATWQRNGSSriCYQFNLlSSLSWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVVK--EVWIGLNQLDEKAGWQWS 217
Cdd:smart00034    1 CPSGWISYGGK--CYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdYYWIGLSDPDSNGSWQWS 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 568915809    218 DGTPL-SYLNWSqeITPGPFVEHHCGTLEVVSAAWRSRDCESTLPYICK 265
Cdd:smart00034   78 DGSGPvSYSNWA--PGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 96.51 E-value: 2.66e-23

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809    865 CPKGWLYFNYKCFLVTipkdpRELKTWTGAQEFCVAKGGTLVSIKSELEQAFIT--MNLFGQTTNVWIGLQSTNHE---K 939
Cdd:smart00034    1 CPSGWISYGGKCYKFS-----TEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNgswQ 75

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915809    940 WVNGKPLV-YSNWSPSdiinipsynttEFQKHIPLCALMSSNpnfhfTGKWYFDDCGKEgYGFVCE 1004
Cdd:smart00034   76 WSDGSGPVsYSNWAPG-----------EPNNSSGDCVVLSTS-----GGKWNDVSCTSK-LPFVCE 124

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 94.61 E-value: 9.23e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  298 KCYKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRDENASETWIGLSSNKIPVSFEWSSGSS-VIFTNWYPL 376
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568915809  377 EPRilPNRRQLCVSAE-ESDGRWKVKDCKERLFYICKK 413
Cdd:cd00037    81 EPN--PGGSEDCVVLSsSSDGKWNDVSCSSKLPFICEK 116

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 89.97 E-value: 5.57e-21

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809    425 CPAGWERHGRFCYKIDTVLRSFEEASSgyYCS---PALLTITSRFEQAFITSLISSVAeKDSYFWIALQDQNNTGEYTWk 501
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQA--FCQslgGHLASIHSEAENDFVASLLKNSG-SSDYYWIGLSDPDSNGSWQW- 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568915809    502 tVGQREPVQYTYWNTRQPSNRGG-CVVVRGGSslGRWEVKDCSDfKAMSLCK 552
Cdd:smart00034   77 -SDGSGPVSYSNWAPGEPNNSSGdCVVLSTSG--GKWNDVSCTS-KLPFVCE 124

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.

Pssm-ID: 238019 Cd Length: 48 Bit Score: 85.43 E-value: 2.03e-20

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568915809   83 NAHGMPCVFPFQFKGHWHHDCIREGQKEHLLWCATTSRYEEDEKWGFC 130
Cdd:cd00062     1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 88.04 E-value: 2.56e-20

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809    724 WLFYQNAEYLFHTHPAEWATFEFVCGWLRSDFLTIYSAQEQEFIHSKIKGLTKYGvKWWIGLEEGGARDQIQWSNGSP-V 802
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGSWQWSDGSGpV 83

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 568915809    803 IFQNWDKGREervDSQRKRCVFISSITGLWGTENCSVPLPSICK 846
Cdd:smart00034   84 SYSNWAPGEP---NNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.

Pssm-ID: 128373 Cd Length: 49 Bit Score: 84.27 E-value: 6.10e-20

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 568915809     82 GNAHGMPCVFPFQFKGHWHHDCIREGQKEHLLWCATTSRYEEDEKWGFC 130
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 86.50 E-value: 9.66e-20

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809   1028 YGNRTYKIIRGNMTWYAAGKSCRMHRAELASIPDAFHQAFLTVLLSRLGHT--HWIGLSTTDNGQTFDWSDGTKS-PFTY 1104
Cdd:smart00034    8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGSGPvSYSN 87

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 568915809   1105 W-KDEESAFLGDCAFADTN-GRWHSTACESFLqGAIC 1139
Cdd:smart00034   88 WaPGEPNNSSGDCVVLSTSgGKWNDVSCTSKL-PFVC 123

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 85.75 E-value: 1.13e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  875 KCFLVTipkdpRELKTWTGAQEFCVAKGGTLVSIKSELEQAFITMNL-FGQTTNVWIGLQSTNHE---KWVNGKPLV-YS 949
Cdd:cd00037     1 SCYKFS-----TEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkKSSSSDVWIGLNDLSSEgtwKWSDGSPLVdYT 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568915809  950 NWSPsdiiNIPSYNTTEFqkhiplCALMSSNPNfhftGKWYFDDCGKEgYGFVCEK 1005
Cdd:cd00037    76 NWAP----GEPNPGGSED------CVVLSSSSD----GKWNDVSCSSK-LPFICEK 116

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 86.11 E-value: 1.32e-19

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809    572 CYMDWESATGlaSCFKVFHSEKvlmkrSWREAEAFCEEFGAHLASFAHIEEENFVNELLHskfNWTQERQFWIGFNRRNp 651
Cdd:smart00034    1 CPSGWISYGG--KCYKFSTEKK-----TWEDAQAFCQSLGGHLASIHSEAENDFVASLLK---NSGSSDYYWIGLSDPD- 69

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 568915809    652 lNAGSWAWSDGSPVVS-SFLDNAYFEEDAKNCAVYKANKTLL-PSNCASKHEWIC 704
Cdd:smart00034   70 -SNGSWQWSDGSGPVSySNWAPGEPNNSSGDCVVLSTSGGKWnDVSCTSKLPFVC 123

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 83.82 E-value: 5.54e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1167 NCYSFSTvlDSRSFEDAHEFCKSEGSNLLAIRDAAENSFLLEelLAFGSSVQMVWLNAQFDNNNKTLRWFDGTPTEQ-SN 1245
Cdd:cd00037     1 SCYKFST--EKLTWEEAQEYCRSLGGHLASIHSEEENDFLAS--LLKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDyTN 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568915809 1246 WGLRKPDMDhlKPHPCVVLRI-PEGIWHFTPCEDKKGFICKM 1286
Cdd:cd00037    77 WAPGEPNPG--GSEDCVVLSSsSDGKWNDVSCSSKLPFICEK 116

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 81.51 E-value: 3.44e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  584 SCFKVFHSekvlmKRSWREAEAFCEEFGAHLASFAHIEEENFVNELLHSKfnwtQERQFWIGFNRRNplNAGSWAWSDGS 663
Cdd:cd00037     1 SCYKFSTE-----KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKS----SSSDVWIGLNDLS--SEGTWKWSDGS 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568915809  664 PVV--SSFLDNAYFEEDAKNCAVYKANKTLL--PSNCASKHEWIC 704
Cdd:cd00037    70 PLVdyTNWAPGEPNPGGSEDCVVLSSSSDGKwnDVSCSSKLPFIC 114

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 80.60 E-value: 6.27e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809   161 SLSWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVVKEVWIGLNQLDEKAGWQWSDGTPLSYLNWSQEITPGPFVEhH 240
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGENE-D 79

                           90       100
                   ....*....|....*....|....*.
gi 568915809   241 CGTLEVVSAAWRSRDCESTLPYICKR 266
Cdd:pfam00059   80 CVELSSSSGKWNDENCNSKNPFVCEK 105

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 79.59 E-value: 2.03e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1033 YKIIRGNMTWYAAGKSCRMHRAELASIPDAFHQAFLTVLLSRLGHTH-WIGLSTTDNGQTFDWSDGTK-SPFTYWKDEE- 1109
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvWIGLNDLSSEGTWKWSDGSPlVDYTNWAPGEp 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568915809 1110 -SAFLGDCAF--ADTNGRWHSTACESfLQGAIC 1139
Cdd:cd00037    83 nPGGSEDCVVlsSSSDGKWNDVSCSS-KLPFIC 114

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 79.06 E-value: 2.14e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  1177 SRSFEDAHEFCKSEGSNLLAIRDAAENSFLLEELLAFGSSvqmVWLNAQFDNNNKTLRWFDGTPTEQSNWGlRKPDMDHL 1256
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY---FWIGLTDRKNEGTWKWVDGSPVNYTNWA-PEPNNNGE 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 568915809  1257 KPHpCVVLRIPEGIWHFTPCEDKKGFICKM 1286
Cdd:pfam00059   77 NED-CVELSSSSGKWNDENCNSKNPFVCEK 105

