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Conserved domains on  [gi|17564684|ref|NP_507234|]
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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 ...
 104-232 8.02e-23

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: 92.28  E-value: 8.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684    104 CAVGFTYINHKCWRLFTDLQTRENADGACMRYGGsTLFSIRNEQENNAMLGFMLN-AGVDNLWTGLICVGKTTfSCTWDM 182
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNsGSSDYYWIGLSDPDSNG-SWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17564684    183 ESGTTSvYNSFASESPDNTYGNCVYFIITGtqaGQWKSGLCNMTMSFVCE 232
Cdd:smart00034  79 GSGPVS-YSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 246-356 3.92e-20

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: 84.96  E-value: 3.92e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684    246 YNNHCYLRYDDSDTVVEAQRFCNTKCANLVSIHSANENRFIQTIYY---VDGYIALGAVAPIIDY-IVWMDGSPQL-YNN 320
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsgSSDYYWIGLSDPDSNGsWQWSDGSGPVsYSN 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 17564684    321 IQ----DNSNGTCVFMrilWGGAGYWYTIDCVKRSWFLCK 356
Cdd:smart00034  88 WApgepNNSSGDCVVL---STSGGKWNDVSCTSKLPFVCE 124
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 104-232 8.02e-23

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: 92.28  E-value: 8.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684    104 CAVGFTYINHKCWRLFTDLQTRENADGACMRYGGsTLFSIRNEQENNAMLGFMLN-AGVDNLWTGLICVGKTTfSCTWDM 182
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNsGSSDYYWIGLSDPDSNG-SWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17564684    183 ESGTTSvYNSFASESPDNTYGNCVYFIITGtqaGQWKSGLCNMTMSFVCE 232
Cdd:smart00034  79 GSGPVS-YSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 246-356 3.92e-20

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: 84.96  E-value: 3.92e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684    246 YNNHCYLRYDDSDTVVEAQRFCNTKCANLVSIHSANENRFIQTIYY---VDGYIALGAVAPIIDY-IVWMDGSPQL-YNN 320
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsgSSDYYWIGLSDPDSNGsWQWSDGSGPVsYSN 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 17564684    321 IQ----DNSNGTCVFMrilWGGAGYWYTIDCVKRSWFLCK 356
Cdd:smart00034  88 WApgepNNSSGDCVVL---STSGGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 114-232 1.42e-14

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: 69.19  E-value: 1.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 114 KCWRLFTDLQTRENADGACMRYGGsTLFSIRNEQENNAMLGFMLNAGVDNLWTGLICVGKTTfSCTWDMESGTTSVYNSF 193
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGG-HLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEG-TWKWSDGSPLVDYTNWA 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17564684 194 ASESPDNTYGNCVYfiITGTQAGQWKSGLCNMTMSFVCE 232
Cdd:cd00037  79 PGEPNPGGSEDCVV--LSSSSDGKWNDVSCSSKLPFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 249-357 1.37e-12

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: 63.79  E-value: 1.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 249 HCYLRYDDSDTVVEAQRFCNTKCANLVSIHSANENRFIQTIYYVDGY----IALGAVAPIIDYiVWMDGSPQL-YNN--- 320
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSsdvwIGLNDLSSEGTW-KWSDGSPLVdYTNwap 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17564684 321 --IQDNSNGTCVFMRilWGGAGYWYTIDCVKRSWFLCKR 357
Cdd:cd00037  80 gePNPGGSEDCVVLS--SSSDGKWNDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 259-357 6.12e-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: 6.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684   259 TVVEAQRFCNTKCANLVSIHSANENRFIQTI---YYVDGYIALGAVaPIIDYIVWMDGSPQLYNNIQ-----DNSNGTCV 330
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTlkkSNKYFWIGLTDR-KNEGTWKWVDGSPVNYTNWApepnnNGENEDCV 81

