NCBI Conserved Domain Search

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other

Pssm-ID: 409552 Cd Length: 114 Bit Score: 149.91 E-value: 1.53e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 145 VSITTPEQTIEKDQGETVHLPCMFTFISKDQGPLNIEWLRLSgpnNEAMDHVVILYSADKIHDDVYPDLKGRVYFTSNDi 224
Cdd:cd20960    1 LLITSAQTEIKKVAGENVTLPCHHQLGLEDQGTLDIEWLLLP---SDKVEKVVITYSGDRVYNHYYPALKGRVAFTSND- 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 124249111 225 KSGDASINITNVQLSDAGTYQCKVKTYPGTVNRNLQL 261
Cdd:cd20960   77 LSGDASLNISNLKLSDTGTYQCKVKKAPGYAWSKITL 113

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other

Pssm-ID: 409552 Cd Length: 114 Bit Score: 142.59 E-value: 1.03e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  20 VSITTPEQTIQEVQGETVHLPCMFTLSPEDQGPLDIEWLRLSgpnNEAMDHVIILYAVDKIYSDFYQDMRGRVNFTSNGI 99
Cdd:cd20960    1 LLITSAQTEIKKVAGENVTLPCHHQLGLEDQGTLDIEWLLLP---SDKVEKVVITYSGDRVYNHYYPALKGRVAFTSNDL 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 124249111 100 tSGEASIKIRDVQPADSGTYLCKVKTAPGVAKTTVQLT 137
Cdd:cd20960   78 -SGDASLNISNLKLSDTGTYQCKVKKAPGYAWSKITLI 114

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other

Pssm-ID: 409552 Cd Length: 114 Bit Score: 131.03 E-value: 2.07e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 270 VSITTPEQTIQKARGETVHLPCTFTLSPEDHGPLFIDWMQLTgpqNEVVNRMFIVYLADKIYDNFYQDMKGRVQFTSNDi 349
Cdd:cd20960    1 LLITSAQTEIKKVAGENVTLPCHHQLGLEDQGTLDIEWLLLP---SDKVEKVVITYSGDRVYNHYYPALKGRVAFTSND- 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 124249111 350 RSGEASINITDARLSDAGTYQCGVSHAFGTAKGTIQLT 387
Cdd:cd20960   77 LSGDASLNISNLKLSDTGTYQCKVKKAPGYAWSKITLI 114

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.

Pssm-ID: 462230 Cd Length: 109 Bit Score: 69.02 E-value: 1.69e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111   24 TPEQTIQEVQGETVHLPCMFTLSpEDQGPLDIEWLRLSGPNNEamDHVIILYavdKIYSDFYQDMrGRVNFTSNgITSGE 103
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSS-MSEASTSVYWYRQPPGKGP--TFLIAYY---SNGSEEGVKK-GRFSGRGD-PSNGD 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 124249111  104 ASIKIRDVQPADSGTYLCKVKTAP-GVAKTTVQLTVV 139
Cdd:pfam07686  73 GSLTIQNLTLSDSGTYTCAVIPSGeGVFGKGTRLTVL 109

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.

Pssm-ID: 462230 Cd Length: 109 Bit Score: 66.71 E-value: 1.05e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  274 TPEQTIQKARGETVHLPCTFTLSpEDHGPLFIDWMQltgpQNEVVNRMFIVYLADKIYDNFYQdmKGRVQFTSnDIRSGE 353
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSS-MSEASTSVYWYR----QPPGKGPTFLIAYYSNGSEEGVK--KGRFSGRG-DPSNGD 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 124249111  354 ASINITDARLSDAGTYQCGV-SHAFGTAKGTIQLTVV 389
Cdd:pfam07686  73 GSLTIQNLTLSDSGTYTCAViPSGEGVFGKGTRLTVL 109

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.

Pssm-ID: 462230 Cd Length: 109 Bit Score: 64.40 E-value: 8.31e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  149 TPEQTIEKDQGETVHLPCMFTfISKDQGPLNIEWLRLSGPNNEamdHVVILYSADKIHDDVYpdlKGRVYFTSnDIKSGD 228
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYS-SSMSEASTSVYWYRQPPGKGP---TFLIAYYSNGSEEGVK---KGRFSGRG-DPSNGD 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 124249111  229 ASINITNVQLSDAGTYQCKV-KTYPGTVNRNLQLAVT 264
Cdd:pfam07686  73 GSLTIQNLTLSDSGTYTCAViPSGEGVFGKGTRLTVL 109

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).

Pssm-ID: 409378 Cd Length: 114 Bit Score: 59.51 E-value: 4.91e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  21 SITTPEQTIQEVQGETVHLPCMftLSPE-DQGPLDIEWLRlSGPNNeamdhVIILY--AVDKiYSDFYQDMRGRVNFTSN 97
Cdd:cd05713    2 SVIGPTEPILALVGEDAELPCH--LSPKmSAEHMEVRWFR-SQFSP-----VVHLYrdGQDQ-EEEQMPEYRGRTELLKD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 124249111  98 GITSGEASIKIRDVQPADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:cd05713   73 AIAEGSVALRIHNVRPSDEGQYTCFFRSGSFYEEATLELKV 113

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.

Pssm-ID: 409380 Cd Length: 117 Bit Score: 58.59 E-value: 1.12e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 145 VSITTPEqTIEKDQGETVHLPCMFTFISKDQGPLNIEWLrlSGPNNEAMDHVVILYSADKIHDDVYPDLKGRVYFTSNDI 224
Cdd:cd05715    1 MEVYTPR-ELNVLNGSDVRLTCTFTSCYTVGDAFSVTWT--YQPEGGNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPS 77

                         90       100
                 ....*....|....*....|....*...
gi 124249111 225 KSgDASINITNVQLSDAGTYQCKVKTYP 252
Cdd:cd05715   78 KK-DASIVISNLQFSDNGTYTCDVKNPP 104

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409379 Cd Length: 123 Bit Score: 57.61 E-value: 2.91e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 279 IQKARGETVHLPCTFTLSPEDHGP----LFIDWMQLTGPQNEVVNRMFIVYLADKIYdnFYQDMKGRVQFTSNDIRSGEA 354
Cdd:cd05714    7 VFSHLGGNVTLPCKFYRDPTAFGSgihkIRIKWTKLTSDSGYLKEVDVLVAMGNVVY--HKKTYGGRVSVPLKPGSDSDA 84

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 124249111 355 SINITDARLSDAGTYQCGVSHAFGTAKGTIQLTVVG 390
Cdd:cd05714   85 SLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQG 120

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.

Pssm-ID: 409576 Cd Length: 110 Bit Score: 56.84 E-value: 3.66e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMFTFISKDQGpLNIEWLRlsgpnnEAMDHVV--ILYSADKIHDDvYPDLKGRVYFTSNDIKSGDASINITNV 236
Cdd:cd20984   12 GEDGILSCTFTPDIKLSD-IVIQWLK------EGDSGLVheFKEGKDELSRQ-SPMFRGRTSLFADQVHVGNASLRLKNV 83

                         90       100
                 ....*....|....*....|....*..
gi 124249111 237 QLSDAGTYQCKVKTYPGTVNRNLQLAV 263
Cdd:cd20984   84 QLTDAGTYLCIISNSKGTGNANMEYKT 110

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), 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. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409461 Cd Length: 117 Bit Score: 55.02 E-value: 1.69e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 149 TPEQTIEKDQGETVHLPCMFTFISKDQGP--LNIEWLRLSgpNNEAMDHVVILYSADkiHDDVYPDLKGRVYFTSNDikS 226
Cdd:cd05877    2 TVQAKVFSHRGGNVTLPCRYHYEPELSAPrkIRVKWTKLE--VDYAKEEDVLVAIGT--RHKSYGSYQGRVFLRRAD--D 75

                         90       100
                 ....*....|....*....|..
gi 124249111 227 GDASINITNVQLSDAGTYQCKV 248
Cdd:cd05877   76 LDASLVITDLRLEDYGRYRCEV 97

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.