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 79.06 E-value: 2.35e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809   306 RKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRDENASeTWIGLSSNKIPVSFEWSSGSSVIFTNWYPLEPRilPNRR 385
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY-FWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNN--NGEN 77

                           90       100
                   ....*....|....*....|....*...
gi 568915809   386 QLCVSAEESDGRWKVKDCKERLFYICKK 413
Cdd:pfam00059   78 EDCVELSSSSGKWNDENCNSKNPFVCEK 105

Fibronectin type II domain;

Pssm-ID: 459645 Cd Length: 42 Bit Score: 74.91 E-value: 9.06e-17

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 568915809    89 CVFPFQFKGHWHHDCIREGQKEHLLWCATTSRYEEDEKWGFC 130
Cdd:pfam00040    1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 76.36 E-value: 1.90e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809   889 KTWTGAQEFCVAKGGTLVSIKSELEQAFITMNLFGQTTNVWIGLQSTNHEK---WVNGKPLVYSNWSPSDIINIPSYNtt 965
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGtwkWVDGSPVNYTNWAPEPNNNGENED-- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 568915809   966 efqkhiplCALMSSNPnfhftGKWYFDDCGKEgYGFVCEK 1005
Cdd:pfam00059   80 --------CVELSSSS-----GKWNDENCNSK-NPFVCEK 105

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 74.19 E-value: 1.29e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  732 YLFHTHPAEWATFEFVCGWLRSDFLTIYSAQEQEFIHSKIKGLTKYgvKWWIGLEEGGARDQIQWSNGSP-VIFQNWDKG 810
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSS--DVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568915809  811 reERVDSQRKRCVFIS-SITGLWGTENCSVPLPSICKR 847
Cdd:cd00037    81 --EPNPGGSEDCVVLSsSSDGKWNDVSCSSKLPFICEK 116

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 74.72 E-value: 1.40e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  153 CYQFnLLSSLSWNQAHSSCLM--QGGALLSIADEDEEDFIRKHLSKVVKE---VWIGLNQLDEKAGWQWSDGTPLSYLNW 227
Cdd:cd03594    12 CYGY-FRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQKAyqpVWIGLHDPQQSRGWEWSDGSKLDYRSW 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568915809  228 SQ-EITPGPfveHHCGTLEVVSA--AWRSRDCESTLPYICK 265
Cdd:cd03594    91 DRnPPYARG---GYCAELSRSTGflKWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 74.29 E-value: 1.44e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  140 CDATWQRNGSSriCYQFNLlSSLSWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKvvKEVWIGLNQLDEKAGWQWSDG 219
Cdd:cd03593     1 CPKDWICYGNK--CYYFSM-EKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568915809  220 TPLSylNWSQEITPGPfvEHHCGTLEVVSAAwrSRDCESTLPYICKR 266
Cdd:cd03593    76 SPLN--NLFNIRGSTK--SGNCAYLSSTGIY--SEDCSTKKRWICEK 116

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 73.49 E-value: 3.23e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  865 CPKGWLYFNYKCFLVTipkdpRELKTWTGAQEFCVAKGGTLVSIKSELEQAFITMNLFGQtTNVWIGLQSTNHE---KWV 941
Cdd:cd03590     1 CPTNWKSFQSSCYFFS-----TEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGN-RSYWIGLSDEETEgewKWV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915809  942 NGKPLV--YSNWSPSDiiniPSYNTTEFQKhiplCALMSSNpnfhfTGKWYFDDCGKEgYGFVCEK 1005
Cdd:cd03590    75 DGTPLNssKTFWHPGE----PNNWGGGGED----CAELVYD-----SGGWNDVPCNLE-YRWICEK 126

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 71.88 E-value: 8.97e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  435 FCYKIDTVLRSFEEASSgyYC---SPALLTITSRFEQAFITSLISSvaEKDSYFWIALQDQNNTGEYTWktVGQREPVQY 511
Cdd:cd00037     1 SCYKFSTEKLTWEEAQE--YCrslGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSEGTWKW--SDGSPLVDY 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568915809  512 TYWNTRQPSNRGG--CVVVRgGSSLGRWEVKDCSDfKAMSLCK 552
Cdd:cd00037    75 TNWAPGEPNPGGSedCVVLS-SSSDGKWNDVSCSS-KLPFICE 115

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 70.09 E-value: 5.88e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  288 CDPDWTPFNRKCYKLKKDRKSWLGALHSCQS--NDSVLMDVASLAEVEFLVSLLRDENASE--TWIGLSSNKIPVSFEWS 363
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQKAYqpVWIGLHDPQQSRGWEWS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915809  364 SGSSVIFTNWYPLEPRilpNRRQLCVSAEESDG--RWKVKDCKERLFYICK 412
Cdd:cd03594    81 DGSKLDYRSWDRNPPY---ARGGYCAELSRSTGflKWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 69.69 E-value: 7.91e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  288 CDPDWTPFNRKCYKLKKDRKSWLGALHSCQSNDSV-----LMDVASLAEVEFLVSLLR----DENASETWIGLSSNKIPV 358
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSIPgliahLVSIHSQEENDFVYDLFEssrgPDTPYGLWIGLHDRTSEG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568915809  359 SFEWSSGSSVIFTNWYPLEPRILPNRRQlCV---SAEESDGRWKVKDCKERLFYICK 412
Cdd:cd03589    81 PFEWTDGSPVDFTKWAGGQPDNYGGNED-CVqmwRRGDAGQSWNDMPCDAVFPYICK 136

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 68.90 E-value: 1.06e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  584 SCFKVFHSEKvlmkrSWREAEAFCEEFGAHLASFAHIEEENFVNELLHSKFnwtqerqFWIGFNRRNPlnAGSWAWSDGS 663
Cdd:cd03593    11 KCYYFSMEKK-----TWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS-------YWIGLSREKS--EKPWKWIDGS 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568915809  664 PVVSSFLDNayFEEDAKNCAVYKANKtLLPSNCASKHEWIC 704
Cdd:cd03593    77 PLNNLFNIR--GSTKSGNCAYLSSTG-IYSEDCSTKKRWIC 114

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 68.27 E-value: 1.31e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  1040 MTWYAAGKSCRMHRAELASIPDAFHQAFLTVLLSRLGHTHWIGLSTTDNGQTFDWSDGTKSPFTYWKDEES--AFLGDCA 1117
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNnnGENEDCV 81

                           90       100
                   ....*....|....*....|....
gi 568915809  1118 -FADTNGRWHSTACESfLQGAICH 1140
Cdd:pfam00059   82 eLSSSSGKWNDENCNS-KNPFVCE 104

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 68.17 E-value: 1.47e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1031 RTYKIIRGNMTWYAAGKSCRMHRAELASIPDAFHQAFLTVLLSRLGHTHWIGLSttDNGQTFDWSDGTKSPFTYWKDEES 1110
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLY--RDVDSWRWSDGSESSFRNWNTFQP 78

                          90       100
                  ....*....|....*....|....
gi 568915809 1111 AFLGDCAFADTNGRWHSTACESFL 1134
Cdd:cd03602    79 FGQGDCATMYSSGRWYAALCSALK 102

