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Conserved domains on  [gi|72000942|ref|NP_507257|]
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C-type lectin domain-containing protein [Caenorhabditis elegans]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10636995)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

CATH:  3.10.100.10
Gene Ontology:  GO:0030246|GO:0120153
PubMed:  16336259|10508765
SCOP:  4002453

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 109-237 5.07e-25

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 98.06  E-value: 5.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942    109 CTDGFTYINNKCWKLVTSSQSRADADQACYNLGGsTLFSIRSDQENQAVLDFVKNE-NVDNLWTGLICDDHGQFlCTWDv 187
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNSgSSDYYWIGLSDPDSNGS-WQWS- 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 72000942    188 DSGDISAYNNFAKTYPNNVTGGCIYYMTTGsqaGQWTNGACNKALSFVCE 237
Cdd:smart00034  78 DGSGPVSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 251-357 4.54e-17

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 76.48  E-value: 4.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942    251 YNNYCYITNDQLKISSDAQQICTSSGSNLVSIHSANENRFLTTIYSP-----PVLVGGVAFSSN-LILWYDGTPST-FNN 323
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgssdYYWIGLSDPDSNgSWQWSDGSGPVsYSN 87

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 72000942    324 IKSI----TNGNCLFINDTHGGWYGFDCFTGSGdFICK 357
Cdd:smart00034  88 WAPGepnnSSGDCVVLSTSGGKWNDVSCTSKLP-FVCE 124
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 109-237 5.07e-25

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 98.06  E-value: 5.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942    109 CTDGFTYINNKCWKLVTSSQSRADADQACYNLGGsTLFSIRSDQENQAVLDFVKNE-NVDNLWTGLICDDHGQFlCTWDv 187
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNSgSSDYYWIGLSDPDSNGS-WQWS- 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 72000942    188 DSGDISAYNNFAKTYPNNVTGGCIYYMTTGsqaGQWTNGACNKALSFVCE 237
Cdd:smart00034  78 DGSGPVSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 251-357 4.54e-17

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 76.48  E-value: 4.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942    251 YNNYCYITNDQLKISSDAQQICTSSGSNLVSIHSANENRFLTTIYSP-----PVLVGGVAFSSN-LILWYDGTPST-FNN 323
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgssdYYWIGLSDPDSNgSWQWSDGSGPVsYSN 87

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 72000942    324 IKSI----TNGNCLFINDTHGGWYGFDCFTGSGdFICK 357
Cdd:smart00034  88 WAPGepnnSSGDCVVLSTSGGKWNDVSCTSKLP-FVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 119-237 2.02e-16

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 74.58  E-value: 2.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 119 KCWKLVTSSQSRADADQACYNLGGsTLFSIRSDQENQAVLDFVKNENVDNLWTGLICDDH-GQFlcTWdVDSGDISAYNN 197
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGG-HLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSeGTW--KW-SDGSPLVDYTN 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 72000942 198 FAKTYPNNVTGG-CIYYmtTGSQAGQWTNGACNKALSFVCE 237
Cdd:cd00037  77 WAPGEPNPGGSEdCVVL--SSSSDGKWNDVSCSSKLPFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 254-358 1.99e-10

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 57.63  E-value: 1.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 254 YCYITNDQLKISSDAQQICTSSGSNLVSIHSANENRFLTTI----YSPPVLVGGVAFSSNLI-LWYDGTP-STFNNIKSI 327
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLlkksSSSDVWIGLNDLSSEGTwKWSDGSPlVDYTNWAPG 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 72000942 328 -----TNGNCLFIN-DTHGGWYGFDCFTGSGdFICKQ 358
Cdd:cd00037  81 epnpgGSEDCVVLSsSSDGKWNDVSCSSKLP-FICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 131-237 6.18e-08

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 50.17  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942   131 ADADQACYNLGGStLFSIRSDQENQAVLDFVKNENVDnLWTGLICDDHGQflcTWDVDSGDISAYNNFAKTYPNNVTGGC 210
Cdd:pfam00059   5 DEAREACRKLGGH-LVSINSAEELDFLSSTLKKSNKY-FWIGLTDRKNEG---TWKWVDGSPVNYTNWAPEPNNNGENED 79

