NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|130701|sp|P09466|]
View 

RecName: Full=Glycodelin; Short=GD; AltName: Full=Placental protein 14; Short=PP14; AltName: Full=Pregnancy-associated endometrial alpha-2 globulin; Short=PAEG; Short=PEG; AltName: Full=Progestagen-associated endometrial protein; AltName: Full=Progesterone-associated endometrial protein; AltName: Full=Zona-binding inhibitory factor-1; Short=ZIF-1; Flags: Precursor

Protein Classification

lipocalin/fatty-acid binding family protein( domain architecture ID 14443748)

lipocalin/fatty-acid binding family protein such as lipocalins, which are transporters for small hydrophobic molecules, including lipids, steroid hormones, bilins, and retinoids

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
lipocalin_beta-LG-like cd19416
beta-lactoglobulin and similar proteins; Beta-Lactoglobulin (beta-LG) is the major whey ...
21-179 2.62e-94

beta-lactoglobulin and similar proteins; Beta-Lactoglobulin (beta-LG) is the major whey protein of ruminant species and present in the milk of many other species, with a notable exception of human. It is the major allergen of bovine milk. Beta-LG has been shown to bind hydrophobic ligands such as curcumin, vitamin E or fatty acids, or hydrophilic such as vitamin B9. This group also includes human glycodelin (also known as placental protein 14, pregnancy-associated endometrial alpha-2 globulin, and progestagen-associated endometrial protein) which is involved in crucial biological processes such as reproduction and immune reaction. Four glycoforms of glycodelin have been identified in reproductive tissue that differ in glycosylation and biological activity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


:

Pssm-ID: 381191  Cd Length: 160  Bit Score: 270.94  E-value: 2.62e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    21 IPQTKQDLELPKLAGTWHSMAMATNNISLMATLKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKF 100
Cdd:cd19416   1 VTQTMKDLDVQKVAGTWYSLAMAASDISLLDAQSAPLRVYIEELKPTPEGNLEIVLQKWENGRCAEKKLLAEKTKIPAVF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 130701   101 KINYTVANEATLLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGFIRAFRPLPRHLWYLLDLKQMEEPCR 179
Cdd:cd19416  81 KINALNENKVLVLDTDYDSYLLFCMENSAEPEQSLACQCLVRTLEVDNEAMEKFDKALKTLPMHIRLLFNPTQLEEQCH 159
 
Name Accession Description Interval E-value
lipocalin_beta-LG-like cd19416
beta-lactoglobulin and similar proteins; Beta-Lactoglobulin (beta-LG) is the major whey ...
21-179 2.62e-94

beta-lactoglobulin and similar proteins; Beta-Lactoglobulin (beta-LG) is the major whey protein of ruminant species and present in the milk of many other species, with a notable exception of human. It is the major allergen of bovine milk. Beta-LG has been shown to bind hydrophobic ligands such as curcumin, vitamin E or fatty acids, or hydrophilic such as vitamin B9. This group also includes human glycodelin (also known as placental protein 14, pregnancy-associated endometrial alpha-2 globulin, and progestagen-associated endometrial protein) which is involved in crucial biological processes such as reproduction and immune reaction. Four glycoforms of glycodelin have been identified in reproductive tissue that differ in glycosylation and biological activity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381191  Cd Length: 160  Bit Score: 270.94  E-value: 2.62e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    21 IPQTKQDLELPKLAGTWHSMAMATNNISLMATLKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKF 100
Cdd:cd19416   1 VTQTMKDLDVQKVAGTWYSLAMAASDISLLDAQSAPLRVYIEELKPTPEGNLEIVLQKWENGRCAEKKLLAEKTKIPAVF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 130701   101 KINYTVANEATLLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGFIRAFRPLPRHLWYLLDLKQMEEPCR 179
Cdd:cd19416  81 KINALNENKVLVLDTDYDSYLLFCMENSAEPEQSLACQCLVRTLEVDNEAMEKFDKALKTLPMHIRLLFNPTQLEEQCH 159
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
34-175 6.97e-30

Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2). Alignment subsumes both the lipocalin and fatty acid binding protein signatures from PROSITE. This is supported on structural and functional grounds. The structure is an eight-stranded beta barrel.