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 67.33 E-value: 4.32e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1161 WIKFKGNCYSFSTvlDSRSFEDAHEFCKSEGSNLLAIRDAAENSFLLEELlafgSSVQMVWLNAQFDNNNKTLRWFDGTP 1240
Cdd:cd03590     5 WKSFQSSCYFFST--EKKSWEESRQFCEDMGAHLVIINSQEEQEFISKIL----SGNRSYWIGLSDEETEGEWKWVDGTP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568915809 1241 --TEQSNWGLRKPDMDHLKPHPCVVLRIPEGIWHFTPCEDKKGFICKM 1286
Cdd:cd03590    79 lnSSKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 67.40 E-value: 5.41e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1161 WIKFKGNCYSFstVLDSRSFEDAHEFCKS--EGSNLLAIRDAAENSFLLEELLAFGSSVQMVWLNAQFDNNNKTLRWFDG 1238
Cdd:cd03594     5 WLPYKGNCYGY--FRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRGWEWSDG 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568915809 1239 TPTEQSNWgLRKPDMdhLKPHPCVVLRIPEGI--WHFTPCEDKKGFICK 1285
Cdd:cd03594    83 SKLDYRSW-DRNPPY--ARGGYCAELSRSTGFlkWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 66.56 E-value: 9.94e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  425 CPAGWERHGRFCYKIDTVLRSFEEASSgyYCSPA---LLTITSRFEQAFITSLISSvaekDSYFWIALQDQNNTGEytWK 501
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQ--FCEDMgahLVIINSQEEQEFISKILSG----NRSYWIGLSDEETEGE--WK 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568915809  502 TV-GQREPVQYTYWNTRQPSNRGG----CVVVRggSSLGRW 537
Cdd:cd03590    73 WVdGTPLNSSKTFWHPGEPNNWGGggedCAELV--YDSGGW 111

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 65.91 E-value: 1.31e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  890 TWTGAQEFCVAKGGTLVSIKSELEQAFITmNLFGQTTNVWIGLQSTNHE---KWVNGKPLVYSNWSPSDiiniPSYNTTE 966
Cdd:cd03603    11 TWEAAQTLAESLGGHLVTINSAEENDWLL-SNFGGYGASWIGASDAATEgtwKWSDGEESTYTNWGSGE----PHNNGGG 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568915809  967 FQKHIPlcalmsSNPNFHFTGKWYFDDCGKEGYGFVCE 1004
Cdd:cd03603    86 NEDYAA------INHFPGISGKWNDLANSYNTLGYVIE 117

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 65.05 E-value: 1.94e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  288 CDPDWTPFNRKCYKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRdenASETWIGLSSNKIPVSFEWSSGSs 367
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIG---SSSYWIGLSREKSEKPWKWIDGS- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568915809  368 vIFTNWYPLeprILPNRRQLCVSAeeSDGRWKVKDCKERLFYICKK 413
Cdd:cd03593    77 -PLNNLFNI---RGSTKSGNCAYL--SSTGIYSEDCSTKKRWICEK 116

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 65.68 E-value: 1.94e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  288 CDPDWTPFNRKCYKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRDENasetWIGLSSNKIPVSFEWSSGSS 367
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ----WIGLNDRTIEGDFRWSDGHP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568915809  368 VIFTNWYPLEPRILPNRRQLC-VSAEESDGRWKVKDCKERLFYICKK 413
Cdd:cd03588    77 LQFENWRPNQPDNFFATGEDCvVMIWHEEGEWNDVPCNYHLPFTCKK 123

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 64.04 E-value: 3.55e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809   741 WATFEFVCGWLRSDFLTIYSAQEQEFIHSKIKgltKYGVKWWIGLEEGGARDQIQWSNGSPVIFQNWdkGREERVDSQRK 820
Cdd:pfam00059    4 WDEAREACRKLGGHLVSINSAEELDFLSSTLK---KSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNW--APEPNNNGENE 78

                           90       100
                   ....*....|....*....|....*..
gi 568915809   821 RCVFISSITGLWGTENCSVPLPSICKR 847
Cdd:pfam00059   79 DCVELSSSSGKWNDENCNSKNPFVCEK 105

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 64.28 E-value: 4.64e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  865 CPKGWLYFNYKCFLVTipkdpRELKTWTGAQEFCVAKGGTLVSIKSELEQAFITMNLFGQttNVWIGL--QSTNHE-KWV 941
Cdd:cd03593     1 CPKDWICYGNKCYYFS-----MEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS--SYWIGLsrEKSEKPwKWI 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915809  942 NGKPLvysnwspSDIINIPSYNTTEFqkhiplCALMSSNpnfhftgKWYFDDCGKEgYGFVCEK 1005
Cdd:cd03593    74 DGSPL-------NNLFNIRGSTKSGN------CAYLSST-------GIYSEDCSTK-KRWICEK 116

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 63.54 E-value: 1.08e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  583 ASCFKVFHSEKvlmkrSWREAEAFCEEF--GAHLASFAHIEEENFVNELLHSKFNWTQErqFWIGFNRrnPLNAGSWAWS 660
Cdd:cd03594    10 GNCYGYFRQPL-----SWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISSYQKAYQP--VWIGLHD--PQQSRGWEWS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568915809  661 DGS-PVVSSFLDNAYFeEDAKNCAVYKANKTLLP---SNCASKHEWICR 705
Cdd:cd03594    81 DGSkLDYRSWDRNPPY-ARGGYCAELSRSTGFLKwndANCEERNPFICK 128

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 62.50 E-value: 1.44e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809   597 KRSWREAEAFCEEFGAHLASFAHIEEENFVNELLHSkfnwtQERQFWIGFNRRNplNAGSWAWSDGSPVVSSFLdNAYFE 676
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKK-----SNKYFWIGLTDRK--NEGTWKWVDGSPVNYTNW-APEPN 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 568915809   677 EDAKN--CAVY-KANKTLLPSNCASKHEWIC 704
Cdd:pfam00059   73 NNGENedCVELsSSSGKWNDENCNSKNPFVC 103

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 62.76 E-value: 2.08e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  425 CPAGWERHGRFCYKIDTVLRSFEEASSgyYC--------SPALLTITSRFEQAFITSLISSVAEKDSYF--WIALQDQNN 494
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAEL--RCrsfsipglIAHLVSIHSQEENDFVYDLFESSRGPDTPYglWIGLHDRTS 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915809  495 TGEYTWkTVGQrePVQYTYWNTRQPSNRGG---CVV-VRGGSSLGRWevKDCSDFKAMSL-CKT 553
Cdd:cd03589    79 EGPFEW-TDGS--PVDFTKWAGGQPDNYGGnedCVQmWRRGDAGQSW--NDMPCDAVFPYiCKM 137

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 62.00 E-value: 4.11e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  865 CPKGWLYFNYKCFLVTipkdpRELKTWTGAQEFCVA--KGGTLVSIKSELEQAFIT---MNLFGQTTNVWIGLQSTNHE- 938
Cdd:cd03594     1 CPKGWLPYKGNCYGYF-----RQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIAsliSSYQKAYQPVWIGLHDPQQSr 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915809  939 --KWVNGKPLVYSNWSPSDIINIPSYnttefqkhiplCALMSSNPNFHftgKWYFDDCGKEgYGFVCE 1004
Cdd:cd03594    76 gwEWSDGSKLDYRSWDRNPPYARGGY-----------CAELSRSTGFL---KWNDANCEER-NPFICK 128

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 60.87 E-value: 1.02e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  865 CPKGwLYFNYKCFLVTipkdpRELKTWTGAQEFCVAKGGTLVSIKSELEQAFIT---MNLFGQTTNVWIGLQSTNHE-KW 940
Cdd:cd03596     1 CLKG-TKIHKKCYLVS-----EETKHYHEASEDCIARGGTLATPRDSDENDALRdyvKASVPGNWEVWLGINDMVAEgKW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915809  941 V--NGKPLVYSNWSpSDIINIPSYNTTEFqkhiplCALMSSNPNfhftGKWYFDDCGKEGYgFVCE 1004
Cdd:cd03596    75 VdvNGSPISYFNWE-REITAQPDGGKREN------CVALSSSAQ----GKWFDEDCRREKP-YVCE 128

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 60.40 E-value: 1.08e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  140 CDATWQRNGSSriCYQFNLlSSLSWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVvKEVWIGLNQLDEKAGWQWSDG 219
Cdd:cd03590     1 CPTNWKSFQSS--CYFFST-EKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGN-RSYWIGLSDEETEGEWKWVDG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915809  220 TPL--SYLNWSQ-EITPGPFVEHHCGTLEVVSAAWRSRDCESTLPYICKR 266
Cdd:cd03590    77 TPLnsSKTFWHPgEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 60.45 E-value: 1.35e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  572 CYMDWESATGlaSCFKVFHSEKvlmkrSWREAEAFCEEFG-----AHLASFAHIEEENFVNELLHSKFNWTQERQFWIGF 646
Cdd:cd03589     1 CPTFWTAFGG--YCYRFFGDRL-----TWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPDTPYGLWIGL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915809  647 NRRNplNAGSWAWSDGSPV-----VSSFLDNAYFEEDaknCAVYKANKTLLPS----NCASKHEWICRI 706
Cdd:cd03589    74 HDRT--SEGPFEWTDGSPVdftkwAGGQPDNYGGNED---CVQMWRRGDAGQSwndmPCDAVFPYICKM 137

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 58.94 E-value: 4.39e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  163 SWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVV---KEVWIGLNQLDEKAGWQWSDGTPLSYLNWSQEITPGPfveh 239
Cdd:cd03596    20 HYHEASEDCIARGGTLATPRDSDENDALRDYVKASVpgnWEVWLGINDMVAEGKWVDVNGSPISYFNWEREITAQP---- 95

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568915809  240 HCGTLE---VVSAA----WRSRDCESTLPYIC 264
Cdd:cd03596    96 DGGKREncvALSSSaqgkWFDEDCRREKPYVC 127

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 58.74 E-value: 5.16e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1161 WIKFKGNCYSFSTvlDSRSFEDAHEFCKSEGSNLLAIRDAAENSFLLEEllafGSSVQMVWLNAQFDNNNktLRWFDGTP 1240
Cdd:cd03588     5 WDKFQGHCYRHFP--DRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN----AQDYQWIGLNDRTIEGD--FRWSDGHP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568915809 1241 TEQSNWGLRKPDMDHLKPHPCVVLRIPE-GIWHFTPCEDKKGFICKM 1286
Cdd:cd03588    77 LQFENWRPNQPDNFFATGEDCVVMIWHEeGEWNDVPCNYHLPFTCKK 123

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 60.51 E-value: 6.79e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  854 EKEKPPTQPGTCPKGWLYFNYKCFLVTipkdpRELKTWTGAQEFCVAKGGTLVSIKSELEQAFitMNLFGQTTNVWIGL- 932
Cdd:PHA02642   77 DTQEPTIKYVTCPKGWIGFGYKCFYFS-----EDSKNWTFGNTFCTSLGATLVKVETEEELNF--LKRYKDSSDHWIGLn 149

                          90
                  ....*....|
gi 568915809  933 -QSTNHE-KW 940
Cdd:PHA02642  150 rESSNHPwKW 159

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 57.38 E-value: 9.30e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  161 SLSWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVVKEVWIGLnqLDEKAGWQWSDGTPLSYLNWSqeiTPGPFVEHH 240
Cdd:cd03602     9 SKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGL--YRDVDSWRWSDGSESSFRNWN---TFQPFGQGD 83

                          90       100
                  ....*....|....*....|....
gi 568915809  241 CGTLEvVSAAWRSRDCESTLPYIC 264
Cdd:cd03602    84 CATMY-SSGRWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 57.77 E-value: 1.10e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  425 CPAGWERHGRFCYKIDTVLRSFEEASS---GYYCSPALLTITSRFEQAFITSLISSVAEKDSYFWIALQDQNNTGEYTWK 501
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELfcqKYGPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRGWEWS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568915809  502 tvgQREPVQYTYWNTRQPSNRGG-CVVVRGGSSLGRWEVKDCSDFKAMsLCK 552
Cdd:cd03594    81 ---DGSKLDYRSWDRNPPYARGGyCAELSRSTGFLKWNDANCEERNPF-ICK 128

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 56.93 E-value: 1.73e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  288 CDPDWTPFNRKCYKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRDENAseTWIGLSSNKIPVSFEWSSGSS 367
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS--YWIGLSDEETEGEWKWVDGTP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568915809  368 VI--FTNWYPLEPRILPNRRQLCVSAEESDGRWKVKDCKERLFYICKK 413
Cdd:cd03590    79 LNssKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 56.28 E-value: 2.62e-09

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915809  160 SSLSWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVvKEVWIGLNQLDEKAGWQWSDGTPLSYLNWSQEITPGPF 236
Cdd:cd03603     8 GGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY-GASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNNG 83

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 56.19 E-value: 3.29e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1161 WIKFKGNCYSFSTvlDSRSFEDAHEFCKSEGSNLLAIRDAAENSFLLEELLAFGSsvqmvWLNAQFDNNNKTLRWFDGTP 1240
Cdd:cd03593     5 WICYGNKCYYFSM--EKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY-----WIGLSREKSEKPWKWIDGSP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568915809 1241 TeqSNWGLRKPDMDHlkpHPCVVLRiPEGIwHFTPCEDKKGFICK 1285
Cdd:cd03593    78 L--NNLFNIRGSTKS---GNCAYLS-STGI-YSEDCSTKKRWICE 115

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 56.21 E-value: 5.11e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1161 WIKFKGNCYSFSTvlDSRSFEDAHEFCKSEGSN-----LLAIRDAAENSFLLE--ELLAFGSSVQMVWLNAQFDNNNKTL 1233
Cdd:cd03589     5 WTAFGGYCYRFFG--DRLTWEEAELRCRSFSIPgliahLVSIHSQEENDFVYDlfESSRGPDTPYGLWIGLHDRTSEGPF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568915809 1234 RWFDGTPTEQSNWGLRKPDmDHLKPHPCVVLR---IPEGIWHFTPCEDKKGFICKM 1286
Cdd:cd03589    83 EWTDGSPVDFTKWAGGQPD-NYGGNEDCVQMWrrgDAGQSWNDMPCDAVFPYICKM 137

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 55.00 E-value: 8.78e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  572 CYMDWESATGlaSCFkvFHSEKvlmKRSWREAEAFCEEFGAHLASFAHIEEENFVNELLHSKFNwtqerqFWIGFNRRNp 651
Cdd:cd03590     1 CPTNWKSFQS--SCY--FFSTE---KKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS------YWIGLSDEE- 66

                          90
                  ....*....|....*...
gi 568915809  652 lNAGSWAWSDGSPVVSSF 669
Cdd:cd03590    67 -TEGEWKWVDGTPLNSSK 83

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 54.23 E-value: 1.51e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  724 WLFYQNAEYLFHTHPAEWATFEFVCGWLRSDFLTIYSAQEQEFihskIKGLTKYGVKWWIGLEEGGARDQIQWSNGSPVI 803
Cdd:cd03590     5 WKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEF----ISKILSGNRSYWIGLSDEETEGEWKWVDGTPLN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568915809  804 --FQNWDKGREERVDSQRKRCVFISSITGLWGTENCSVPLPSICKR 847
Cdd:cd03590    81 ssKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 52.43 E-value: 6.07e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915809 1031 RTYKIIRGNMTWYAAGKSCRMHRAELASIPDAFHQAFLTVLLSRLGHThWIGLSTTDNGQTFDWSDGTKSPFTYWKDEE 1109
Cdd:cd03603     1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGAS-WIGASDAATEGTWKWSDGEESTYTNWGSGE 78

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 52.75 E-value: 7.18e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1027 EYGNRTYKIIRGNMTWYAAGKSCRM-----HRAELASIPDAFHQAFLTVLL--SRLGHT---HWIGLSTTDNGQTFDWSD 1096
Cdd:cd03589     7 AFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFesSRGPDTpygLWIGLHDRTSEGPFEWTD 86

                          90
                  ....*....|
gi 568915809 1097 GTKSPFTYWK 1106
Cdd:cd03589    87 GSPVDFTKWA 96

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 51.97 E-value: 1.45e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  865 CPKGWLYFNYKCFlvtipkdpR---ELKTWTGAQEFCV-----AKGGTLVSIKSELEQAFITmNLF------GQTTNVWI 930
Cdd:cd03589     1 CPTFWTAFGGYCY--------RffgDRLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFVY-DLFessrgpDTPYGLWI 71

                          90       100
                  ....*....|....*....|....*..
gi 568915809  931 GLQSTNHE---KWVNGKPLVYSNWSPS 954
Cdd:cd03589    72 GLHDRTSEgpfEWTDGSPVDFTKWAGG 98

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 51.42 E-value: 1.52e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  572 CYMDWESATGlaSCFKVFHSekvlmKRSWREAEAFCEEFGAHLASFAHIEEENFVNellhskfNWTQERQfWIGFNRRnp 651
Cdd:cd03588     1 CEEGWDKFQG--HCYRHFPD-----RETWEDAERRCREQQGHLSSIVTPEEQEFVN-------NNAQDYQ-WIGLNDR-- 63

                          90
                  ....*....|....
gi 568915809  652 LNAGSWAWSDGSPV 665
Cdd:cd03588    64 TIEGDFRWSDGHPL 77

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 51.97 E-value: 1.57e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  724 WLFYQNAEYLFHTHPAEWATFEFVC-----GWLRSDFLTIYSAQEQEFIHSKIKGLTK----YGVkwWIGLEEGGARDQI 794
Cdd:cd03589     5 WTAFGGYCYRFFGDRLTWEEAELRCrsfsiPGLIAHLVSIHSQEENDFVYDLFESSRGpdtpYGL--WIGLHDRTSEGPF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568915809  795 QWSNGSPVIFQNWDkGREERVDSQRKRCVFI---SSITGLWGTENCSVPLPSICK 846
Cdd:cd03589    83 EWTDGSPVDFTKWA-GGQPDNYGGNEDCVQMwrrGDAGQSWNDMPCDAVFPYICK 136

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 51.14 E-value: 1.62e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  886 RELKTWTGAQEFCVAKGGTLVSIKSELEQAFItMNLFGQ-TTNVWIG---LQSTNHEKWVNGKPLVYSNWSPSDiiniPS 961
Cdd:cd03591     8 GEEKNFDDAQKLCSEAGGTLAMPRNAAENAAI-ASYVKKgNTYAFIGitdLETEGQFVYLDGGPLTYTNWKPGE----PN 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568915809  962 -YNTTEfqkhipLCALMSSNpnfhftGKWYFDDCGKEGYgFVCE 1004
Cdd:cd03591    83 nAGGGE------DCVEMYTS------GKWNDVACNLTRL-FVCE 113

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 51.04 E-value: 1.95e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  724 WLFYQNAEYLFHTHPAEWATFEFVCGWLRSDFLTIYSAQEQEFIHSKIKGLTkygvkwWIGLEEGGARDQIQWSNGSPVI 803
Cdd:cd03588     5 WDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ------WIGLNDRTIEGDFRWSDGHPLQ 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568915809  804 FQNWDKGREERVDSQRKRC-VFISSITGLWGTENCSVPLPSICKR 847
Cdd:cd03588    79 FENWRPNQPDNFFATGEDCvVMIWHEEGEWNDVPCNYHLPFTCKK 123

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 51.59 E-value: 2.13e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  153 CYQ-FNLlsSLSWNQAHSSCLMQG-----GALLSIADEDEEDFIRKHLSKVVK-----EVWIGLNQLDEKAGWQWSDGTP 221
Cdd:cd03589    12 CYRfFGD--RLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGpdtpyGLWIGLHDRTSEGPFEWTDGSP 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915809  222 LSYLNW--SQeitPGPFVEHH-CGTLEVVSAA---WRSRDCESTLPYICK 265
Cdd:cd03589    90 VDFTKWagGQ---PDNYGGNEdCVQMWRRGDAgqsWNDMPCDAVFPYICK 136

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 50.06 E-value: 2.80e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  300 YKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEfLVSLLRDENASETWIGLSSNKIPVSfeWSSGSSVIFTNWYPLEPR 379
Cdd:cd03602     3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNA-LLSNLSRVSNSAAWIGLYRDVDSWR--WSDGSESSFRNWNTFQPF 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568915809  380 IlpnrRQLCVsAEESDGRWKVKDCKERLFYIC 411
Cdd:cd03602    80 G----QGDCA-TMYSSGRWYAALCSALKPFIC 106

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 50.50 E-value: 3.25e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915809 1179 SFEDAHEFCKSEGSNLLAIRDAAENSFLLEELLAFGSSvqmvWLNAQFDNNNKTLRWFDGTPTEQSNWG 1247
Cdd:cd03603    11 TWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGAS----WIGASDAATEGTWKWSDGEESTYTNWG 75

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 50.50 E-value: 3.34e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915809  459 LLTITSRFEQAFITSLISSVAEkdsyFWIALQDQNNTGEYTWKTvgqREPVQYTYWNTRQPSNRGG 524
Cdd:cd03603    26 LVTINSAEENDWLLSNFGGYGA----SWIGASDAATEGTWKWSD---GEESTYTNWGSGEPHNNGG 84

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 50.07 E-value: 3.91e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1169 YSFSTVLdsRSFEDAHEFCKSEGSNLLAIRDAAENSFLLEELLAFGSSvqMVWLNAqfDNNNKTLRWFD--GTPTEQSNW 1246
Cdd:cd03592     3 YHYSTEK--MTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLG--YYWIDG--NDINNEGTWVDtdKKELEYKNW 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568915809 1247 GLRKPdmDHLKPHPCV-VLRIPEGIWHFTPCEDKKGFIC 1284
Cdd:cd03592    77 APGEP--NNGRNENCLeIYIKDNGKWNDEPCSKKKSAIC 113

Lectin C-type domain; This family includes both long and short form C-type

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 49.40 E-value: 5.75e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809   445 SFEEASSgyYCSPA---LLTITSRFEQAFITSLissVAEKDSYFWIALQDQNNTGEYTWkTVGqrEPVQYTYWNTRQPSN 521
Cdd:pfam00059    3 TWDEARE--ACRKLgghLVSINSAEELDFLSST---LKKSNKYFWIGLTDRKNEGTWKW-VDG--SPVNYTNWAPEPNNN 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 568915809   522 RGG--CVVVRggSSLGRWEVKDCSDfKAMSLCKT 553
Cdd:pfam00059   75 GENedCVELS--SSSGKWNDENCNS-KNPFVCEK 105

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 49.50 E-value: 8.10e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  140 CDATWQRNGSSriCYQFnLLSSLSWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVVkevWIGLNQLDEKAGWQWSDG 219
Cdd:cd03588     1 CEEGWDKFQGH--CYRH-FPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEGDFRWSDG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568915809  220 TPLSYLNWSQEITPGPFVEhhcGTLEVV-----SAAWRSRDCESTLPYICKR 266
Cdd:cd03588    75 HPLQFENWRPNQPDNFFAT---GEDCVVmiwheEGEWNDVPCNYHLPFTCKK 123

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 49.50 E-value: 1.15e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  146 RNGSSRICYQF----NLLSSLSWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVVK---EVWIGLNQLDEKAG----- 213
Cdd:cd03595     5 RRGTEKPCYKIayfqDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRAsdgDFWIGLRRSSQYNVtssac 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568915809  214 ---WQWSDGTPLSYLNWSqeitpgpFVEHHCGTLEVV------SAA----------WRSRDCESTLPYICK 265
Cdd:cd03595    85 sslYYWLDGSISTFRNWY-------VDEPSCGSEVCVvmyhqpSAPagqggpylfqWNDDNCNMKNNFICK 148

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 48.06 E-value: 1.96e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  165 NQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVVKEVWIGLNQLdEKAG-WQWSDGTPLSYLNWSQEITPGPFVEHHCGT 243
Cdd:cd03591    14 DDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDL-ETEGqFVYLDGGPLTYTNWKPGEPNNAGGGEDCVE 92

                          90       100
                  ....*....|....*....|.
gi 568915809  244 LeVVSAAWRSRDCESTLPYIC 264
Cdd:cd03591    93 M-YTSGKWNDVACNLTRLFVC 112