Pssm-ID: 409355 [Multi-domain] Cd Length: 111 Bit Score: 53.88 E-value: 4.52e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 272 ITTPEQTIQKARGETVHLPCTFTLSPeDHGPLFidWMQLTGPQNevvnRMFIVYLaDKIYDNFYQDMKGRVQFTSNDIRS 351
Cdd:cd00099    1 VTQSPRSLSVQEGESVTLSCEVSSSF-SSTYIY--WYRQKPGQG----PEFLIYL-SSSKGKTKGGVPGRFSGSRDGTSS 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 124249111 352 geASINITDARLSDAGTYQCGVSHAFGTAK-----GTiQLTV 388
Cdd:cd00099   73 --FSLTISNLQPEDSGTYYCAVSESGGTDKltfgsGT-RLTV 111

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Unlike aggrecan which is widely distributed in connective tissue and extracellular matrices, neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409483 Cd Length: 121 Bit Score: 53.30 E-value: 8.72e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 277 QTIQKARGETVHLPCTFTLSPED----HGPlFIDWMQLTGP-----QNEVVNRMFIVYLAdkiydnfyQDMKGRVQFTSN 347
Cdd:cd05902    5 PPVRRPLSSSVLLPCVFTLPPSAssppEGP-RIKWTKLSTSggqqqRPVLVARDNVVRVA--------KAFQGRVSLPGY 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 124249111 348 DIRSGEASINITDARLSDAGTYQCGVSHAFGTAKGTIQLTVVG 390
Cdd:cd05902   76 PKNRYNASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTG 118

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409482 Cd Length: 128 Bit Score: 52.65 E-value: 1.66e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 279 IQKARGETVHLPCTFTLSP---------EDHgpLFIDWMQLTGPQNEVVNRMFIVYLADKIYDNFYQDMKGRVQFTSNDI 349
Cdd:cd05901    7 VHGSLSGSVVLPCRFSTLPtlppsynitSEF--LRIKWTKIQVDKNGKDHKETTVLVAQNGIIKIGQEYMGRVSVPSHPE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 124249111 350 RSGEASINITDARLSDAGTYQCGVSHAFGTAKGTIQLTVVG 390
Cdd:cd05901   85 DQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSG 125

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.

Pssm-ID: 409380 Cd Length: 117 Bit Score: 52.05 E-value: 1.95e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  20 VSITTPEqTIQEVQGETVHLPCMFTLSPEDQGPLDIEWLrlSGPNNEAMDHVIILYAVDKIYSDFYQDMRGRVNFTSNgI 99
Cdd:cd05715    1 MEVYTPR-ELNVLNGSDVRLTCTFTSCYTVGDAFSVTWT--YQPEGGNTTESMFHYSKGKPYILKVGRFKDRVSWAGN-P 76

                         90       100
                 ....*....|....*....|....*...
gi 124249111 100 TSGEASIKIRDVQPADSGTYLCKVKTAP 127
Cdd:cd05715   77 SKKDASIVISNLQFSDNGTYTCDVKNPP 104

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

Pssm-ID: 214653 [Multi-domain] Cd Length: 85 Bit Score: 50.97 E-value: 2.23e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111    25 PEQTIQEvqGETVHLPCMFTLSPEDQgpldIEWLRLSGpnneamdhVIILYavdkiysdfyqdmRGRVNFTSNGitsGEA 104
Cdd:smart00410   2 PSVTVKE--GESVTLSCEASGSPPPE----VTWYKQGG--------KLLAE-------------SGRFSVSRSG---STS 51

                           90       100       110
                   ....*....|....*....|....*....|....
gi 124249111   105 SIKIRDVQPADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:smart00410  52 TLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.

Pssm-ID: 409576 Cd Length: 110 Bit Score: 51.45 E-value: 3.13e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  34 GETVHLPCMFTLSPEDQGpLDIEWLRlsgpnnEAMDHVI--ILYAVDKIySDFYQDMRGRVNFTSNGITSGEASIKIRDV 111
Cdd:cd20984   12 GEDGILSCTFTPDIKLSD-IVIQWLK------EGDSGLVheFKEGKDEL-SRQSPMFRGRTSLFADQVHVGNASLRLKNV 83

                         90       100
                 ....*....|....*....|....*..
gi 124249111 112 QPADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:cd20984   84 QLTDAGTYLCIISNSKGTGNANMEYKT 110

Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core protein (CSPG); The members here are composed of the immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core proteins (CSPGs). Included in this group are the Ig domains of other CSPGs: versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409462 Cd Length: 125 Bit Score: 51.08 E-value: 5.74e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 279 IQKARGETVHLPCTFTLSPEDHGP------LFIDWMQLTGPQNEVVNRMFIVYLADKIYDNfyQDMKGRVQFTSNDIRSG 352
Cdd:cd05878    7 VRVLLGTSVTLPCYFIDPPHPVTPstaplaPRIKWSKVSVDGKKEKEVVLLVATEGRVRVN--SAYQGRVSLPNYPAIPS 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 124249111 353 EASINITDARLSDAGTYQCGVSHAFGTAKGTIQLTVVG 390
Cdd:cd05878   85 DATLEVQSLRASDSGLYRCEVMHGIEDSQDTVELVVKG 122

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), 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. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409461 Cd Length: 117 Bit Score: 50.40 E-value: 8.15e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 274 TPEQTIQKARGETVHLPCTFTLSPEDHGP--LFIDWMQLT---GPQNEVvnrmfIVYLADKiyDNFYQDMKGRVQFTSND 348
Cdd:cd05877    2 TVQAKVFSHRGGNVTLPCRYHYEPELSAPrkIRVKWTKLEvdyAKEEDV-----LVAIGTR--HKSYGSYQGRVFLRRAD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 124249111 349 irSGEASINITDARLSDAGTYQCGVSHAFGTAKGTIQLTVVG 390
Cdd:cd05877   75 --DLDASLVITDLRLEDYGRYRCEVIDGLEDESVVVALRLRG 114

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

Pssm-ID: 214653 [Multi-domain] Cd Length: 85 Bit Score: 49.43 E-value: 8.43e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111   277 QTIQKARGETVHLPCTFTLSPEDHgplfIDWMQltgPQNEVVNRmfivyladkiydnfyqdmKGRVQFTSNdirSGEASI 356
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPE----VTWYK---QGGKLLAE------------------SGRFSVSRS---GSTSTL 53

                           90       100       110
                   ....*....|....*....|....*....|..
gi 124249111   357 NITDARLSDAGTYQCGVSHAFGTAKGTIQLTV 388
Cdd:smart00410  54 TISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).

Pssm-ID: 409383 Cd Length: 113 Bit Score: 49.75 E-value: 1.23e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  34 GETVHLPCMFTlSPEDQGPLDIEWLRLSGPNNEAMdhviilyavdKIYS-----DFYQDMRGRVNFTSNGITSGEASIKI 108
Cdd:cd05718   14 GGSVTLPCSLT-SPGTTKITQVTWMKIGAGSSQNV----------AVFHpqygpSVPNPYAERVEFLAARLGLRNATLRI 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 124249111 109 RDVQPADSGTYLCKVKTAP-GVAKTTVQLTV 138
Cdd:cd05718   83 RNLRVEDEGNYICEFATFPqGNRQGTTWLRV 113

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.

Pssm-ID: 409464 Cd Length: 116 Bit Score: 49.44 E-value: 1.67e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  20 VSITTPEQtIQEVQGETVHLPCMFTLSPEDQGPLDIEWL--RLSGPNNEAmdhviILYAVDKIYSDFYQDMRGRVNFTSN 97
Cdd:cd05880    1 IEVYTSKE-VEAVNGTDVRLKCTFSSSAPIGDTLVITWNfrPLDGGREES-----VFYYHKRPYPPPDGRFKGRVVWDGN 74

                         90       100       110
                 ....*....|....*....|....*....|..
gi 124249111  98 gITSGEASIKIRDVQPADSGTYLCKVKTAPGV 129
Cdd:cd05880   75 -IMRRDASILIWQLQPTDNGTYTCQVKNPPDV 105

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.

Pssm-ID: 409380 Cd Length: 117 Bit Score: 49.35 E-value: 1.89e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 270 VSITTPEqTIQKARGETVHLPCTFTLSPEDHGPLFIDW-MQLTGPQNEVvnRMFIvYLADKIYDNFYQDMKGRVQFTSND 348
Cdd:cd05715    1 MEVYTPR-ELNVLNGSDVRLTCTFTSCYTVGDAFSVTWtYQPEGGNTTE--SMFH-YSKGKPYILKVGRFKDRVSWAGNP 76

                         90       100
                 ....*....|....*....|....*
gi 124249111 349 IRSgEASINITDARLSDAGTYQCGV 373
Cdd:cd05715   77 SKK-DASIVISNLQFSDNGTYTCDV 100

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).