                          90       100
                  ....*....|....*....|....*..
gi 17564684   331 FMRIlwgGAGYWYTIDCVKRSWFLCKR 357
Cdd:pfam00059  82 ELSS---SSGKWNDENCNSKNPFVCEK 105
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 112-237 1.70e-03

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


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 40.45  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684    112 NHKCWRLFTDLQTRENADGACMRYGGSTLFSIRNEQENNAMLGFMLNAGVDNLWTGLICV-GKTTFSCTWDMESGTTSVY 190
Cdd:TIGR00864  328 NGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDRGVWIGFSDVnGAEKGPAHQGEAFEAEECE 407

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 17564684    191 NSFASESPDNTYGNCVYFiitgTQAGQWKSGLCNMTMSFVCELPPTV 237
Cdd:TIGR00864  408 EGLAGEPHPARAEHCVRL----DPRGQCNSDLCNAPHAYVCELNPGG 450
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 104-232 8.02e-23

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: 92.28  E-value: 8.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684    104 CAVGFTYINHKCWRLFTDLQTRENADGACMRYGGsTLFSIRNEQENNAMLGFMLN-AGVDNLWTGLICVGKTTfSCTWDM 182
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNsGSSDYYWIGLSDPDSNG-SWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17564684    183 ESGTTSvYNSFASESPDNTYGNCVYFIITGtqaGQWKSGLCNMTMSFVCE 232
Cdd:smart00034  79 GSGPVS-YSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 246-356 3.92e-20

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: 84.96  E-value: 3.92e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684    246 YNNHCYLRYDDSDTVVEAQRFCNTKCANLVSIHSANENRFIQTIYY---VDGYIALGAVAPIIDY-IVWMDGSPQL-YNN 320
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsgSSDYYWIGLSDPDSNGsWQWSDGSGPVsYSN 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 17564684    321 IQ----DNSNGTCVFMrilWGGAGYWYTIDCVKRSWFLCK 356
Cdd:smart00034  88 WApgepNNSSGDCVVL---STSGGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 114-232 1.42e-14

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: 69.19  E-value: 1.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 114 KCWRLFTDLQTRENADGACMRYGGsTLFSIRNEQENNAMLGFMLNAGVDNLWTGLICVGKTTfSCTWDMESGTTSVYNSF 193
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGG-HLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEG-TWKWSDGSPLVDYTNWA 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17564684 194 ASESPDNTYGNCVYfiITGTQAGQWKSGLCNMTMSFVCE 232
Cdd:cd00037  79 PGEPNPGGSEDCVV--LSSSSDGKWNDVSCSSKLPFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 249-357 1.37e-12

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: 63.79  E-value: 1.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 249 HCYLRYDDSDTVVEAQRFCNTKCANLVSIHSANENRFIQTIYYVDGY----IALGAVAPIIDYiVWMDGSPQL-YNN--- 320
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSsdvwIGLNDLSSEGTW-KWSDGSPLVdYTNwap 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17564684 321 --IQDNSNGTCVFMRilWGGAGYWYTIDCVKRSWFLCKR 357
Cdd:cd00037  80 gePNPGGSEDCVVLS--SSSDGKWNDVSCSSKLPFICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 246-356 1.98e-09

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: 55.44  E-value: 1.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 246 YNNHCYLRYDDSDTVVEAQRFCNT-----KCANLVSIHSANENRFIQTIYyvdgyiaLGAVAPIIDY------------- 307
Cdd:cd03589   8 FGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLF-------ESSRGPDTPYglwiglhdrtseg 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17564684 308 -IVWMDGSPQLYNNIQ----DNSNGT--CVFMRiLWGGAGY-WYTIDCVKRSWFLCK 356
Cdd:cd03589  81 pFEWTDGSPVDFTKWAggqpDNYGGNedCVQMW-RRGDAGQsWNDMPCDAVFPYICK 136
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 104-233 7.45e-09