                          90       100
                  ....*....|....*....|....*..
gi 72000942   211 IYYMTTGSqaGQWTNGACNKALSFVCE 237
Cdd:pfam00059  80 CVELSSSS--GKWNDENCNSKNPFVCE 104
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 267-358 1.88e-03

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 37.46  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942   267 DAQQICTSSGSNLVSIHSANENRFLTTIYSPPvlvgGVAF--------SSNLILWYDGTPSTFNNIK-----SITNGNCL 333
Cdd:pfam00059   6 EAREACRKLGGHLVSINSAEELDFLSSTLKKS----NKYFwigltdrkNEGTWKWVDGSPVNYTNWApepnnNGENEDCV 81

                          90       100
                  ....*....|....*....|....*
gi 72000942   334 FINDTHGGWYGFDCFTGSGdFICKQ 358
Cdd:pfam00059  82 ELSSSSGKWNDENCNSKNP-FVCEK 105
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 109-237 5.07e-25

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 98.06  E-value: 5.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942    109 CTDGFTYINNKCWKLVTSSQSRADADQACYNLGGsTLFSIRSDQENQAVLDFVKNE-NVDNLWTGLICDDHGQFlCTWDv 187
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNSgSSDYYWIGLSDPDSNGS-WQWS- 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 72000942    188 DSGDISAYNNFAKTYPNNVTGGCIYYMTTGsqaGQWTNGACNKALSFVCE 237
Cdd:smart00034  78 DGSGPVSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 251-357 4.54e-17

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 76.48  E-value: 4.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942    251 YNNYCYITNDQLKISSDAQQICTSSGSNLVSIHSANENRFLTTIYSP-----PVLVGGVAFSSN-LILWYDGTPST-FNN 323
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgssdYYWIGLSDPDSNgSWQWSDGSGPVsYSN 87

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 72000942    324 IKSI----TNGNCLFINDTHGGWYGFDCFTGSGdFICK 357
Cdd:smart00034  88 WAPGepnnSSGDCVVLSTSGGKWNDVSCTSKLP-FVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 119-237 2.02e-16

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 74.58  E-value: 2.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 119 KCWKLVTSSQSRADADQACYNLGGsTLFSIRSDQENQAVLDFVKNENVDNLWTGLICDDH-GQFlcTWdVDSGDISAYNN 197
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGG-HLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSeGTW--KW-SDGSPLVDYTN 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 72000942 198 FAKTYPNNVTGG-CIYYmtTGSQAGQWTNGACNKALSFVCE 237
Cdd:cd00037  77 WAPGEPNPGGSEdCVVL--SSSSDGKWNDVSCSSKLPFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 254-358 1.99e-10

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 57.63  E-value: 1.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 254 YCYITNDQLKISSDAQQICTSSGSNLVSIHSANENRFLTTI----YSPPVLVGGVAFSSNLI-LWYDGTP-STFNNIKSI 327
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLlkksSSSDVWIGLNDLSSEGTwKWSDGSPlVDYTNWAPG 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 72000942 328 -----TNGNCLFIN-DTHGGWYGFDCFTGSGdFICKQ 358
Cdd:cd00037  81 epnpgGSEDCVVLSsSSDGKWNDVSCSSKLP-FICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 131-237 6.18e-08

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 50.17  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942   131 ADADQACYNLGGStLFSIRSDQENQAVLDFVKNENVDnLWTGLICDDHGQflcTWDVDSGDISAYNNFAKTYPNNVTGGC 210
Cdd:pfam00059   5 DEAREACRKLGGH-LVSINSAEELDFLSSTLKKSNKY-FWIGLTDRKNEG---TWKWVDGSPVNYTNWAPEPNNNGENED 79

                          90       100
                  ....*....|....*....|....*..
gi 72000942   211 IYYMTTGSqaGQWTNGACNKALSFVCE 237
Cdd:pfam00059  80 CVELSSSS--GKWNDENCNSKNPFVCE 104
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 109-237 9.73e-07

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


Pssm-ID: 153066  Cd Length: 129  Bit Score: 47.38  E-value: 9.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 109 CTDGfTYINNKCWKLVTSSQSRADADQACYNLGGsTLFSIRSDQENQAVLDFVKNE--NVDNLWTGlICD--DHGQFLct 184
Cdd:cd03596   1 CLKG-TKIHKKCYLVSEETKHYHEASEDCIARGG-TLATPRDSDENDALRDYVKASvpGNWEVWLG-INDmvAEGKWV-- 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 72000942 185 wDVDSGDISaYNNFAKTYPNNVTGG----CIYYmtTGSQAGQWTNGACNKALSFVCE 237
Cdd:cd03596  76 -DVNGSPIS-YFNWEREITAQPDGGkrenCVAL--SSSAQGKWFDEDCRREKPYVCE 128
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 131-238 1.98e-06

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


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 46.14  E-value: 1.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 131 ADADQACYNLGGsTLFSIRSDQENQAVLDFVKNENvDNLWTGlICDD--HGQFLctwDVDSGDISaYNNFAKTYPNNVTG 208
Cdd:cd03591  14 DDAQKLCSEAGG-TLAMPRNAAENAAIASYVKKGN-TYAFIG-ITDLetEGQFV---YLDGGPLT-YTNWKPGEPNNAGG 86

                        90       100       110
                ....*....|....*....|....*....|..
gi 72000942 209 G--CIYYMTTGsqagQWTNGACNKALSFVCEL 238
Cdd:cd03591  87 GedCVEMYTSG----KWNDVACNLTRLFVCEF 114
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 109-237 4.80e-05

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


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 42.74  E-value: 4.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 109 CTDGFTYINNKCWKLVTSSQSRADADQACYNLG-GSTLFSIRSDQENQAVLDFVKN--ENVDNLWTGLICDDHGQflcTW 185
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGpGAHLASIHSPAEAAAIASLISSyqKAYQPVWIGLHDPQQSR---GW 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 72000942 186 DVDSGDISAYNNFAKTYPNNVTGGCIyYMTTGSQAGQWTNGACNKALSFVCE 237
Cdd:cd03594  78 EWSDGSKLDYRSWDRNPPYARGGYCA-ELSRSTGFLKWNDANCEERNPFICK 128
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 118-236 6.55e-05

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 42.05  E-value: 6.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 118 NKCWKLVTSSQSRADADQACYNLGGSTLFSIRSDQENQAVLDFVKNENVDNLWTGLICDDHG---QFlcTWdVDsGDISA 194
Cdd:cd03598   1 GRCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGrcrRF--SW-VD-GSVWN 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 72000942 195 YNNFAKTYPNNVTGGCIYYMTTGsqaGQWTNGACNKALSFVC 236
Cdd:cd03598  77 YAYWAPGQPGNRRGHCVELCTRG---GHWRRAHCKLRRPFIC 115
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 109-238 7.30e-05

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 42.35  E-value: 7.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 109 CTDGFTYINNKCWKLVTSSQSRADADQAC--YNLGG--STLFSIRSDQENQAVLDFVKNENVDN----LWTGLicDDH-- 178
Cdd:cd03589   1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCrsFSIPGliAHLVSIHSQEENDFVYDLFESSRGPDtpygLWIGL--HDRts 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72000942 179 -GQFlcTW-DVDSGDisaYNNFAKTYPNNVTGG--CIYYMTTGSQAGQWTNGACNKALSFVCEL 238
Cdd:cd03589  79 eGPF--EWtDGSPVD---FTKWAGGQPDNYGGNedCVQMWRRGDAGQSWNDMPCDAVFPYICKM 137
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 251-357 7.66e-05

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 42.35  E-value: 7.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 251 YNNYCYITNDQLKISSDAQQICTSSGSN-----LVSIHSANENRFLTTIY---SPPVLVGGVAF------SSNLILWYDG 316
Cdd:cd03589   8 FGGYCYRFFGDRLTWEEAELRCRSFSIPgliahLVSIHSQEENDFVYDLFessRGPDTPYGLWIglhdrtSEGPFEWTDG 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 72000942 317 TPSTFNNIK------SITNGNCLFI---NDTHGGWYGFDCfTGSGDFICK 357
Cdd:cd03589  88 SPVDFTKWAggqpdnYGGNEDCVQMwrrGDAGQSWNDMPC-DAVFPYICK 136
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 256-356 6.36e-04

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 38.89  E-value: 6.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 256 YITNDQLKISSDAQQICTSSGSNLVSIHSANENRFLTTIY--SPPVLVGGVAFSSNLILWYDGTPSTFNNIKSIT---NG 330
Cdd:cd03602   3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSrvSNSAAWIGLYRDVDSWRWSDGSESSFRNWNTFQpfgQG 82

                        90       100
                ....*....|....*....|....*.
gi 72000942 331 NCLFINDThGGWYGFDCfTGSGDFIC 356
Cdd:cd03602  83 DCATMYSS-GRWYAALC-SALKPFIC 106
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 249-357 1.22e-03

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


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 38.44  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 249 YNYNNYCYITNDQLKISSDAQQICTSSGSNLVSIHSANENRFLTTIysppvLVGGVAF--------SSNLILWYDGTP-- 318
Cdd:cd03590   6 KSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKI-----LSGNRSYwiglsdeeTEGEWKWVDGTPln 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 72000942 319 --STF------NNIKSiTNGNCLFINDTHGGWYGFDCFTgSGDFICK 357
Cdd:cd03590  81 ssKTFwhpgepNNWGG-GGEDCAELVYDSGGWNDVPCNL-EYRWICE 125
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 267-358 1.88e-03

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 37.46  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942   267 DAQQICTSSGSNLVSIHSANENRFLTTIYSPPvlvgGVAF--------SSNLILWYDGTPSTFNNIK-----SITNGNCL 333
Cdd:pfam00059   6 EAREACRKLGGHLVSINSAEELDFLSSTLKKS----NKYFwigltdrkNEGTWKWVDGSPVNYTNWApepnnNGENEDCV 81

                          90       100
                  ....*....|....*....|....*
gi 72000942   334 FINDTHGGWYGFDCFTGSGdFICKQ 358
Cdd:pfam00059  82 ELSSSSGKWNDENCNSKNP-FVCEK 105
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 109-237 3.30e-03

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 37.17  E-value: 3.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 109 CTDGFTYINNKCWKLVTSSQSRADADQACyNLGGSTLFSIRSDQENQavldFVKNENVDNLWTGLicDD---HGQFlcTW 185
Cdd:cd03588   1 CEEGWDKFQGHCYRHFPDRETWEDAERRC-REQQGHLSSIVTPEEQE----FVNNNAQDYQWIGL--NDrtiEGDF--RW 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 72000942 186 DvdSGDISAYNNFAKTYPNN--VTG-GCIyyMTTGSQAGQWTNGACNKALSFVCE 237
Cdd:cd03588  72 S--DGHPLQFENWRPNQPDNffATGeDCV--VMIWHEEGEWNDVPCNYHLPFTCK 122
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 120-237 8.85e-03

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


Pssm-ID: 153065  Cd Length: 149  Bit Score: 36.41  E-value: 8.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000942 120 CWKLVTSSQSR-----ADADQACYNLGGStLFSIRSDQENQAVLDFVKNENVDN--LWTGLICDDHGQFLCTWDVD---- 188
Cdd:cd03595  12 CYKIAYFQDSRrrlnfEEARQACREDGGE-LLSIESENEQKLIERFIQTLRASDgdFWIGLRRSSQYNVTSSACSSlyyw 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 72000942 189 -SGDISAYNNFAKTYPNNVTGGCI--YYMTTGS--QAG----QWTNGACNKALSFVCE 237
Cdd:cd03595  91 lDGSISTFRNWYVDEPSCGSEVCVvmYHQPSAPagQGGpylfQWNDDNCNMKNNFICK 148
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 109-173 9.29e-03

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


Pssm-ID: 153067  Cd Length: 129  Bit Score: 36.02  E-value: 9.29e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72000942 109 CTDGFTYINNKCWKLVTSSQSRADADQACYNLGGsTLFSIRSDQENQAVLDFVKNENVDNL----WTGL 173
Cdd:cd03597   1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNA-VLASLTTQKKVEFVLKELQKHQMTKQkltpWVGL 68
 
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.
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