Pssm-ID: 409383 Cd Length: 113 Bit Score: 48.98 E-value: 2.09e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMFTfISKDQGPLNIEWLRLSGPNNEamdhVVILYSADkiHDDVYPD-LKGRVYFTSNDIKSGDASINITNVQ 237
Cdd:cd05718   14 GGSVTLPCSLT-SPGTTKITQVTWMKIGAGSSQ----NVAVFHPQ--YGPSVPNpYAERVEFLAARLGLRNATLRIRNLR 86

                         90       100
                 ....*....|....*....|....*..
gi 124249111 238 LSDAGTYQCKVKTYP-GTVNRNLQLAV 263
Cdd:cd05718   87 VEDEGNYICEFATFPqGNRQGTTWLRV 113

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.

Pssm-ID: 409355 [Multi-domain] Cd Length: 111 Bit Score: 48.87 E-value: 2.55e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 147 ITTPEQTIEKDQGETVHLPC-MFTFISKDqgplNIEWLRLSGPNneamdHVVILYSADKIHDDVYPDLKGRvyFTSNDIK 225
Cdd:cd00099    1 VTQSPRSLSVQEGESVTLSCeVSSSFSST----YIYWYRQKPGQ-----GPEFLIYLSSSKGKTKGGVPGR--FSGSRDG 69

                         90       100
                 ....*....|....*....|....*....
gi 124249111 226 SGDASINITNVQLSDAGTYQCKVKTYPGT 254
Cdd:cd00099   70 TSSFSLTISNLQPEDSGTYYCAVSESGGT 98

Immunoglobulin V-Type;

Pssm-ID: 214650 Cd Length: 81 Bit Score: 47.38 E-value: 3.64e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111    36 TVHLPCmfTLSPEDQGPLDIEWLRLsgPNNEAMDHVIILYAVDKIYSDfyQDMRGRVNFTSNGiTSGEASIKIRDVQPAD 115
Cdd:smart00406   1 SVTLSC--KFSGSTFSSYYVSWVRQ--PPGKGLEWLGYIGSNGSSYYQ--ESYKGRFTISKDT-SKNDVSLTISNLRVED 73


                   ....*...
gi 124249111   116 SGTYLCKV 123
Cdd:smart00406  74 TGTYYCAV 81

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.

Pssm-ID: 409512 Cd Length: 107 Bit Score: 48.15 E-value: 3.70e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 284 GETVHLPCTFTLSPEdhgpLFIDWMQltgPQNEVVNRMFIvYLADKiYDNFYQDMKGRVQFTSNDIRSGEASINITDARL 363
Cdd:cd16091   12 SEDCILPCSFTPGSE----VVIHWYK---QDSDIKVHSYY-YGKDQ-LESQDQRYRNRTSLFKDQISNGNASLLLRRVQL 82

                         90       100
                 ....*....|....*....|....*
gi 124249111 364 SDAGTYQCGVSHAFGTAKGTIQLTV 388
Cdd:cd16091   83 QDEGRYKCYTSTIIGNQESFVNLKV 107

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).

Pssm-ID: 409383 Cd Length: 113 Bit Score: 48.21 E-value: 3.75e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 284 GETVHLPCTFTlSPEDHGPLFIDWMQLTGPQNEVVnrmfivyladKIYD-----NFYQDMKGRVQFTSNDIRSGEASINI 358
Cdd:cd05718   14 GGSVTLPCSLT-SPGTTKITQVTWMKIGAGSSQNV----------AVFHpqygpSVPNPYAERVEFLAARLGLRNATLRI 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 124249111 359 TDARLSDAGTYQCG-VSHAFGTAKGTIQLTV 388
Cdd:cd05718   83 RNLRVEDEGNYICEfATFPQGNRQGTTWLRV 113

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Unlike aggrecan which is widely distributed in connective tissue and extracellular matrices, neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409483 Cd Length: 121 Bit Score: 47.52 E-value: 8.45e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  27 QTIQEVQGETVHLPCMFTLSPEDQGPLD---IEWLRLSGPNNEamDHVIILYAVDKIYSdFYQDMRGRVNFTSNGITSGE 103
Cdd:cd05902    5 PPVRRPLSSSVLLPCVFTLPPSASSPPEgprIKWTKLSTSGGQ--QQRPVLVARDNVVR-VAKAFQGRVSLPGYPKNRYN 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 124249111 104 ASIKIRDVQPADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:cd05902   82 ASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEV 116

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.

Pssm-ID: 409355 [Multi-domain] Cd Length: 111 Bit Score: 47.33 E-value: 8.61e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  34 GETVHLPCMFTLSPedqGPLDIEWLRLSGpnNEAMDHVIILYAVDKIYSDFYQDMrgrvnFTSNGITSGEASIKIRDVQP 113
Cdd:cd00099   13 GESVTLSCEVSSSF---SSTYIYWYRQKP--GQGPEFLIYLSSSKGKTKGGVPGR-----FSGSRDGTSSFSLTISNLQP 82

                         90       100
                 ....*....|....*....|....*....
gi 124249111 114 ADSGTYLCKVKTAPGVAKTT----VQLTV 138
Cdd:cd00099   83 EDSGTYYCAVSESGGTDKLTfgsgTRLTV 111

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

Pssm-ID: 214653 [Multi-domain] Cd Length: 85 Bit Score: 46.34 E-value: 1.06e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111   152 QTIEKDQGETVHLPCmftfISKDQGPLNIEWLRlsgpnneamdhvvilysadkiHDDVYPDLKGRVYFTSNdikSGDASI 231
Cdd:smart00410   2 PSVTVKEGESVTLSC----EASGSPPPEVTWYK---------------------QGGKLLAESGRFSVSRS---GSTSTL 53

                           90       100       110
                   ....*....|....*....|....*....|..
gi 124249111   232 NITNVQLSDAGTYQCKVKTYPGTVNRNLQLAV 263
Cdd:smart00410  54 TISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85

Immunoglobulin I-set domain;

Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 46.10 E-value: 1.27e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111   21 SITTPEQTIQEVQGETVHLPCMFTLSPedqgPLDIEWLRlsgpNNEamdhviilyavdKIYSDfyqdmrGRVNFTSNGit 100
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTP----DPEVSWFK----DGQ------------PLRSS------DRFKVTYEG-- 53

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 124249111  101 sGEASIKIRDVQPADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:pfam07679  54 -GTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).

Pssm-ID: 409378 Cd Length: 114 Bit Score: 46.42 E-value: 1.63e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 271 SITTPEQTIQKARGETVHLPCtftlspedhgplfidwmQLTGPQN----EVvnRMF------IVYLADKIYDNFYQDM-- 338
Cdd:cd05713    2 SVIGPTEPILALVGEDAELPC-----------------HLSPKMSaehmEV--RWFrsqfspVVHLYRDGQDQEEEQMpe 62

                         90       100       110
                 ....*....|....*....|....*....|....
gi 124249111 339 -KGRVQFTSNDIRSGEASINITDARLSDAGTYQC 371
Cdd:cd05713   63 yRGRTELLKDAIAEGSVALRIHNVRPSDEGQYTC 96

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).

Pssm-ID: 409378 Cd Length: 114 Bit Score: 46.42 E-value: 1.65e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 146 SITTPEQTIEKDQGETVHLPCMFtFISKDQGPLNIEWLRlSGPNNeamdhVVILYSADKIHDDV-YPDLKGRVYFTSNDI 224
Cdd:cd05713    2 SVIGPTEPILALVGEDAELPCHL-SPKMSAEHMEVRWFR-SQFSP-----VVHLYRDGQDQEEEqMPEYRGRTELLKDAI 74

                         90       100
                 ....*....|....*....|..
gi 124249111 225 KSGDASINITNVQLSDAGTYQC 246
Cdd:cd05713   75 AEGSVALRIHNVRPSDEGQYTC 96

First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-4 (also known as poliovirus receptor related protein 4 or LNIR receptor). Nectin-4 belongs to the nectin family, which is comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example nectin-4 trans-interacts with nectin-1. Nectin-4 has also been shown to interact with the actin filament-binding protein, afadin. Unlike the other nectins, which are widely expressed in adult tissues, nectin-4 is mainly expressed during embryogenesis, and is not detected in normal adult tissue or in serum. Nectin-4 is re-expressed in breast carcinoma, and patients having metastatic breast cancer have a circulating form of nectin-4 formed from the ectodomain

Pssm-ID: 409471 Cd Length: 108 Bit Score: 45.66 E-value: 2.65e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMFTFISKDQgPLNIEWLRLSgpNNEAMDHVVILYSADKIHddVYPDLKGRVYF-TSNDIksGDASINITNVQ 237
Cdd:cd05888    8 GQDAKLPCFYRGDSGEQ-VGQVAWARVD--AGEGAQEIALLHSKYGLH--VFPAYEGRVEQpPPPRP--ADGSVLLRNAV 80

                         90       100
                 ....*....|....*....|....*..
gi 124249111 238 LSDAGTYQCKVKTYP-GTVNRNLQLAV 263
Cdd:cd05888   81 QADEGEYECRVSTFPaGNFQAELRLRV 107

Immunoglobulin Variable region-containing chitin-binding proteins; an immunoglobulin V-set domain; The members here are composed of the immunoglobulin variable (IgV) region-containing chitin-binding proteins (VCBPs). VCBPs are secreted, immune-type molecules that have been identified in both amphioxus and sea squirt (Ciona intestinalis). VCBPs, which consist of a leader peptide, two tandem N-terminal immunoglobulin V-type domains and a single C-terminal chitin-binding domain, belong to a multigene family encoding secreted proteins. The VCBPs were identified first in the cephalochordate Branchiostoma floridae and show structural similarities with V-type domains of immunoglobulins and T cell receptors, suggesting that VCBPs represent a unique gut-associated form of innate immune proteins. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other.

Pssm-ID: 409555 Cd Length: 123 Bit Score: 45.69 E-value: 3.64e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  21 SITTPEQTIQEVQ-GETVHLPCMFTLSPEDQGPLdIEWLRLSGPNneamDHVIILYAVDKI------YSDFYQDMRGRVN 93
Cdd:cd20963    3 TVTVPSYTRTDPTwGNRVELPCSYTISPAAQPPT-ITWLKGISVD----RAEVVFKGFKYWnetsssGEVYFGDYAGRAS 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 124249111  94 FTSngitSGEASIKIRDVQPADSGTYLCKV 123
Cdd:cd20963   78 VAS----LTQPTLVLTDLKFDDWGRYWCRV 103

Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core protein (CSPG); The members here are composed of the immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core proteins (CSPGs). Included in this group are the Ig domains of other CSPGs: versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409462 Cd Length: 125 Bit Score: 45.69 E-value: 3.93e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  29 IQEVQGETVHLPCMFTLSPEDQGP------LDIEWLRLSGPNNEAMDhVIILYAVD---KIYSDFyqdmRGRVNFTSNGI 99
Cdd:cd05878    7 VRVLLGTSVTLPCYFIDPPHPVTPstaplaPRIKWSKVSVDGKKEKE-VVLLVATEgrvRVNSAY----QGRVSLPNYPA 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 124249111 100 TSGEASIKIRDVQPADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:cd05878   82 IPSDATLEVQSLRASDSGLYRCEVMHGIEDSQDTVELVV 120

Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP); The members here are composed of the immunoglobulin (Ig)-like domain of the Signal-Regulatory Protein (SIRP). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions, but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three immunoglobulin superfamily domains, a single V-set, and two C1-set IgSF domains. Their cytoplasmic tails that contain either ITIMs or transmembrane regions have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs, but also binds CD47 with much less affinity. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

Pssm-ID: 409516 Cd Length: 111 Bit Score: 45.24 E-value: 4.08e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 147 ITTPEQTIEKDQGETVHLPCMFTFISKdQGPlnIEWLRLSGPNNEamdhvvILYSADKIHddvYPdlkgRVYFTSNDIKS 226
Cdd:cd16097    2 VIQPEKSVSVAAGESATLHCTVTSLIP-VGP--IQWFRGAGPGRE------LIYNQKEGH---FP----RVTTVSDLTKR 65

                         90       100
                 ....*....|....*....|..
gi 124249111 227 G--DASINITNVQLSDAGTYQC 246
Cdd:cd16097   66 NnmDFSIRISNITPADAGTYYC 87

Immunoglobulin V-Type;

Pssm-ID: 214650 Cd Length: 81 Bit Score: 44.30 E-value: 4.46e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111   161 TVHLPCmfTFISKDQGPLNIEWLRlsgpnnEAMDHVVILYSADKIHDDVYPD--LKGRVyFTSNDIKSGDASINITNVQL 238
Cdd:smart00406   1 SVTLSC--KFSGSTFSSYYVSWVR------QPPGKGLEWLGYIGSNGSSYYQesYKGRF-TISKDTSKNDVSLTISNLRV 71

                           90
                   ....*....|
gi 124249111   239 SDAGTYQCKV 248
Cdd:smart00406  72 EDTGTYYCAV 81

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

Pssm-ID: 409372 [Multi-domain] Cd Length: 109 Bit Score: 44.95 E-value: 4.95e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 272 ITTPEQTIQKARGETVHLPCTFTLSPEDhgPLFidWM-QLTGPQNEVVNRMFIVYLADKiydnfyqdmKGRVQFTSNDiR 350
Cdd:cd04983    1 VTQSPQSLSVQEGENVTLNCNYSTSTFY--YLF--WYrQYPGQGPQFLIYISSDSGNKK---------KGRFSATLDK-S 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 124249111 351 SGEASINITDARLSDAGTYQCGVSHAFGTAK-----GTiQLTV 388
Cdd:cd04983   67 RKSSSLHISAAQLSDSAVYFCALSESGGTGKltfgkGT-RLTV 108

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.

Pssm-ID: 409512 Cd Length: 107 Bit Score: 44.69 E-value: 5.57e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  34 GETVHLPCMFTLSPEDQgpldIEWLRlsgPNNEAMDHVIIlYAVDKiYSDFYQDMRGRVNFTSNGITSGEASIKIRDVQP 113
Cdd:cd16091   12 SEDCILPCSFTPGSEVV----IHWYK---QDSDIKVHSYY-YGKDQ-LESQDQRYRNRTSLFKDQISNGNASLLLRRVQL 82

                         90       100
                 ....*....|....*....|....*
gi 124249111 114 ADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:cd16091   83 QDEGRYKCYTSTIIGNQESFVNLKV 107

Immunoglobulin V-Type;

Pssm-ID: 214650 Cd Length: 81 Bit Score: 43.91 E-value: 6.16e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111   286 TVHLPCTFTLSPEDHgpLFIDWM-QLTGPQNEVVnrMFIVYLADKIYDNFYqdmKGRVQFtSNDIRSGEASINITDARLS 364
Cdd:smart00406   1 SVTLSCKFSGSTFSS--YYVSWVrQPPGKGLEWL--GYIGSNGSSYYQESY---KGRFTI-SKDTSKNDVSLTISNLRVE 72


                   ....*....
gi 124249111   365 DAGTYQCGV 373
Cdd:smart00406  73 DTGTYYCAV 81

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.

Pssm-ID: 409576 Cd Length: 110 Bit Score: 44.51 E-value: 6.94e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 283 RGETVHLPCTFTLSPEDHGpLFIDWMQLTGPQneVVNRMFivYLADKIYDNfYQDMKGRVQFTSNDIRSGEASINITDAR 362
Cdd:cd20984   11 IGEDGILSCTFTPDIKLSD-IVIQWLKEGDSG--LVHEFK--EGKDELSRQ-SPMFRGRTSLFADQVHVGNASLRLKNVQ 84

                         90       100
                 ....*....|....*....|....*.
gi 124249111 363 LSDAGTYQCGVSHAFGTAKGTIQLTV 388
Cdd:cd20984   85 LTDAGTYLCIISNSKGTGNANMEYKT 110

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

Pssm-ID: 409372 [Multi-domain] Cd Length: 109 Bit Score: 44.57 E-value: 7.02e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  23 TTPEQTIQEvqGETVHLPCMFTLSPEDqgplDIEWLRLsgPNNEAMDHVIILYAVDKIYSDFyqdmRGRVNFTSngiTSG 102
Cdd:cd04983    4 SPQSLSVQE--GENVTLNCNYSTSTFY----YLFWYRQ--YPGQGPQFLIYISSDSGNKKKG----RFSATLDK---SRK 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 124249111 103 EASIKIRDVQPADSGTYLCKVKTAPGVAKTT----VQLTV 138
Cdd:cd04983   69 SSSLHISAAQLSDSAVYFCALSESGGTGKLTfgkgTRLTV 108

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.

Pssm-ID: 409512 Cd Length: 107 Bit Score: 44.69 E-value: 7.04e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMFTfiskDQGPLNIEWLRlsgPNNEAMDHVVIlYSADKIhDDVYPDLKGRVYFTSNDIKSGDASINITNVQL 238
Cdd:cd16091   12 SEDCILPCSFT----PGSEVVIHWYK---QDSDIKVHSYY-YGKDQL-ESQDQRYRNRTSLFKDQISNGNASLLLRRVQL 82

                         90       100
                 ....*....|....*....|....*
gi 124249111 239 SDAGTYQCKVKTYPGTVNRNLQLAV 263
Cdd:cd16091   83 QDEGRYKCYTSTIIGNQESFVNLKV 107

Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core protein (CSPG); The members here are composed of the immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core proteins (CSPGs). Included in this group are the Ig domains of other CSPGs: versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409462 Cd Length: 125 Bit Score: 44.53 E-value: 1.01e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMFTFISKDQGPLN------IEWLRLSGPNNEAMDHVVILYSADKIHddVYPDLKGRVYFTSNDIKSGDASIN 232
Cdd:cd05878   12 GTSVTLPCYFIDPPHPVTPSTaplaprIKWSKVSVDGKKEKEVVLLVATEGRVR--VNSAYQGRVSLPNYPAIPSDATLE 89

                         90
                 ....*....|....*.
gi 124249111 233 ITNVQLSDAGTYQCKV 248
Cdd:cd05878   90 VQSLRASDSGLYRCEV 105

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409379 Cd Length: 123 Bit Score: 44.12 E-value: 1.32e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  29 IQEVQGETVHLPCMFTLSPEDQGP----LDIEWLRLSGPNNEAMDhVIILYAVDKIYSdFYQDMRGRVNFTSNGITSGEA 104
Cdd:cd05714    7 VFSHLGGNVTLPCKFYRDPTAFGSgihkIRIKWTKLTSDSGYLKE-VDVLVAMGNVVY-HKKTYGGRVSVPLKPGSDSDA 84

                         90       100       110
                 ....*....|....*....|....*....|....
gi 124249111 105 SIKIRDVQPADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:cd05714   85 SLVITDLTASDYGLYRCEVIEGIEDDQDVVALDV 118

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), 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. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409461 Cd Length: 117 Bit Score: 42.70 E-value: 3.29e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  24 TPEQTIQEVQGETVHLPCMFTLSPEDQGP--LDIEWLRLSgpNNEAMDHVIILyAVDKIYSDfYQDMRGRVNFtsNGITS 101
Cdd:cd05877    2 TVQAKVFSHRGGNVTLPCRYHYEPELSAPrkIRVKWTKLE--VDYAKEEDVLV-AIGTRHKS-YGSYQGRVFL--RRADD 75

                         90       100
                 ....*....|....*....|..
gi 124249111 102 GEASIKIRDVQPADSGTYLCKV 123
Cdd:cd05877   76 LDASLVITDLRLEDYGRYRCEV 97

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.

Pssm-ID: 409464 Cd Length: 116 Bit Score: 42.89 E-value: 3.69e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 145 VSITTPEQtIEKDQGETVHLPCMFTFISKDQGPLNIEWLrlSGPNNEAMDHVVILYsadkiHDDVYPDL----KGRVYFT 220
Cdd:cd05880    1 IEVYTSKE-VEAVNGTDVRLKCTFSSSAPIGDTLVITWN--FRPLDGGREESVFYY-----HKRPYPPPdgrfKGRVVWD 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 124249111 221 SNdIKSGDASINITNVQLSDAGTYQCKVKTYP 252
Cdd:cd05880   73 GN-IMRRDASILIWQLQPTDNGTYTCQVKNPP 103

Immunoglobulin domain; This family contains immunoglobulin-like domains.

Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 41.78 E-value: 3.99e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  146 SITTPEQTIEKDQGETVHLPCMFTFISkdqgPLNIEWLRlsgpNNEAMDHVVILYSadkihddvypdlkgrvyftsnDIK 225
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSP----PPTITWYK----NGEPISSGSTRSR---------------------SLS 53

                          90       100
                  ....*....|....*....|....
gi 124249111  226 SGDASINITNVQLSDAGTYQCKVK 249
Cdd:pfam13927  54 GSNSTLTISNVTRSDAGTYTCVAS 77

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409379 Cd Length: 123 Bit Score: 42.97 E-value: 4.06e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMFTFISKDQGP----LNIEWLRLSGPNNEAMDHVVILYSADKIHddVYPDLKGRVYFTSNDIKSGDASINIT 234
Cdd:cd05714   12 GGNVTLPCKFYRDPTAFGSgihkIRIKWTKLTSDSGYLKEVDVLVAMGNVVY--HKKTYGGRVSVPLKPGSDSDASLVIT 89

                         90
                 ....*....|....
gi 124249111 235 NVQLSDAGTYQCKV 248
Cdd:cd05714   90 DLTASDYGLYRCEV 103

Immunoglobulin domain; This family contains immunoglobulin-like domains.

Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 41.40 E-value: 4.53e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111   21 SITTPEQTIQEVQGETVHLPCMFTLSPEDQgpldIEWLRLSGPNNEamdhviilyavdkiysdfyqdmrgrVNFTSNGIT 100
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPT----ITWYKNGEPISS-------------------------GSTRSRSLS 53

                          90       100
                  ....*....|....*....|....
gi 124249111  101 SGEASIKIRDVQPADSGTYLCKVK 124
Cdd:pfam13927  54 GSNSTLTISNVTRSDAGTYTCVAS 77

Immunoglobulin Variable region-containing chitin-binding proteins; an immunoglobulin V-set domain; The members here are composed of the immunoglobulin variable (IgV) region-containing chitin-binding proteins (VCBPs). VCBPs are secreted, immune-type molecules that have been identified in both amphioxus and sea squirt (Ciona intestinalis). VCBPs, which consist of a leader peptide, two tandem N-terminal immunoglobulin V-type domains and a single C-terminal chitin-binding domain, belong to a multigene family encoding secreted proteins. The VCBPs were identified first in the cephalochordate Branchiostoma floridae and show structural similarities with V-type domains of immunoglobulins and T cell receptors, suggesting that VCBPs represent a unique gut-associated form of innate immune proteins. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other.

Pssm-ID: 409555 Cd Length: 123 Bit Score: 42.60 E-value: 5.09e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 267 IGSVSITTPEQTIQKArGETVHLPCTFTLSPEDHGPLfIDWMQ-LTGPQNEVVNRMFIVYLADK-IYDNFYQDMKGRVQF 344
Cdd:cd20963    1 ITTVTVPSYTRTDPTW-GNRVELPCSYTISPAAQPPT-ITWLKgISVDRAEVVFKGFKYWNETSsSGEVYFGDYAGRASV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 124249111 345 TSNDirsgEASINITDARLSDAGTYQCGV-----SHAFGT 379
Cdd:cd20963   79 ASLT----QPTLVLTDLKFDDWGRYWCRVanwsqRDEFGT 114

Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP); The members here are composed of the immunoglobulin (Ig)-like domain of the Signal-Regulatory Protein (SIRP). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions, but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three immunoglobulin superfamily domains, a single V-set, and two C1-set IgSF domains. Their cytoplasmic tails that contain either ITIMs or transmembrane regions have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs, but also binds CD47 with much less affinity. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

Pssm-ID: 409516 Cd Length: 111 Bit Score: 42.16 E-value: 5.61e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  22 ITTPEQTIQEVQGETVHLPCMFT-LSPedQGPldIEWLRLSGPNNEAmdhviilyavdkIYSdFYQDMRGRVNFTSNGIT 100
Cdd:cd16097    2 VIQPEKSVSVAAGESATLHCTVTsLIP--VGP--IQWFRGAGPGREL------------IYN-QKEGHFPRVTTVSDLTK 64

                         90       100
                 ....*....|....*....|...
gi 124249111 101 SG--EASIKIRDVQPADSGTYLC 121
Cdd:cd16097   65 RNnmDFSIRISNITPADAGTYYC 87

First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of DNAX accessory molecule 1 (DNAM-1, also known as CD226). DNAM-1 is a transmembrane protein having two Ig-like domains. It is an adhesion molecule which plays a part in tumor-directed cytotoxicity and adhesion in natural killer (NK) cells and T lymphocytes. It has been shown to regulate the NK cell killing of several tumor types, including myeloma cells and ovarian carcinoma cells. DNAM-1 interacts specifically with poliovirus receptor (PVR; CD155) and nectin -2 (CD211), other members of the Ig superfamily. DNAM-1 is expressed in most peripheral T cells, NK cells, monocytes and a subset of B lymphocytes.

Pssm-ID: 409472 Cd Length: 111 Bit Score: 41.77 E-value: 8.11e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 160 ETVHLPCMFTfiSKDQgPLNIEWLRLSGPNneamDHVVILYSADKIHDDvyPDLKGRVYFTSNDIKSGDASINITNVQLS 239
Cdd:cd05889   15 ENMSLECVYP--STGI-LTQVEWTKIGGQK----DNIAVYHPTHGMHIR--KPYAGRVYFLNSTMASNNMSLSFRNASED 85

                         90
                 ....*....|...
gi 124249111 240 DAGTYQCKVKTYP 252
Cdd:cd05889   86 DVGYYSCSLYTYP 98

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.

Pssm-ID: 409470 Cd Length: 110 Bit Score: 41.07 E-value: 1.16e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMftfISKDQGPLNIEWLRLSGPNNE--AMDHVVILYSadkihddVYPDLKGRVYFTSNDIKsgDASINITNV 236
Cdd:cd05887   14 GKNVSLKCL---IEVNETITQISWEKIHGKSSQtvAVHHPQYGIS-------IQGEYQGRVSFKNYSLN--DATITLHNV 81

                         90
                 ....*....|....*.
gi 124249111 237 QLSDAGTYQCKVKTYP 252
Cdd:cd05887   82 GFSDSGKYICKAVTFP 97

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

Pssm-ID: 409568 [Multi-domain] Cd Length: 90 Bit Score: 40.31 E-value: 1.40e-04

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 124249111 102 GEASIKIRDVQPADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:cd20976   54 GVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90

Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H6 (also known as NCR3LG1). B7-H6 contains one IgV domain and one IgC domain (IgV-IgC) and belongs to the B7-family, which consists of structurally related cell-surface protein ligands which bind to receptors on lymphocytes that regulate immune responses. B7-H6 is a ligand of NKp30, which is a member of CD28 family and an activating receptor of natural killer (NK) cells. The expression of NKp30 has been found in most of NK cells, which is involved in the process of tumor cell killing and interaction with antigen presenting cells (APCs) such as dendritic cells. Studies showed that NK cells eliminate B7-H6-expressing tumor cells either directly via cytotoxicity or indirectly by cytokine secretion. For instance, chimeric NKp30-expressing T cells responded to B7-H6(+) tumor cells and those T cells produced IFN-gamma and killed B7-H6-expressing tumor cells in vivo. B7-H6 mRNA is not found in normal cells, while high expression of B7-H6 is found in certain type tumor cells, such as lymphoma, leukemia, ovarian cancer, brain tumors, breast cancers, and various sarcomas. Since B7-H6 can bind NKp30 to exert anti-tumor effects by NK cells, which are able to recognize the difference between cancer cells and normal cells, B7-H6 may serve as a promising target for cancer immunotherapy.

Pssm-ID: 409573 Cd Length: 114 Bit Score: 41.06 E-value: 1.57e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 124249111 224 IKSGDASINITNVQLSDAGTYQCKVKTYPGTVNRNLQLAV 263
Cdd:cd20981   75 LKSGDASLQLPGVQLEEAGEYRCEVVVTPLKAQGTVQLEV 114

First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-4 (also known as poliovirus receptor related protein 4 or LNIR receptor). Nectin-4 belongs to the nectin family, which is comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example nectin-4 trans-interacts with nectin-1. Nectin-4 has also been shown to interact with the actin filament-binding protein, afadin. Unlike the other nectins, which are widely expressed in adult tissues, nectin-4 is mainly expressed during embryogenesis, and is not detected in normal adult tissue or in serum. Nectin-4 is re-expressed in breast carcinoma, and patients having metastatic breast cancer have a circulating form of nectin-4 formed from the ectodomain

Pssm-ID: 409471 Cd Length: 108 Bit Score: 40.27 E-value: 2.36e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  32 VQGETVHLPCMFTLSPEDQgPLDIEWLRlSGPNNEAMDhviILYAVDKIYSDFYQDMRGRVNFTSNgITSGEASIKIRDV 111
Cdd:cd05888    6 VLGQDAKLPCFYRGDSGEQ-VGQVAWAR-VDAGEGAQE---IALLHSKYGLHVFPAYEGRVEQPPP-PRPADGSVLLRNA 79

                         90       100
                 ....*....|....*....|....*...
gi 124249111 112 QPADSGTYLCKVKTAP-GVAKTTVQLTV 138
Cdd:cd05888   80 VQADEGEYECRVSTFPaGNFQAELRLRV 107

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409482 Cd Length: 128 Bit Score: 40.71 E-value: 2.40e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 162 VHLPCMFTFISKDQGP-------LNIEWLRLSGPNNEAMDHVVILYSADKIHDDVYPDLKGRVYFTSNDIKSGDASINIT 234
Cdd:cd05901   15 VVLPCRFSTLPTLPPSynitsefLRIKWTKIQVDKNGKDHKETTVLVAQNGIIKIGQEYMGRVSVPSHPEDQGDASLTIV 94

                         90
                 ....*....|....
gi 124249111 235 NVQLSDAGTYQCKV 248
Cdd:cd05901   95 KLRASDAGVYRCEV 108

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409482 Cd Length: 128 Bit Score: 40.33 E-value: 3.70e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  37 VHLPCMFTLSPEDQGP-------LDIEWLRL-SGPNNEAMDHVIILYAVDKIYSdFYQDMRGRVNFTSNGITSGEASIKI 108
Cdd:cd05901   15 VVLPCRFSTLPTLPPSynitsefLRIKWTKIqVDKNGKDHKETTVLVAQNGIIK-IGQEYMGRVSVPSHPEDQGDASLTI 93

                         90       100       110
                 ....*....|....*....|....*....|
gi 124249111 109 RDVQPADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:cd05901   94 VKLRASDAGVYRCEVMHGIEDTQDTVSLDV 123

Immunoglobulin variable (IgV) domain of Natural Killer cell activating receptor NKp30 and similar domains; The members here are composed of the immunoglobulin variable region (IgV) of Natural Killer cell activating receptor NKp30 (also known as Natural Cytotoxicity triggering Receptor 3 (NCR3)) and similar domains. NKp30 Recognizes the N-Terminal IgV Domain of B7-H6. In humans, the activating natural cytotoxicity receptor NKp30 plays a major role in NK cell-mediated tumor cell lysis. NKp30 recognizes the cell-surface protein B7-H6, which is expressed on tumor, but not healthy, cells.

Pssm-ID: 409520 Cd Length: 112 Bit Score: 39.57 E-value: 4.30e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  25 PEqtIQEVQGETVHLPCMFTLSpedQGPLDI---EWLRlsgpnneamDHVIILYAVDKIYSDFyqdmRGRV-NFTSNGIT 100
Cdd:cd20926    8 PE--IRTLEGSSAFLPCSFNAS---QGRLAIgsvTWFR---------DEVAPGKEVRNGTPEF----RGRLaPLASSRFL 69

                         90       100
                 ....*....|....*....|....*
gi 124249111 101 SG-EASIKIRDVQPADSGTYLCKVK 124
Cdd:cd20926   70 RDhQAELHIWDVRGHDAGIYVCRVE 94

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.

Pssm-ID: 409539 Cd Length: 110 Bit Score: 39.53 E-value: 4.93e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 272 ITTPEQTIQKARGETVHLPCTFTLSPE-DHGPLFIDWmqltgpqnEVVNRMFIVYLADKiydnfyQDMK-------GRVQ 343
Cdd:cd20947    1 VTVPKDLYVVEYGSNMTIECKFPVEKQlDLAALIVYW--------EMEDKNIIQFVHGE------EDLKvqhssyrQRAR 66

                         90       100       110
                 ....*....|....*....|....*....|..
gi 124249111 344 FTSNDIRSGEASINITDARLSDAGTYQCGVSH 375
Cdd:cd20947   67 LLKDQLSLGNAALQITDVKLQDAGVYRCMISY 98

Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP); The members here are composed of the immunoglobulin (Ig)-like domain of the Signal-Regulatory Protein (SIRP). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions, but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three immunoglobulin superfamily domains, a single V-set, and two C1-set IgSF domains. Their cytoplasmic tails that contain either ITIMs or transmembrane regions have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs, but also binds CD47 with much less affinity. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

Pssm-ID: 409516 Cd Length: 111 Bit Score: 39.46 E-value: 5.02e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 272 ITTPEQTIQKARGETVHLPCTFT-LSPEdhGPlfIDWMQLTGPQNEVvnrmfivyladkIYdNFYQDMKGRVQFTSNDIR 350
Cdd:cd16097    2 VIQPEKSVSVAAGESATLHCTVTsLIPV--GP--IQWFRGAGPGREL------------IY-NQKEGHFPRVTTVSDLTK 64

                         90       100
                 ....*....|....*....|...
gi 124249111 351 SG--EASINITDARLSDAGTYQC 371
Cdd:cd16097   65 RNnmDFSIRISNITPADAGTYYC 87

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.