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: 53.52  E-value: 7.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 104 CAVGFTYINHKCWRLFTDLQTRENADGACMRYGGST----LFSIRNEQENNAMLGFMLNAGVDN----LWTGLicvGKTT 175
Cdd:cd03589   1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSIPGliahLVSIHSQEENDFVYDLFESSRGPDtpygLWIGL---HDRT 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 176 FSCTWDMESGTTSVYNSFASESPDNTYGN--CVYFIITGTQAGQWKSGLCNMTMSFVCEL 233
Cdd:cd03589  78 SEGPFEWTDGSPVDFTKWAGGQPDNYGGNedCVQMWRRGDAGQSWNDMPCDAVFPYICKM 137
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 259-357 6.12e-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: 6.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684   259 TVVEAQRFCNTKCANLVSIHSANENRFIQTI---YYVDGYIALGAVaPIIDYIVWMDGSPQLYNNIQ-----DNSNGTCV 330
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTlkkSNKYFWIGLTDR-KNEGTWKWVDGSPVNYTNWApepnnNGENEDCV 81

                          90       100
                  ....*....|....*....|....*..
gi 17564684   331 FMRIlwgGAGYWYTIDCVKRSWFLCKR 357
Cdd:pfam00059  82 ELSS---SSGKWNDENCNSKNPFVCEK 105
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 244-357 6.42e-08

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: 50.65  E-value: 6.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 244 NNYNNHCYLRYDDSDTVVEAQRFCNTKCANLVSIHSANENRFIQTIYYVDGYIALGAVAPIIDYiVWMDGSPQLYNNIQD 323
Cdd:cd03588   6 DKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDF-RWSDGHPLQFENWRP 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17564684 324 N-------SNGTCVFMriLWGGAGYWYTIDCVKRSWFLCKR 357
Cdd:cd03588  85 NqpdnffaTGEDCVVM--IWHEEGEWNDVPCNYHLPFTCKK 123
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 251-355 5.99e-07

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: 47.37  E-value: 5.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 251 YLRYDDSDTVVEAQRFCNTKCANLVSIHSANENRFIQT---IYYVDGYIALgavAPIIDYIVWMDGSPQLY---NNIQDN 324
Cdd:cd03602   3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNlsrVSNSAAWIGL---YRDVDSWRWSDGSESSFrnwNTFQPF 79

                        90       100       110
                ....*....|....*....|....*....|.
gi 17564684 325 SNGTCVFMRIlwggAGYWYTIDCVKRSWFLC 355
Cdd:cd03602  80 GQGDCATMYS----SGRWYAALCSALKPFIC 106
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 104-232 5.56e-06

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: 45.26  E-value: 5.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 104 CAVGFTYINHKCWRLFTDLQTRENADGACmRYGGSTLFSIRNEQENNamlgFMLNAGVDNLWTGLicvGKTTFSCTWDME 183
Cdd:cd03588   1 CEEGWDKFQGHCYRHFPDRETWEDAERRC-REQQGHLSSIVTPEEQE----FVNNNAQDYQWIGL---NDRTIEGDFRWS 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17564684 184 SGTTSVYNSFASESPDNTYG---NCVYFIitGTQAGQWKSGLCNMTMSFVCE 232
Cdd:cd03588  73 DGHPLQFENWRPNQPDNFFAtgeDCVVMI--WHEEGEWNDVPCNYHLPFTCK 122
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 259-357 7.10e-05

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


Pssm-ID: 153062  Cd Length: 115  Bit Score: 41.59  E-value: 7.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 259 TVVEAQRFCNTKCANLVSIHSANENRFI--------QTIYYVDG------YIALGAVAPIIDYIVWMDGSPqlyNNiqdN 324
Cdd:cd03592  11 TFNEAVKYCKSRGTDLVAIQNAEENALLngfalkynLGYYWIDGndinneGTWVDTDKKELEYKNWAPGEP---NN---G 84