Pssm-ID: 395015  Cd Length: 143  Bit Score: 106.76  E-value: 6.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701      34 AGTWHSMAMATNNisLMATLKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFKINYTVA---NEA 110
Cdd:pfam00061   1 SGKWYLIASANFN--ELEEEMKALGVGFATIKVLENGNLPVTEITKEGGKCKTVSVTFKKTEEPGKLGVEFDEYaggRKV 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 130701     111 TLLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGFIRAFRPLPRHLWYLLDLKQME 175
Cdd:pfam00061  79 KVLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQKD 143
 
Name Accession Description Interval E-value
lipocalin_beta-LG-like cd19416
beta-lactoglobulin and similar proteins; Beta-Lactoglobulin (beta-LG) is the major whey ...
21-179 2.62e-94

beta-lactoglobulin and similar proteins; Beta-Lactoglobulin (beta-LG) is the major whey protein of ruminant species and present in the milk of many other species, with a notable exception of human. It is the major allergen of bovine milk. Beta-LG has been shown to bind hydrophobic ligands such as curcumin, vitamin E or fatty acids, or hydrophilic such as vitamin B9. This group also includes human glycodelin (also known as placental protein 14, pregnancy-associated endometrial alpha-2 globulin, and progestagen-associated endometrial protein) which is involved in crucial biological processes such as reproduction and immune reaction. Four glycoforms of glycodelin have been identified in reproductive tissue that differ in glycosylation and biological activity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381191  Cd Length: 160  Bit Score: 270.94  E-value: 2.62e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    21 IPQTKQDLELPKLAGTWHSMAMATNNISLMATLKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKF 100
Cdd:cd19416   1 VTQTMKDLDVQKVAGTWYSLAMAASDISLLDAQSAPLRVYIEELKPTPEGNLEIVLQKWENGRCAEKKLLAEKTKIPAVF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 130701   101 KINYTVANEATLLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGFIRAFRPLPRHLWYLLDLKQMEEPCR 179
Cdd:cd19416  81 KINALNENKVLVLDTDYDSYLLFCMENSAEPEQSLACQCLVRTLEVDNEAMEKFDKALKTLPMHIRLLFNPTQLEEQCH 159
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
34-175 6.97e-30

Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2). Alignment subsumes both the lipocalin and fatty acid binding protein signatures from PROSITE. This is supported on structural and functional grounds. The structure is an eight-stranded beta barrel.


Pssm-ID: 395015  Cd Length: 143  Bit Score: 106.76  E-value: 6.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701      34 AGTWHSMAMATNNisLMATLKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFKINYTVA---NEA 110
Cdd:pfam00061   1 SGKWYLIASANFN--ELEEEMKALGVGFATIKVLENGNLPVTEITKEGGKCKTVSVTFKKTEEPGKLGVEFDEYaggRKV 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 130701     111 TLLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGFIRAFRPLPRHLWYLLDLKQME 175
Cdd:pfam00061  79 KVLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQKD 143
lipocalin_9 cd19429
lipocalin 9; Lipocalin 9 (LCN9) is specifically expressed in the epididymis. It belongs to the ...
25-159 6.67e-14

lipocalin 9; Lipocalin 9 (LCN9) is specifically expressed in the epididymis. It belongs to the lipocalin/cytosolic fatty-acid binding protein family. Lipocalins are typically small extracellular proteins that bind small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They are involved in many important functions, like ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior.


Pssm-ID: 381204  Cd Length: 156  Bit Score: 65.63  E-value: 6.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    25 KQDLELPKLAGTWHSMAMATNNISLMATlKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFKINY 104
Cdd:cd19429   5 RRDYNMARISGVWYSISMASDNMTRIEE-NGDLRLFIRNIELLNNGSLQFDFHFMLQGECVAVTVVCEKTKKNGEFSIAY 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 130701   105 TVANEATLLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGFIRAFR 159
Cdd:cd19429  84 EGENKVLLLETDYSMYIIFYLQNIRNGTETQVLALYGRSILLDKTHQRRFENICN 138
lipocalin_FABP cd00301
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
32-142 2.48e-13

lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They have a large beta-barrel ligand-binding cavity. Members include retinol-binding protein, retinoic acid-binding protein, complement protein C8 gamma, Can f 2, apolipoprotein D, extracellular fatty acid-binding protein, beta-lactoglobulin, oderant-binding protein, and bacterial lipocalin Blc. Lipocalins are involved in many important processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty acid-binding proteins also bind hydrophobic ligands in a non-covalent, reversible manner, and are involved in protection and shuttling of fatty acids within the cell, and in acquisition and removal of fatty acids from intracellular sites.