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 48.10 E-value: 1.99e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  724 WLFYQNAEYLFHTHPAEWATFEFVCGWLRSDFLTIYSAQEQEFIHSKIKGLTkygvkWWIGLEEGGARDQIQWSNGSPvi 803
Cdd:cd03593     5 WICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS-----YWIGLSREKSEKPWKWIDGSP-- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568915809  804 fqnWDKGREERVDSQRKRCVFISSiTGLWgTENCSVPLPSICKR 847
Cdd:cd03593    78 ---LNNLFNIRGSTKSGNCAYLSS-TGIY-SEDCSTKKRWICEK 116

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 48.22 E-value: 2.06e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  298 KCYKLKKDRKSWLGALHSCQS-NDSVLMDVASLAEVEFLVSLLRDENASETWIG--LSSNKIPVSFEWSSGSSVIFTNWY 374
Cdd:cd03598     2 RCYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYWA 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568915809  375 PLEPRilpNRRQLCVSAEESDGRWKVKDCKERLFYIC 411
Cdd:cd03598    82 PGQPG---NRRGHCVELCTRGGHWRRAHCKLRRPFIC 115

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 48.73 E-value: 2.48e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  584 SCFKVFHSEKVLMKRSWREAEAFCEEFGAHLASFAHIEE----ENFVNELLHSkfnwtqERQFWIGFNRRNPLNAGS--- 656
Cdd:cd03595    11 PCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEqkliERFIQTLRAS------DGDFWIGLRRSSQYNVTSsac 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915809  657 ---WAWSDGSPvvsSFLDNAYFEEDA---KNCAVYKANKTLLPS------------NCASKHEWICR 705
Cdd:cd03595    85 sslYYWLDGSI---STFRNWYVDEPScgsEVCVVMYHQPSAPAGqggpylfqwnddNCNMKNNFICK 148

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 47.29 E-value: 3.44e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  298 KCYKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRDENaSETWIGLSSNKIPVSFEWSSGSSVIFTNWYPLE 377
Cdd:cd03591     2 KIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGN-TYAFIGITDLETEGQFVYLDGGPLTYTNWKPGE 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568915809  378 PRilpNRR--QLCVsAEESDGRWKVKDCKERLFYIC 411
Cdd:cd03591    81 PN---NAGggEDCV-EMYTSGKWNDVACNLTRLFVC 112

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 47.38 E-value: 4.39e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  297 RKCYKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRDE--NASETWIGLSSNKIPVSFEWSSGSSVIFTNWY 374
Cdd:cd03596     9 KKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASvpGNWEVWLGINDMVAEGKWVDVNGSPISYFNWE 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568915809  375 PLEPRIlPN--RRQLCVS-AEESDGRWKVKDCKERLFYIC 411
Cdd:cd03596    89 REITAQ-PDggKRENCVAlSSSAQGKWFDEDCRREKPYVC 127

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 46.60 E-value: 5.02e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  887 ELKTWTGAQEFCVAKGGTLVSIKSELEQAFITMNLFGQTTNVWIGL-QSTNHEKWVNGKPLVYSNWSPsdiinipsynTT 965
Cdd:cd03602     8 ESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLyRDVDSWRWSDGSESSFRNWNT----------FQ 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568915809  966 EFQKHipLCALMSSNpnfhftGKWYFDDCGKEGYgFVC 1003
Cdd:cd03602    78 PFGQG--DCATMYSS------GRWYAALCSALKP-FIC 106

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 46.98 E-value: 5.60e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1026 LEYGNRTYKIIRGNMTWYAAGKSCRMHR--AELASIPDAFHQAFLTVLLSRLGHTH---WIGLSTTDNGQTFDWSDGTKS 1100
Cdd:cd03594     6 LPYKGNCYGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSYQKAYqpvWIGLHDPQQSRGWEWSDGSKL 85

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568915809 1101 PFTYW-KDEESAFLGDCA-FADTNG--RWHSTACES 1132
Cdd:cd03594    86 DYRSWdRNPPYARGGYCAeLSRSTGflKWNDANCEE 121

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 46.98 E-value: 6.60e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  724 WLFYQNAEYLFHTHPAEWATFEFVCGWLRS--DFLTIYSAQEQEFIHSKIKGLTKYGVKWWIGLEEGGARDQIQWSNGSP 801
Cdd:cd03594     5 WLPYKGNCYGYFRQPLSWSDAELFCQKYGPgaHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRGWEWSDGSK 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568915809  802 VIFQNWDKGREERvdsQRKRCVFISSITG--LWGTENCSVPLPSICK 846
Cdd:cd03594    85 LDYRSWDRNPPYA---RGGYCAELSRSTGflKWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 46.68 E-value: 7.20e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1030 NRTYKIIRGNMTWYAAGKSCR-MHRAELASIPD-AFHQAfLTVLLSRLGHTH-WIGLSTTDNG--QTFDWSDGTKSPFTY 1104
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRrCYRGNLASIHSfAFNYR-VQRLVSTLNQAQvWIGGIITGKGrcRRFSWVDGSVWNYAY 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568915809 1105 W-KDEESAFLGDC-AFADTNGRWHSTACeSFLQGAIC 1139
Cdd:cd03598    80 WaPGQPGNRRGHCvELCTRGGHWRRAHC-KLRRPFIC 115

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 46.42 E-value: 9.81e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  865 CPKGWLYFNYKCFlvtipKDPRELKTWTGAQEFCVAKGGTLVSIKSELEQAFITMNlfGQTTNvWIGLQSTNHE---KWV 941
Cdd:cd03588     1 CEEGWDKFQGHCY-----RHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN--AQDYQ-WIGLNDRTIEgdfRWS 72

                          90
                  ....*....|..
gi 568915809  942 NGKPLVYSNWSP 953
Cdd:cd03588    73 DGHPLQFENWRP 84

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 49.70 E-value: 1.61e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809   287 HCDPDWT--PFNRKCYKLKKDRKSWLGALHSCQS-NDSVLMDVASLAEVEFLVSLLRDENASETWIGLSS-NKIPVS-FE 361
Cdd:TIGR00864  317 HCPKDGEifEENGHCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSLDRGVWIGFSDvNGAEKGpAH 396

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915809   362 WSSGSSV-IFTNWYPLEPRilPNRRQLCVSAEESdGRWKVKDCKERLFYICKKAGQVPADEQS----GCPAGWERH 432
Cdd:TIGR00864  397 QGEAFEAeECEEGLAGEPH--PARAEHCVRLDPR-GQCNSDLCNAPHAYVCELNPGGPVPDAEnfamGAASFDLHG 469

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 45.06 E-value: 1.83e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  748 CGWLRSDFLTIYSAQEQEFIHSKIKGltkYGVKWWIGLEEGgaRDQIQWSNGSPVIFQNWDKGReervDSQRKRCVFISS 827
Cdd:cd03602    19 CRENYTDLATVQNQEDNALLSNLSRV---SNSAAWIGLYRD--VDSWRWSDGSESSFRNWNTFQ----PFGQGDCATMYS 89

                          90
                  ....*....|....*...
gi 568915809  828 iTGLWGTENCSVPLPSIC 845
Cdd:cd03602    90 -SGRWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 44.67 E-value: 2.73e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915809  886 RELKTWTGAQEFCVAKGGTLVSIKSELEQAFItmNLFGQTTNV---WIGLQSTNHE-KWV--NGKPLVYSNWSP 953
Cdd:cd03592     7 TEKMTFNEAVKYCKSRGTDLVAIQNAEENALL--NGFALKYNLgyyWIDGNDINNEgTWVdtDKKELEYKNWAP 78

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 44.88 E-value: 4.41e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1164 FKGNCYSFSTVLDSR---SFEDAHEFCKSEGSNLLAIRDAAENSFLLEELLAFGSSVQMVWL--------NAQFDNNNKT 1232
Cdd:cd03595     8 TEKPCYKIAYFQDSRrrlNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWIglrrssqyNVTSSACSSL 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915809 1233 LRWFDGTPTEQSNWGLRKPDMDHlkpHPCVVL----RIPEGI-------WHFTPCEDKKGFICK 1285
Cdd:cd03595    88 YYWLDGSISTFRNWYVDEPSCGS---EVCVVMyhqpSAPAGQggpylfqWNDDNCNMKNNFICK 148

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 44.73 E-value: 5.26e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  584 SCFKVFHSekvlmKRSWREAEAFCEEFGAHLASFAHIEEENFVNELLHS--KFNWTQERQFWIGFNRR--------NPLN 653
Cdd:cd03600     5 ACYTLHPQ-----KLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAgpGRHGRGSLRLWIGLQREprqcsdpsLPLR 79


                  ....*...
gi 568915809  654 AGSWAWSD 661
Cdd:cd03600    80 GFSWVTGD 87

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 48.15 E-value: 5.50e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809   148 GSSRiCYQFnLLSSLSWNQAHSSCLMQGGALLSIADED--EEDFIRKHLSKVVKEVWIGLNQLD--EKAGWQWSDGTPL- 222
Cdd:TIGR00864  327 ENGH-CFQI-VPEEAAWLDAQEQCLARAGAALAIVDNDalQNFLARKVTHSLDRGVWIGFSDVNgaEKGPAHQGEAFEAe 404

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568915809   223 SYLNWSQEiTPGPFVEHHCGTLEVVSaaWRSRD-CESTLPYICK 265
Cdd:TIGR00864  405 ECEEGLAG-EPHPARAEHCVRLDPRG--QCNSDlCNAPHAYVCE 445

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 43.44 E-value: 8.44e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1171 FSTVLDSRSFEDAHEFCKSEGSNLLAIRDAAENSfLLEELLAFGSSVQMVWLN-----AQFdnnnktlRWFDGTPTEQSN 1245
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENA-AIASYVKKGNTYAFIGITdleteGQF-------VYLDGGPLTYTN 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568915809 1246 WGLRKPDmDHLKPHPCVVLrIPEGIWHFTPCEDKKGFIC 1284
Cdd:cd03591    76 WKPGEPN-NAGGGEDCVEM-YTSGKWNDVACNLTRLFVC 112

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 42.82 E-value: 1.34e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  153 CYQFNLlSSLSWNQAHSSCL-MQGGALLSIADEDEEDFIRKHLSKV-VKEVWIGlNQLDEKAG---WQWSDGTPLSYLNW 227
Cdd:cd03598     3 CYRFVK-SPRTFRDAQVICRrCYRGNLASIHSFAFNYRVQRLVSTLnQAQVWIG-GIITGKGRcrrFSWVDGSVWNYAYW 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568915809  228 SQEiTPGPFVEHhCGTLEVVSAAWRSRDCESTLPYIC 264
Cdd:cd03598    81 APG-QPGNRRGH-CVELCTRGGHWRRAHCKLRRPFIC 115

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 42.80 E-value: 1.49e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  300 YKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRdeNASETWIGLSSNKIPVSFEWSSGSSVIFTNWYPLEPR 379
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFG--GYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 43.19 E-value: 1.76e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  299 CYKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLR------DENASETWIGL-------SSNKIPV-SFEW-S 363
Cdd:cd03600     6 CYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAagpgrhGRGSLRLWIGLqreprqcSDPSLPLrGFSWvT 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568915809  364 SGSSVIFTNWYPLEPRILPNRRqlCVSAEESDG-----RWKVKDCKERL-FYICK 412
Cdd:cd03600    86 GDQDTDFSNWLQEPAGTCTSPR--CVALSAAGStpdnlKWKDGPCSARAdGYLCK 138

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 42.68 E-value: 1.91e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1033 YKIIRGNMTWYAAGKSCRMHRAELASIPDAFHQAFLTVLLSRlGHTHWIGLSTTDNGQTFDWSDGTK--SPFTYWKDEE- 1109
Cdd:cd03590    13 YFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSG-NRSYWIGLSDEETEGEWKWVDGTPlnSSKTFWHPGEp 91

                          90       100
                  ....*....|....*....|....*.
gi 568915809 1110 --SAFLG-DCA-FADTNGRWHSTACE 1131
Cdd:cd03590    92 nnWGGGGeDCAeLVYDSGGWNDVPCN 117

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 43.95 E-value: 2.46e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  288 CDPDWTPFNRKCYKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVsllRDENASETWIGLSSNKIPVSFEWSSGSS 367
Cdd:PHA02642   88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLK---RYKDSSDHWIGLNRESSNHPWKWADNSN 164

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 43.57 E-value: 4.08e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  132 DPTSMKVFCDATWQrnGSSRICYQFNLlSSLSWNQAHSSCLMQGGALLSIADEDEEDFIRKHlsKVVKEVWIGLNQLDEK 211
Cdd:PHA02642   80 EPTIKYVTCPKGWI--GFGYKCFYFSE-DSKNWTFGNTFCTSLGATLVKVETEEELNFLKRY--KDSSDHWIGLNRESSN 154


                  ....*....
gi 568915809  212 AGWQWSDGT 220
Cdd:PHA02642  155 HPWKWADNS 163

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 41.79 E-value: 4.15e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1033 YKIIRGNMTWYAAGKSCRMHRAELASIPDAFHQAFltvlLSRLGHTH-WIGLSTTDNGQTFDWSDGTKSPFTYWKDEE-- 1109
Cdd:cd03588    13 YRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEF----VNNNAQDYqWIGLNDRTIEGDFRWSDGHPLQFENWRPNQpd 88

                          90       100
                  ....*....|....*....|....*
gi 568915809 1110 SAFLG--DCAFA--DTNGRWHSTAC 1130
Cdd:cd03588    89 NFFATgeDCVVMiwHEEGEWNDVPC 113

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 42.18 E-value: 4.64e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  422 QSGCPAGWERHgrfCYKI----DTVLR-SFEEASSGyyC---SPALLTITSRFEQAFITSLISSVAEKDSYFWIAL---Q 490
Cdd:cd03595     1 QRICRRGTEKP---CYKIayfqDSRRRlNFEEARQA--CredGGELLSIESENEQKLIERFIQTLRASDGDFWIGLrrsS 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915809  491 DQNNTG-----EYTWKtvgQREPVQYTYWNTRQPS-NRGGCVVV---------RGGSSLGRWEVKDCsDFKAMSLCK 552
Cdd:cd03595    76 QYNVTSsacssLYYWL---DGSISTFRNWYVDEPScGSEVCVVMyhqpsapagQGGPYLFQWNDDNC-NMKNNFICK 148

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 40.82 E-value: 4.88e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  459 LLTITSRFEQAFITSLISSvaeKDSYFWIALQDQNntgeYTWKTVGQrEPVQYTYWNTRQPSNRGGCVVVRggsSLGRWE 538
Cdd:cd03602    26 LATVQNQEDNALLSNLSRV---SNSAAWIGLYRDV----DSWRWSDG-SESSFRNWNTFQPFGQGDCATMY---SSGRWY 94


                  ....*...
gi 568915809  539 VKDCSDFK 546
Cdd:cd03602    95 AALCSALK 102

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 40.43 E-value: 8.00e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  598 RSWREAEAFCEEFGAHLASFAHIEEenfvNELLhSKFNWTQERQFWIGFNRRNplnaGSWAWSDGSPvvSSFLDNAYFEE 677
Cdd:cd03602    10 KTWSEAQQYCRENYTDLATVQNQED----NALL-SNLSRVSNSAAWIGLYRDV----DSWRWSDGSE--SSFRNWNTFQP 78

                          90       100
                  ....*....|....*....|....*...
gi 568915809  678 DAK-NCAVYKANKTLLPSNCASKHEWIC 704
Cdd:cd03602    79 FGQgDCATMYSSGRWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 40.44 E-value: 8.76e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1031 RTYKIIRGNMTWYAAGKSCRMHRAELASIPDAFHQAFL-TVLLSRLGHTHWIGLSttDNGQTFDWSDGTKSPFTY--WKD 1107
Cdd:cd03592     1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLnGFALKYNLGYYWIDGN--DINNEGTWVDTDKKELEYknWAP 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568915809 1108 EESAFLG--DC--AFADTNGRWHSTACESfLQGAICH 1140
Cdd:cd03592    79 GEPNNGRneNCleIYIKDNGKWNDEPCSK-KKSAICY 114