                        90       100       110
                ....*....|....*....|....*....|...
gi 17564684 325 SNGTCVFMRILwgGAGYWYTIDCVKRSWFLCKR 357
Cdd:cd03592  85 RNENCLEIYIK--DNGKWNDEPCSKKKSAICYT 115
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 246-357 1.11e-04

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 41.16  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 246 YNNHCYLRYDDSDTVVEAQRFCNTKCANLVSIHSANENRFIQTIYYVDGY-IALgAVAPIIDYIVWMDGSP--QLYNNIQ 322
Cdd:cd03593   8 YGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYwIGL-SREKSEKPWKWIDGSPlnNLFNIRG 86

                        90       100       110
                ....*....|....*....|....*....|....*
gi 17564684 323 DNSNGTCVFMrilwgGAGYWYTIDCVKRSWFLCKR 357
Cdd:cd03593  87 STKSGNCAYL-----SSTGIYSEDCSTKKRWICEK 116
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 132-233 2.94e-04

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: 39.97  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 132 CMRYGGsTLFSIRNEQENNAMLGFmLNAGVDNLWTGLIcvgkttfsctwDME--------SGTTSVYNSFASESPDNTYG 203
Cdd:cd03591  20 CSEAGG-TLAMPRNAAENAAIASY-VKKGNTYAFIGIT-----------DLEtegqfvylDGGPLTYTNWKPGEPNNAGG 86

                        90       100       110
                ....*....|....*....|....*....|..
gi 17564684 204 --NCVYfIITGtqaGQWKSGLCNMTMSFVCEL 233
Cdd:cd03591  87 geDCVE-MYTS---GKWNDVACNLTRLFVCEF 114
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 104-232 4.44e-04

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: 39.66  E-value: 4.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 104 CAVGFTYINHKCWRLFTDLQTRENADGACMRYG-GSTLFSIRNEQENNAMLGFMLNAGV--DNLWTGLicvGKTTFSCTW 180
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGpGAHLASIHSPAEAAAIASLISSYQKayQPVWIGL---HDPQQSRGW 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17564684 181 DMESGTTSVYNSFASESPDNTYGNCVyfIITGTQAGQ-WKSGLCNMTMSFVCE 232
Cdd:cd03594  78 EWSDGSKLDYRSWDRNPPYARGGYCA--ELSRSTGFLkWNDANCEERNPFICK 128
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 109-232 8.76e-04

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


Pssm-ID: 153066  Cd Length: 129  Bit Score: 38.91  E-value: 8.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684 109 TYINHKCWRLFTDLQTRENADGACMRYGGsTLFSIRNEQENNAMLGFMLNA--GVDNLWTGlicVGKTTFSCTWDMESGT 186
Cdd:cd03596   5 TKIHKKCYLVSEETKHYHEASEDCIARGG-TLATPRDSDENDALRDYVKASvpGNWEVWLG---INDMVAEGKWVDVNGS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17564684 187 TSVYNSFASESPDNTYG----NCVYFiiTGTQAGQWKSGLCNMTMSFVCE 232
Cdd:cd03596  81 PISYFNWEREITAQPDGgkreNCVAL--SSSAQGKWFDEDCRREKPYVCE 128
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 112-237 1.70e-03

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


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 40.45  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564684    112 NHKCWRLFTDLQTRENADGACMRYGGSTLFSIRNEQENNAMLGFMLNAGVDNLWTGLICV-GKTTFSCTWDMESGTTSVY 190
Cdd:TIGR00864  328 NGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDRGVWIGFSDVnGAEKGPAHQGEAFEAEECE 407

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 17564684    191 NSFASESPDNTYGNCVYFiitgTQAGQWKSGLCNMTMSFVCELPPTV 237
Cdd:TIGR00864  408 EGLAGEPHPARAEHCVRL----DPRGQCNSDLCNAPHAYVCELNPGG 450
 
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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