Pssm-ID: 381182  Cd Length: 109  Bit Score: 62.95  E-value: 2.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    32 KLAGTWHSMAMATNNISlmatlKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFKINYTV---AN 108
Cdd:cd00301   1 KFSGKWYEVASASNAPE-----EDEGKCTTAEYTLEGNGNLKVTNSFVRDGVCKSITGTLKKTDGPGKFTVTYPGytgKN 75
                        90       100       110
                ....*....|....*....|....*....|....
gi 130701   109 EATLLDTDYDNFLFLCLQDTTTPIQSMMCQYLAR 142
Cdd:cd00301  76 ELYVLSTDYDNYAIVYSCKNLDGGHTVVAWLLSR 109
lipocalin_L-PGDS cd19419
lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5. ...
22-158 7.46e-11

lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5.3.99.2) is a secreted enzyme and the second most abundant protein in human cerebrospinal fluid. L-PGDS acts as both, an enzyme and as a lipid transporter, converting prostaglandin H2 to prostaglandin D2 and serving as a carrier for hydrophobic ligands including retinoids, hemoglobin metabolites, thyroid hormones, gangliosides, and fatty acids. L-PGDS belongs to the lipocalin/cytosolic fatty-acid binding protein family which has a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381194  Cd Length: 158  Bit Score: 57.36  E-value: 7.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    22 PQTkqDLELPKLAGTWHSMAMATNNiSLMATLKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFK 101
Cdd:cd19419   1 PQP--DFDLDKFAGRWYSVGLASNS-NWFVEKKAKLKMCTTVVAPTTDGNLNLTMTFLKKNGCETRTYLYEKTEQPGRFT 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701   102 ---INYTVANEATLLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGFiRAF 158
Cdd:cd19419  78 yksPRWGSDHDVRVVETNYDEYALVHTIKTKGNEEFTMVTLYSRTQTLRPELKEKF-RQF 136
lipocalin_15-like cd19422
lipocalin 15 and similar proteins, such as chicken CALbeta; This subfamily includes ...
32-154 4.16e-08

lipocalin 15 and similar proteins, such as chicken CALbeta; This subfamily includes uncharacterized human lipocalin 15, and chicken chondrogenesis-associated lipocalin (CAL) beta which is associated with chondrogenesis and inflammation. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381197  Cd Length: 143  Bit Score: 49.86  E-value: 4.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    32 KLAGTWHSMAMATnNISLMATLKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFKINYTVANEAT 111
Cdd:cd19422   1 KFAGLWHVMAMAS-DCPVFLGMKDHMTSSTTAIRPTPEGDLTMHTEFPLPDGCKQIEAEFQKSGQAGHFRVPELGKRDLR 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 130701   112 LLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGF 154
Cdd:cd19422  80 VMDTDYSSYAILYIYKELEGESSTMVQLYTRNQDVSPQLLQKF 122
lipocalin_MUP-like cd19428
major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary ...
24-127 5.28e-07

major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary proteins (MUPs) which bind low molecular weight hydrophobic organic compounds such as urinary volatile pheromones such as the male-specific 2-sec-butyl-4,5-dihydrothiazole (SB2HT) which hastens puberty in female mice. The association between MUPs and these volatiles slows the release of the volatiles into the air from urine marks. MUPs may also act as pheromones themselves. MUPs, expressed in the nasal and vomeronasal mucosa, may be important for delivering urinary volatiles to receptors in the vomeronasal organ. This group includes MUPs encoded by central genes in the MUP cluster, as well as those encoded by peripheral genes such as Darcin/Mup20 which binds most of the male pheromone SB2HT in urine and was the first MUP shown to have male pheromonal activity in its own right. This group includes rat MUPs (also called alpha-2U globulins) and other lipocalins such as major horse allergen Equ c 1 and boar salivary lipocalin, a pheromone-binding protein specifically expressed in the submaxillary glands of the boar. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381203  Cd Length: 158  Bit Score: 47.05  E-value: 5.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    24 TKQDLELPKLAGTWHSMAMATN---NISLMATLKAPLRvHITSLlptpEDNLEIVLHRWENNSCVEKKVLGEKTENPKKF 100
Cdd:cd19428   2 VTRNFDVSKINGEWYSILLASDkreKIEENGSMRVFVE-HIHVL----ENSLAFKFHTKVNGECTELNLVADKTEKAGEY 76
                        90       100
                ....*....|....*....|....*..
gi 130701   101 KINYTVANEATLLDTDYDNFLFLCLQD 127
Cdd:cd19428  77 SVTYDGYNTFTILETDYDNYIMFHLIN 103
lipocalin_5_8-like cd19421
lipocalin similar to human epididymal-specific lipocalin-8, mouse lipocalin-5 and -8, and ...
24-149 4.67e-06