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 40.64 E-value: 9.14e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  425 CPAGWERHGRFCYKIDTVLRSFEEASSgyYCSPA---LLTITSRFEQAFITSLissvaeKDSYFWIALQDQNNTGEYTWK 501
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAER--RCREQqghLSSIVTPEEQEFVNNN------AQDYQWIGLNDRTIEGDFRWS 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568915809  502 tvgQREPVQYTYWNTRQPSN---RGGCVVVRGGSSLGRWEVKDCS 543
Cdd:cd03588    73 ---DGHPLQFENWRPNQPDNffaTGEDCVVMIWHEEGEWNDVPCN 114

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 40.49 E-value: 9.82e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568915809  599 SWREAEAFCEEFGAHLASFAHIEEenfvNELLHSKFNWTQErqFWIGFNRRNplNAGSWAWSDGSPVVSSF 669
Cdd:cd03603    11 TWEAAQTLAESLGGHLVTINSAEE----NDWLLSNFGGYGA--SWIGASDAA--TEGTWKWSDGEESTYTN 73

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 40.13 E-value: 1.16e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915809  779 VKWWIG--LEEGGARDQIQWSNGSPVIFQNWDKGREERvdsQRKRCVFISSITGLWGTENCSVPLPSIC 845
Cdd:cd03598    50 AQVWIGgiITGKGRCRRFSWVDGSVWNYAYWAPGQPGN---RRGHCVELCTRGGHWRRAHCKLRRPFIC 115

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 39.62 E-value: 1.92e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1028 YGNRTYKIIRGNMTWYAAGKSCRMHRAELASIPDafhQAFLTVLLSRLGH-THWIGLSTTDNGQTFDWSDGtkSPFTYW- 1105
Cdd:cd03593     8 YGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDD---EEELEFLQSQIGSsSYWIGLSREKSEKPWKWIDG--SPLNNLf 82

                          90       100
                  ....*....|....*....|....*..
gi 568915809 1106 KDEESAFLGDCAFADtNGRWHSTACES 1132
Cdd:cd03593    83 NIRGSTKSGNCAYLS-STGIYSEDCST 108

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

Pssm-ID: 153068 Cd Length: 117 Bit Score: 39.36 E-value: 1.99e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809 1166 GNCYSFstVLDSRSFEDAHEFC-KSEGSNLLAIRDAAENSFLLEelLAFGSSVQMVWLNAQFDNN--NKTLRWFDGTPTE 1242
Cdd:cd03598     1 GRCYRF--VKSPRTFRDAQVICrRCYRGNLASIHSFAFNYRVQR--LVSTLNQAQVWIGGIITGKgrCRRFSWVDGSVWN 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568915809 1243 QSNWGLRKPDMDhlKPHpCVVLRIPEGIWHFTPCEDKKGFIC 1284
Cdd:cd03598    77 YAYWAPGQPGNR--RGH-CVELCTRGGHWRRAHCKLRRPFIC 115

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.

Pssm-ID: 153067 Cd Length: 129 Bit Score: 39.87 E-value: 2.14e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  288 CDPDWTPFNRKCYKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRDENASET----WIGLssNKIPVSFeWS 363
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMTKQkltpWVGL--RKINVSY-WC 77

                          90
                  ....*....|....*....
gi 568915809  364 SGSSVIFTN----WYPLEP 378
Cdd:cd03597    78 WEDMSPFTNttlqWLPGEP 96

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 39.28 E-value: 2.17e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  162 LSWNQAHSSCLMQGGALLSIADEDEEDFIRKHLSKVVKEV-WIGLNQLDEKAGWQWSDGTPLSYLNWSQEiTPGPFVEHH 240
Cdd:cd03592    10 MTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYyWIDGNDINNEGTWVDTDKKELEYKNWAPG-EPNNGRNEN 88

                          90       100
                  ....*....|....*....|....*..
gi 568915809  241 CGT-LEVVSAAWRSRDCESTLPYICKR 266
Cdd:cd03592    89 CLEiYIKDNGKWNDEPCSKKKSAICYT 115

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 39.33 E-value: 2.63e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568915809  756 LTIYSAQEQEFIHSKIKGLTKYgvkwWIGLEEGGARDQIQWSNGSPVIFQNWDKG 810
Cdd:cd03603    27 VTINSAEENDWLLSNFGGYGAS----WIGASDAATEGTWKWSDGEESTYTNWGSG 77

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

Pssm-ID: 153066 Cd Length: 129 Bit Score: 38.91 E-value: 3.56e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  760 SAQEQEFIHSKIKGLTKYGVKWWIGLEEGGARDQIQWSNGSPVIFQNWDKGREERVD-SQRKRCVFISSIT-GLWGTENC 837
Cdd:cd03596    40 DSDENDALRDYVKASVPGNWEVWLGINDMVAEGKWVDVNGSPISYFNWEREITAQPDgGKRENCVALSSSAqGKWFDEDC 119


                  ....*...
gi 568915809  838 SVPLPSIC 845
Cdd:cd03596   120 RREKPYVC 127

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 39.49 E-value: 4.00e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  295 FNRKCYKLK-----KDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRDENASET--WIGL--------SSNKIPVS 359
Cdd:cd03595     8 TEKPCYKIAyfqdsRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGdfWIGLrrssqynvTSSACSSL 87

                          90
                  ....*....|....*....
gi 568915809  360 FEWSSGSSVIFTNWYPLEP 378
Cdd:cd03595    88 YYWLDGSISTFRNWYVDEP 106

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 40.10 E-value: 4.66e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  598 RSWREAEAFCEEFGAHLASFAHIEEENFVNEllhskfnWTQERQFWIGFNRRNplNAGSWAWSDGSPVVSSFLDNAYFEe 677
Cdd:PHA02642  107 KNWTFGNTFCTSLGATLVKVETEEELNFLKR-------YKDSSDHWIGLNRES--SNHPWKWADNSNYNASFVITGTGE- 176

                          90       100
                  ....*....|....*....|....*..
gi 568915809  678 daknCAvYKANKTLLPSNCASKHEWIC 704
Cdd:PHA02642  177 ----CA-YLNDIRISSSRVYANRKWIC 198

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 38.13 E-value: 6.30e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  300 YKLKKDRKSWLGALHSCQSNDSVLMDVASLAEVEFLVSLLRDENASETWIGLssNKIPVSFEW--SSGSSVIFTNWYPLE 377
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYYWIDG--NDINNEGTWvdTDKKELEYKNWAPGE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568915809  378 PRilPNRRQLCV-SAEESDGRWKVKDCKERLFYIC 411
Cdd:cd03592    81 PN--NGRNENCLeIYIKDNGKWNDEPCSKKKSAIC 113

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 38.72 E-value: 6.49e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568915809  754 DFLTIYSAQEQEFIHSKIKGLTKYGVKWWIGL--------EEGGARDQIQWSNGSPVIFQNW 807
Cdd:cd03595    40 ELLSIESENEQKLIERFIQTLRASDGDFWIGLrrssqynvTSSACSSLYYWLDGSISTFRNW 101

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 38.33 E-value: 8.46e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915809  876 CFLVTIPKDPRELKTWTGAQEFCVAKGGTLVSIKSELEQAFI---TMNLFGQTTNVWIGL------QSTNHE-----KWV 941
Cdd:cd03595    12 CYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIerfIQTLRASDGDFWIGLrrssqyNVTSSAcsslyYWL 91

                          90
                  ....*....|
gi 568915809  942 NGKPLVYSNW 951
Cdd:cd03595    92 DGSISTFRNW 101

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 37.70 E-value: 8.59e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915809  425 CPAGWERHGRFCYKIDTVLRSFEEasSGYYCS---PALLTITSRFEQAFITSLISSvaekdSYFWIALQDQNNTGEYTW 500
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNE--SKEACSsknSSLLKIDDEEELEFLQSQIGS-----SSYWIGLSREKSEKPWKW 72