Pssm-ID: 409433 Cd Length: 108 Bit Score: 39.25 E-value: 5.48e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMFTFiskDQGPLNIEWLRLSGPNNEAMdhvvILYSAdKIHDDVYPDLKGRVYFTSndIKSGDASINITNVQL 238
Cdd:cd05846   13 GGNATLSCNLTL---PEEVLQVTWQKIKASSPENI----VTYSK-KYGVKIQPSYVRRISFTS--SGLNSTSITIWNVTL 82

                         90
                 ....*....|....
gi 124249111 239 SDAGTYQCKVKTYP 252
Cdd:cd05846   83 EDEGCYKCLFNTFP 96

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

Pssm-ID: 409570 [Multi-domain] Cd Length: 88 Bit Score: 38.53 E-value: 6.30e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  22 ITTPEQTIQEVQGETVHLPCMFTLSPEDQgpldIEWL----RLSGPnneamdhviilyavdkiysdfyqdmRGRVNFTSN 97
Cdd:cd20978    4 IQKPEKNVVVKGGQDVTLPCQVTGVPQPK----ITWLhngkPLQGP-------------------------MERATVEDG 54

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 124249111  98 GITsgeasikIRDVQPADSGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:cd20978   55 TLT-------IINVQPEDTGYYGCVATNEIGDIYTETLLHV 88

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.

Pssm-ID: 409538 Cd Length: 102 Bit Score: 38.67 E-value: 6.97e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  21 SITTPEQTIQEVQGETVHLPCMFTLSPEDQgplDIEWLRLSGpnneamDHVIILYAVDKIYSDFyqdmRGRVNFTSngit 100
Cdd:cd20946    1 TVPSSQQVVTVVENQEVILSCKTPKKTSSP---RVEWKKLQR------DVTFVVFQNNKIQGDY----KGRAEILG---- 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 124249111 101 sgeASIKIRDVQPADSGTYLCKVkTAPG----VAKTTVQLTV 138
Cdd:cd20946   64 ---TNITIKNVTRSDSGKYRCEV-SARSdgqnLGEVTVTLEV 101

Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3), and similar domains; The members here are composed of the immunoglobulin variable (IgV) domain of T cell immunoglobulin domain and mucin domain 3 (Tim-3; also known as Hepatitis A virus cellular receptor 2 (HAVcr-2) and Cluster of Differentiation 366 (CD366)) and similar proteins. TIM-3 is a checkpoint inhibitor in immune responses to tumors, as well as involved in chronic viral infections. Thus, Tim-3 has emerged as one of most promising immune checkpoint targets for cancer immunotherapy. Tim-3 is highly expressed on Th1 lymphocytes and CD11b(+) macrophages and is upregulated on activated T and myeloid cells. TIM-3 regulates macrophage, activation and inhibits Th1 mediated immune responses to promote immunological tolerance. There are three TIM family members in humans (TIM-1, TIM-3, and TIM-4) and eight members in mice (TIM-1 to TIM-8). The IgV domain of human TIM-3 has been shown to bind ligands such as carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1), high mobility group protein B1 (HMGB1)and galectin-9 (GAL9). The binding of GAL9 to TIM-3 can negatively regulate Th1 immune response, enhance immune tolerance and inhibit anti#tumor immunity. Dysregulation of the TIM-3/GAL9 pathway is implicated in numerous chronic autoimmune diseases, such as multiple sclerosis and systemic lupus erythematosus.

Pssm-ID: 409574 Cd Length: 107 Bit Score: 38.59 E-value: 7.61e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 124249111 214 KGRVYFTSNDIKSGDASINITNVQLSDAGTYQCKVKtYPGTVN 256
Cdd:cd20982   56 KSSRYQLKGDFSKGDVSLTIENVTLADSGIYCCRIQ-IPGIMN 97

Immunoglobulin I-set domain;

Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 38.39 E-value: 7.82e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 124249111  340 GRVQFTSNDirsGEASINITDARLSDAGTYQCGVSHAFGTAKGTIQLTV 388
Cdd:pfam07679  45 DRFKVTYEG---GTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90

Immunoglobulin domain; This family contains immunoglobulin-like domains.

Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 37.93 E-value: 7.86e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  271 SITTPEQTIQKARGETVHLPCTFTLSPEDHgplfIDWMQLTGPQNEVVNRMFIVYladkiydnfyqdmkgrvqftsndir 350
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPT----ITWYKNGEPISSGSTRSRSLS------------------------- 53

                          90       100
                  ....*....|....*....|....
gi 124249111  351 SGEASINITDARLSDAGTYQCGVS 374
Cdd:pfam13927  54 GSNSTLTISNVTRSDAGTYTCVAS 77

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

Pssm-ID: 409372 [Multi-domain] Cd Length: 109 Bit Score: 38.41 E-value: 1.02e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 147 ITTPEQTIEKDQGETVHLPCMFTfiskDQGPLNIEWLRLsgPNNEAMDHVVILYSADKihddvyPDLKGRvyFTSNDIKS 226
Cdd:cd04983    1 VTQSPQSLSVQEGENVTLNCNYS----TSTFYYLFWYRQ--YPGQGPQFLIYISSDSG------NKKKGR--FSATLDKS 66

                         90       100
                 ....*....|....*....|....*....
gi 124249111 227 -GDASINITNVQLSDAGTYQCKVKTYPGT 254
Cdd:cd04983   67 rKSSSLHISAAQLSDSAVYFCALSESGGT 95

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.

Pssm-ID: 409469 Cd Length: 113 Bit Score: 38.41 E-value: 1.04e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMFTFISKDQGPLNIEWLRLSgpnNEAMDHVVILYSADKIhdDVYPDLKGRVYFTSNDIKsgDASINITNVQL 238
Cdd:cd05886   14 GTDVVLHCSFANPLPSVKITQVTWQKST---NGSKQNVAIYNPSMGV--SVLPPYRERVTFLNPSFT--DGTIRLSRLEL 86

                         90       100
                 ....*....|....*....|....*.
gi 124249111 239 SDAGTYQCKVKTYPgTVNRNLQLAVT 264
Cdd:cd05886   87 EDEGVYICEFATFP-TGNRESQLNLT 111

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

Pssm-ID: 409353 [Multi-domain] Cd Length: 70 Bit Score: 37.31 E-value: 1.05e-03

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 124249111 220 TSNDIKSGDASINITNVQLSDAGTYQCKVKTYPGT 254
Cdd:cd00096   30 DSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGG 64

Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H6 (also known as NCR3LG1). B7-H6 contains one IgV domain and one IgC domain (IgV-IgC) and belongs to the B7-family, which consists of structurally related cell-surface protein ligands which bind to receptors on lymphocytes that regulate immune responses. B7-H6 is a ligand of NKp30, which is a member of CD28 family and an activating receptor of natural killer (NK) cells. The expression of NKp30 has been found in most of NK cells, which is involved in the process of tumor cell killing and interaction with antigen presenting cells (APCs) such as dendritic cells. Studies showed that NK cells eliminate B7-H6-expressing tumor cells either directly via cytotoxicity or indirectly by cytokine secretion. For instance, chimeric NKp30-expressing T cells responded to B7-H6(+) tumor cells and those T cells produced IFN-gamma and killed B7-H6-expressing tumor cells in vivo. B7-H6 mRNA is not found in normal cells, while high expression of B7-H6 is found in certain type tumor cells, such as lymphoma, leukemia, ovarian cancer, brain tumors, breast cancers, and various sarcomas. Since B7-H6 can bind NKp30 to exert anti-tumor effects by NK cells, which are able to recognize the difference between cancer cells and normal cells, B7-H6 may serve as a promising target for cancer immunotherapy.

Pssm-ID: 409573 Cd Length: 114 Bit Score: 38.36 E-value: 1.27e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  37 VHLPC-MFTLSPEDQGPLDIEWLRLSgPNNEAMdhviilYAVDKIYSDFYQDMRGRVNFTSNGITSGEASIKIRDVQPAD 115
Cdd:cd20981   19 VTIFCnIFYSQPLNITSMGITWFRKS-LTFDKE------VKVFEFFGDHQKAFRPGAIVSPWRLKSGDASLQLPGVQLEE 91

                         90       100
                 ....*....|....*....|...
gi 124249111 116 SGTYLCKVKTAPGVAKTTVQLTV 138
Cdd:cd20981   92 AGEYRCEVVVTPLKAQGTVQLEV 114

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Unlike aggrecan which is widely distributed in connective tissue and extracellular matrices, neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409483 Cd Length: 121 Bit Score: 38.28 E-value: 1.33e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 160 ETVHLPCMFTF----ISKDQGPlNIEWLRLSGPNNEamDHVVILYSADKIHDdVYPDLKGRVYFTSNDIKSGDASINITN 235
Cdd:cd05902   13 SSVLLPCVFTLppsaSSPPEGP-RIKWTKLSTSGGQ--QQRPVLVARDNVVR-VAKAFQGRVSLPGYPKNRYNASLVLSR 88

                         90
                 ....*....|...
gi 124249111 236 VQLSDAGTYQCKV 248
Cdd:cd05902   89 LRYSDSGTYRCEV 101

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

Pssm-ID: 409391 [Multi-domain] Cd Length: 98 Bit Score: 37.63 E-value: 1.73e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 124249111 226 SGDasINITNVQLSDAGTYQCKVKTYPGTVNRNLQLAVTD 265
Cdd:cd05726   59 TGD--LTITNVQRSDVGYYICQALNVAGSILAKAQLEVTD 96

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

Pssm-ID: 409353 [Multi-domain] Cd Length: 70 Bit Score: 36.54 E-value: 1.99e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  37 VHLPCMFTLSPedqgPLDIEWLRLSGPNNEAMDHviilyavdkiysdfyqdmrgrvnftSNGITSGEASIKIRDVQPADS 116
Cdd:cd00096    1 VTLTCSASGNP----PPTITWYKNGKPLPPSSRD-------------------------SRRSELGNGTLTISNVTLEDS 51

                         90
                 ....*....|....*..
gi 124249111 117 GTYLCKVKTAPGVAKTT 133
Cdd:cd00096   52 GTYTCVASNSAGGSASA 68

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.

Pssm-ID: 409470 Cd Length: 110 Bit Score: 37.61 E-value: 2.06e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124249111  87 DMRGRVNFTSNGITsgEASIKIRDVQPADSGTYLCKVKTAP-GVAKTTVQLTVV 139
Cdd:cd05887   59 EYQGRVSFKNYSLN--DATITLHNVGFSDSGKYICKAVTFPlGNAQSSTTVTVL 110

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.

Pssm-ID: 409381 Cd Length: 100 Bit Score: 36.99 E-value: 2.69e-03

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 124249111 339 KGRVQFTSNDiRSGEASINITDARLSDAGTYQCGV 373
Cdd:cd05716   52 GGRISLTDDP-DNGVFTVTLNQLRKEDAGWYWCGV 85

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.

Pssm-ID: 409508 Cd Length: 108 Bit Score: 36.92 E-value: 3.03e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMFTfiskdqGPLNIEWLRLSGPNNEAMDHVVI-LYSADKIHDDVYPDLKGRVYFTSNDIksgdaSINITNVQ 237
Cdd:cd16087    8 NETAYLPCQFK------NPQNISLSELVVFWQDQKKLVLYeLYLGKEKLDNVNSKYIGRTSFDQENW-----TLQLHNVQ 76


                 ....*....
gi 124249111 238 LSDAGTYQC 246
Cdd:cd16087   77 IKDQGTYQC 85

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.

Pssm-ID: 409538 Cd Length: 102 Bit Score: 36.75 E-value: 3.24e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 146 SITTPEQTIEKDQGETVHLPCMFTfisKDQGPLNIEWLRLSGpnneamDHVVILYSADKIHDDvypdLKGRVYFTsndik 225
Cdd:cd20946    1 TVPSSQQVVTVVENQEVILSCKTP---KKTSSPRVEWKKLQR------DVTFVVFQNNKIQGD----YKGRAEIL----- 62

                         90       100
                 ....*....|....*....|...
gi 124249111 226 sgDASINITNVQLSDAGTYQCKV 248
Cdd:cd20946   63 --GTNITIKNVTRSDSGKYRCEV 83

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.

Pssm-ID: 409377 Cd Length: 119 Bit Score: 37.37 E-value: 3.28e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111  21 SITTPEQ-TIQEvqGETVHLPCMFTLSPEDQGPLDIE--WLRlsGPNNEAMDHVIILYAVDKIYSDFYqdmRGRVNFTSN 97
Cdd:cd05712    2 GLQMPKSvTVQE--GLCVLIPCSFSYPADYWVSNPVHgyWYR--GGPYPKYRPPVATNNRTREVHEST---QGRFRLLGD 74

                         90       100
                 ....*....|....*....|..
gi 124249111  98 gITSGEASIKIRDVQPADSGTY 119
Cdd:cd05712   75 -PGKKNCSLSISDARPEDSGKY 95

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.

Pssm-ID: 409539 Cd Length: 110 Bit Score: 36.83 E-value: 3.77e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 147 ITTPEQTIEKDQGETVHLPCMFTFISK-DQGPLNIEWlrlsgpnnEAMDHVVILYSADKIHDDV-YPDLKGRVYFTSNDI 224
Cdd:cd20947    1 VTVPKDLYVVEYGSNMTIECKFPVEKQlDLAALIVYW--------EMEDKNIIQFVHGEEDLKVqHSSYRQRARLLKDQL 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 124249111 225 KSGDASINITNVQLSDAGTYQCKVkTYPGTVNRNLQLAV 263
Cdd:cd20947   73 SLGNAALQITDVKLQDAGVYRCMI-SYGGADYKRITVKV 110

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggrecan has a wide distribution in connective tissue and extracellular matrices. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

Pssm-ID: 409481 Cd Length: 123 Bit Score: 36.84 E-value: 4.63e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 159 GETVHLPCMFTF-ISKDQG-----PL--NIEWLRLSgpnnEAMDHVVILYSADKIHddVYPDLKGRVYFTSNDIKSGDAS 230
Cdd:cd05900   12 GSSLLIPCYFQDpIAKDPGaptvaPLspRIKWSFIS----KEKESVLLVATEGKVR--VNTEYLDRVSLPNYPAIPSDAT 85

                         90
                 ....*....|....*...
gi 124249111 231 INITNVQLSDAGTYQCKV 248
Cdd:cd05900   86 LEITELRSNDSGTYRCEV 103

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.

Pssm-ID: 409377 Cd Length: 119 Bit Score: 36.60 E-value: 5.37e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 145 VSITTPEqtiekdqGETVHLPCMFTFISK--DQGPLNIEWLRlsGPNNEAMDHVVILYSADKIhddVYPDLKGRVYFTSn 222
Cdd:cd05712    7 KSVTVQE-------GLCVLIPCSFSYPADywVSNPVHGYWYR--GGPYPKYRPPVATNNRTRE---VHESTQGRFRLLG- 73

                         90       100
                 ....*....|....*....|..
gi 124249111 223 DIKSGDASINITNVQLSDAGTY 244
Cdd:cd05712   74 DPGKKNCSLSISDARPEDSGKY 95

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.

Pssm-ID: 409394 [Multi-domain] Cd Length: 83 Bit Score: 35.46 E-value: 5.90e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249111 275 PEQTIQKARGETVHLPCTFTLSPEDHgplfIDWMQLTGPqnevvnrmfivYLADKI-YDNFYQDMKgrvqftsndirsge 353
Cdd:cd05731    1 SESSTMVLRGGVLLLECIAEGLPTPD----IRWIKLGGE-----------LPKGRTkFENFNKTLK-------------- 51

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 124249111 354 asinITDARLSDAGTYQCGVSHAFGTAKGTIQLTV 388
Cdd:cd05731   52 ----IENVSEADSGEYQCTASNTMGSARHTISVTV 82