lipocalin similar to human epididymal-specific lipocalin-8, mouse lipocalin-5 and -8, and similar proteins; Lipocalin 5 (LCN5; also known as epididymal retinoic acid binding protein Erabp, mouse epididymal protein 10, MEP10, and E-RABP) and Lipocalin 8 (LCN8; also known as mouse epididymal protein 17, MEP17) are homologous proteins belonging to the epididymis-specific lipocalins; they may play a role in male fertility, and may act as retinoid carrier proteins within the epididymis. In mice, genes encoding the two proteins are contiguous; in humans, there is one gene LCN8 (which has been previously called LCN5). This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381196  Cd Length: 150  Bit Score: 44.52  E-value: 4.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    24 TKQDLELPKLAGTWHSMAMATNnislMAT-LKAPLRVHiTSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFKi 102
Cdd:cd19421   1 VVKDLDISKILGFWYEVAVASD----QGLvLHAEERVE-GLFLTLSGNNLTVKTTYNSSGSCVLEKVTGSEGDGPGKFA- 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 130701   103 nYTVANEATLLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDE 149
Cdd:cd19421  75 -FPGKREIHVLDTDYETYAILDITLLWAGRNFRVLKYFTRSLEDDDG 120
lipocalin_Can_f_2 cd19431
Minor allergen Can f 2; The minor dog lipocalin allergen Can f 2 is an important cause of ...
30-158 3.26e-05

Minor allergen Can f 2; The minor dog lipocalin allergen Can f 2 is an important cause of allergic sensitization in humans worldwide. It is one of two major allergens present in dog dander extracts, and is produced by tongue and the parotid gland (a major salivary gland). Can f 2 belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381206  Cd Length: 162  Bit Score: 42.38  E-value: 3.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    30 LPKLAGTWHSMAMATNNISLMATLkAPLRVHITSlLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFKINYTVANE 109
Cdd:cd19431  12 LEELSGRWHSVALASNKSDLIKPW-GHFRVFIHS-MSAKDGNLHGDILIPQDGQCEKVSLTAFKTATSNKFDLEYWGHND 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 130701   110 ATLLDTDYDNFLFLCLQDTTTPIQSMmcqyLARVLVEDDEIMQGFIRAF 158
Cdd:cd19431  90 LYLAEVDPKSYLILYMINQYNDDTSL----VAHLMVRDLSRQQDFLPAF 134
lipocalin_OBP-like cd19427
Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) ...
30-122 8.31e-05

Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) transport small hydrophobic molecules in the nasal mucosa of vertebrates. This subfamily includes mouse odorant-binding protein 1a (Obp1a), Obp1b, and probasin. Mouse Obp1a and Obp1b, which are expressed in the nasal mucosa, bind the chemical odorant 2-isobutyl-3-methoxypyrazine, and may form a OBPO1a/Opb1B heterodimer. Mouse probasin may play a role in the biology of the prostate gland. This group also includes hamster female-specific lacrimal gland protein (FLP) and aphrodisin. FLP may bind tear lipids or lipid-like pheromones found in hamster tears; aphrodisin is found in hamster vaginal discharge, carries pheromones, and stimulates copulatory behavior in males. This group also includes dog allergen Ca f4 which is expressed by tongue epithelial tissue and found in saliva and dander. Bovine OBP is believed to act as a homodimer, having the C-terminal alpha-helix of each monomer stacking against the beta-barrel of the other monomer; this is possible due to its lack of cysteines and therefore lack of disulfide bonds. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381202  Cd Length: 147  Bit Score: 40.71  E-value: 8.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    30 LPKLAGTWHSMAMATNNISLMATlKAPLRVHITSLLPT-PEDNLEIVLHRWENNSCVEKKVLGEKTENpKKFKINYTVAN 108
Cdd:cd19427   1 LSELSGPWRTIYIAADNVEKIEE-GGPLRTYFREIECDdECQKIKITFYVKKNGQCQETTVVGYKQED-GTYVADYEGQN 78
                        90
                ....*....|....
gi 130701   109 EATLLDTDYDNFLF 122
Cdd:cd19427  79 YFKVVSVSEDALVF 92
lipocalin_C8gamma cd19417
complement protein C8 gamma; Human complement protein C8 gamma, together with C8alpha and ...
23-154 1.02e-03

complement protein C8 gamma; Human complement protein C8 gamma, together with C8alpha and C8beta, form one of five components of the cytolytic membrane attack complex (MAC), a pore-like structure that assembles on bacterial membranes. C8alpha and C8gamma form a disulfide-linked heterodimer that is noncovalently associated with C8beta. MAC plays an important role in the defense against gram-negative bacteria and other pathogenic organisms. C8gamma belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381192  Cd Length: 162  Bit Score: 37.81  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    23 QTKQDLELPKLAGTWHSMAMATNNISLMatlKAPLRVHITSLLPTPE-DNLEIVLHRWENNSCVEKKVLGEKTENPKKFK 101
Cdd:cd19417   1 QPAQNFDIQQFSGKWYLVAVASACRYLQ---ESGHKVEATVLTVAPPkTTVAVSTFRKLNGICWEIKQEYGKTGTLGRFL 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 130701   102 INYTVANEAT---LLDTDYDNFLFLCLQDTttpiQSMMCQYLARVLVEDDEIMQGF 154
Cdd:cd19417  78 LKARRPRGNTdivVGETDYSSYAILYYQRA----GKLTMKLYGRSTELSENILDKF 129
lipocalin_trichosorin-like cd19430
trichosurin and similar proteins; Trichosurin is a protein from the milk whey of the common ...
33-175 1.11e-03

trichosurin and similar proteins; Trichosurin is a protein from the milk whey of the common brushtail possum, Trichosurus Vulpecula, and shows a preference for binding small phenolic ligands. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381205  Cd Length: 153  Bit Score: 37.73  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130701    33 LAGTWHSMAMATNNISLMAtLKAPLRVHITSLlpTPED-NLEIVLHRWENNSCVEKKVLGEKTENPKKFKINYTVANEAT 111
Cdd:cd19430  11 LSRHWHTVVLASSDRSLIE-EEGPFRNFIQNI--TVESgNLNGFFLTRKNGQCIPLYLTAFKTEEARQFKLNYYGTNDVY 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 130701   112 LLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGFIRAFRPLPRHLWYLLDLKQME 175
Cdd:cd19430  88 YESSKPNEYAKFIFYNYHDGKVNVVANLFGRTPNLSNEIKKRFEEDFMNRGFRRENILDISEVD 151
lipocalin_1_3_4_13-like cd19414
lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, ...
29-101 1.20e-03

lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, von ebner's gland protein, or tear specific prealbumin), the main lipid carrier in human tears, is critical to functions involving lipids in protection of the ocular surface. Its large ligand pocket accommodates a range of ligands including alkyl alcohols, glycolipids, phospholipids, cholesterol, steroids, and siderophores. Lipocalin-3 (LCN3, also known as vomeronasal secretory protein 1) and lipocalin-4 (LCN4, also known as vomeronasal secretory protein 2) are involved in transport of lipophilic molecules, and are possibly pheromone-carriers. Lipocalin-13 (LCN13, also known as odorant binding protein 2A) may bind and transport small hydrophobic volatile molecules with a higher affinity for aldehydes and large fatty acids. Another member of this family is late lactation protein B (LLPB), a milk protein produced during the late phase of lactation, which may be involved in transporting a small ligand released during the hydrolysis of milk fat. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381189  Cd Length: 147  Bit Score: 37.69  E-value: 1.20e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 130701    29 ELPKLAGTWHSMAMATN------NISLMATlkaPLRvhITSLlptPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFK 101
Cdd:cd19414   1 EEEDVSGTWYLKAMVVDkefpekRRPRKVS---PVT--VTAL---EGGNLEAKFTFMINGRCEEVKIVLEKTDEPGKYT 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH