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Conserved domains on  [gi|225903411|ref|NP_742074|]
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regenerating islet-derived protein 3-alpha precursor [Rattus norvegicus]

Protein Classification

C-type lectin-like domain-containing protein( domain architecture ID 96)

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

PubMed:  16336259|10508765

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT super family cl02432
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 39-172 2.15e-46

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.


The actual alignment was detected with superfamily member cd03594:

Pssm-ID: 470576 [Multi-domain]  Cd Length: 129  Bit Score: 147.90  E-value: 2.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  39 CPMGSKAYRSYCYTLVTTLKSWFQADLACQKR-PSGHLVSILSGGEASFVSSLVTGRVNNNQDIWIGLHDPTMGQqpngg 117
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSR----- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225903411 118 GWEWSNSDVLNYLNWDGDPSSTvNRGNCGSLTATSEFLKWGDHHCDVELPFVCKF 172
Cdd:cd03594   76 GWEWSDGSKLDYRSWDRNPPYA-RGGYCAELSRSTGFLKWNDANCEERNPFICKY 129
 
Name Accession Description Interval E-value
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 39-172 2.15e-46

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: 147.90  E-value: 2.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  39 CPMGSKAYRSYCYTLVTTLKSWFQADLACQKR-PSGHLVSILSGGEASFVSSLVTGRVNNNQDIWIGLHDPTMGQqpngg 117
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSR----- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225903411 118 GWEWSNSDVLNYLNWDGDPSSTvNRGNCGSLTATSEFLKWGDHHCDVELPFVCKF 172
Cdd:cd03594   76 GWEWSDGSKLDYRSWDRNPPYA-RGGYCAELSRSTGFLKWNDANCEERNPFICKY 129
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 39-171 4.55e-28

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: 101.14  E-value: 4.55e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411    39 CPMGSKAYRSYCYTLVTTLKSWFQADLACQKRpSGHLVSILSGGEASFVSSLVTgRVNNNQDIWIGLHDPTmgqqpNGGG 118
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSL-GGHLASIHSEAENDFVASLLK-NSGSSDYYWIGLSDPD-----SNGS 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 225903411   119 WEWSN-SDVLNYLNWDgDPSSTVNRGNCGSLTATSefLKWGDHHCDVELPFVCK 171
Cdd:smart00034  74 WQWSDgSGPVSYSNWA-PGEPNNSSGDCVVLSTSG--GKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 58-172 3.56e-26

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 96.01  E-value: 3.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411   58 KSWFQADLACQKrPSGHLVSILSGGEASFVSSLVTgrvNNNQDIWIGLHDptmgqQPNGGGWEWSNSDVLNYLNWDGDPS 137
Cdd:pfam00059   2 KTWDEAREACRK-LGGHLVSINSAEELDFLSSTLK---KSNKYFWIGLTD-----RKNEGTWKWVDGSPVNYTNWAPEPN 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 225903411  138 STVNRGNCGSLTATSefLKWGDHHCDVELPFVCKF 172
Cdd:pfam00059  73 NNGENEDCVELSSSS--GKWNDENCNSKNPFVCEK 105
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 25-173 6.47e-06

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: 45.46  E-value: 6.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411    25 GEDSQKAVPSTrtsCPMGSKAY--RSYCYTLVTTLKSWFQADLACQKRPSGHLVSILSGGEASFVSSLVTGRVnnNQDIW 102
Cdd:TIGR00864  307 GEEPAKASHPH---CPKDGEIFeeNGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSL--DRGVW 381

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225903411   103 IGLHD---PTMGQQPNGGGWEWSNSDvlnylNWDGdPSSTVNRGN-CGSLTATSEFlkwGDHHCDVELPFVCKFK 173
Cdd:TIGR00864  382 IGFSDvngAEKGPAHQGEAFEAEECE-----EGLA-GEPHPARAEhCVRLDPRGQC---NSDLCNAPHAYVCELN 447
 
Name Accession Description Interval E-value
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 39-172 2.15e-46

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: 147.90  E-value: 2.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  39 CPMGSKAYRSYCYTLVTTLKSWFQADLACQKR-PSGHLVSILSGGEASFVSSLVTGRVNNNQDIWIGLHDPTMGQqpngg 117
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSR----- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225903411 118 GWEWSNSDVLNYLNWDGDPSSTvNRGNCGSLTATSEFLKWGDHHCDVELPFVCKF 172
Cdd:cd03594   76 GWEWSDGSKLDYRSWDRNPPYA-RGGYCAELSRSTGFLKWNDANCEERNPFICKY 129
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 39-171 4.55e-28

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: 101.14  E-value: 4.55e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411    39 CPMGSKAYRSYCYTLVTTLKSWFQADLACQKRpSGHLVSILSGGEASFVSSLVTgRVNNNQDIWIGLHDPTmgqqpNGGG 118
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSL-GGHLASIHSEAENDFVASLLK-NSGSSDYYWIGLSDPD-----SNGS 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 225903411   119 WEWSN-SDVLNYLNWDgDPSSTVNRGNCGSLTATSefLKWGDHHCDVELPFVCK 171
Cdd:smart00034  74 WQWSDgSGPVSYSNWA-PGEPNNSSGDCVVLSTSG--GKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 58-172 3.56e-26

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 96.01  E-value: 3.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411   58 KSWFQADLACQKrPSGHLVSILSGGEASFVSSLVTgrvNNNQDIWIGLHDptmgqQPNGGGWEWSNSDVLNYLNWDGDPS 137
Cdd:pfam00059   2 KTWDEAREACRK-LGGHLVSINSAEELDFLSSTLK---KSNKYFWIGLTD-----RKNEGTWKWVDGSPVNYTNWAPEPN 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 225903411  138 STVNRGNCGSLTATSefLKWGDHHCDVELPFVCKF 172
Cdd:pfam00059  73 NNGENEDCVELSSSS--GKWNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 49-172 2.29e-25

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 94.22  E-value: 2.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  49 YCYTLVTTLKSWFQADLACQKRpSGHLVSILSGGEASFVSSLVtgRVNNNQDIWIGLHDptmgqQPNGGGWEWSN-SDVL 127
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLL--KKSSSSDVWIGLND-----LSSEGTWKWSDgSPLV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 225903411 128 NYLNWDGDPSSTVNRGNCGSLTATSEFlKWGDHHCDVELPFVCKF 172
Cdd:cd00037   73 DYTNWAPGEPNPGGSEDCVVLSSSSDG-KWNDVSCSSKLPFICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 39-171 7.20e-20

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: 80.48  E-value: 7.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  39 CPMGSKAYRSYCYTLVTTLKSWFQADLACQK----RPSGHLVSILSGGEASFVSSLVTGRVNNNQ--DIWIGLHDPTmgq 112
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipGLIAHLVSIHSQEENDFVYDLFESSRGPDTpyGLWIGLHDRT--- 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225903411 113 qpNGGGWEWSNSDVLNYLNWD-GDPSSTVNRGNCGSLTATSEFL-KWGDHHCDVELPFVCK 171
Cdd:cd03589   78 --SEGPFEWTDGSPVDFTKWAgGQPDNYGGNEDCVQMWRRGDAGqSWNDMPCDAVFPYICK 136
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 39-171 3.67e-14

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: 65.40  E-value: 3.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  39 CPMGSKAYRSYCYTLVTTLKSWFQADLACQKRpSGHLVSILSGGEASFVSSLvtgrVNNNQDIWIGLHDPTMgqqpnGGG 118
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDM-GAHLVIINSQEEQEFISKI----LSGNRSYWIGLSDEET-----EGE 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 225903411 119 WEW-SNSDVL-NYLNW-DGDPSSTVNRG-NCGSLTATSEFlkWGDHHCDVELPFVCK 171
Cdd:cd03590   71 WKWvDGTPLNsSKTFWhPGEPNNWGGGGeDCAELVYDSGG--WNDVPCNLEYRWICE 125
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 39-171 3.91e-13

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: 62.59  E-value: 3.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  39 CPMGSKAYRSYCYTLVTTLKSWFQADLACQKRpSGHLVSILSGGEASFVSslvtgrvNNNQDI-WIGLHDPTMGqqpngG 117
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQ-QGHLSSIVTPEEQEFVN-------NNAQDYqWIGLNDRTIE-----G 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225903411 118 GWEWSNSDVLNYLNW-DGDPSSTVNRGNCGSLTATSEFLKWGDHHCDVELPFVCK 171
Cdd:cd03588   68 DFRWSDGHPLQFENWrPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCK 122
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 39-172 6.42e-12

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: 59.71  E-value: 6.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  39 CPMGSKAYRSyCYTLVTTLKSWFQADLACQKRpSGHLVSILSGGEASFVSSLVTGRVNNNQDIWIGLHDptmgqQPNGGG 118
Cdd:cd03596    1 CLKGTKIHKK-CYLVSEETKHYHEASEDCIAR-GGTLATPRDSDENDALRDYVKASVPGNWEVWLGIND-----MVAEGK 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 225903411 119 WEWSNSDVLNYLNWDGDPSSTVNRG---NCGSLTATSEFlKWGDHHCDVELPFVCKF 172
Cdd:cd03596   74 WVDVNGSPISYFNWEREITAQPDGGkreNCVALSSSAQG-KWFDEDCRREKPYVCEF 129
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 51-170 2.87e-11

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 57.38  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  51 YTLVTTLKSWFQADLACQKRpSGHLVSILSGGEASFVSSLVTGrvnNNQDIWIGLHDPTmgqqpngGGWEWSNSDVLNYL 130
Cdd:cd03602    3 FYLVNESKTWSEAQQYCREN-YTDLATVQNQEDNALLSNLSRV---SNSAAWIGLYRDV-------DSWRWSDGSESSFR 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 225903411 131 NWDGDPSStvNRGNCGSLTATSeflKWGDHHCDVELPFVC 170
Cdd:cd03602   72 NWNTFQPF--GQGDCATMYSSG---RWYAALCSALKPFIC 106
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 51-159 1.29e-10

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 55.89  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  51 YTLVTTLKSWFQADLACQKRpSGHLVSILSGGEASFVSSLVtgrvNNNQDIWIGLHDPTmgqqpNGGGWEWSNSDVLNYL 130
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESL-GGHLVTINSAEENDWLLSNF----GGYGASWIGASDAA-----TEGTWKWSDGEESTYT 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 225903411 131 NWDGD---PSSTVNRGNCGSLTATSEFLKWGD 159
Cdd:cd03603   73 NWGSGephNNGGGNEDYAAINHFPGISGKWND 104
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 39-171 4.11e-09

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: 51.95  E-value: 4.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  39 CPMGSKAYRSYCYTLVTTLKSWFQADLACQKRPSgHLVSILSGGEASFVSSLVTgrvnnNQDIWIGLHDPTMGQQpnggg 118
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNS-SLLKIDDEEELEFLQSQIG-----SSSYWIGLSREKSEKP----- 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225903411 119 WEWSNSDVLNYLNwdgDPSSTVNRGNCGSLTATSEFlkwgDHHCDVELPFVCK 171
Cdd:cd03593   70 WKWIDGSPLNNLF---NIRGSTKSGNCAYLSSTGIY----SEDCSTKKRWICE 115
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 50-172 8.09e-08

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 48.22  E-value: 8.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  50 CYTLVTTLKSWFQADLACQKRPSGHLVSILSGGEASFVSSLVtGRVNNNQdIWIGlhdptmGQQPNGGG---WEWSNSDV 126
Cdd:cd03598    3 CYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLV-STLNQAQ-VWIG------GIITGKGRcrrFSWVDGSV 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 225903411 127 LNYLNW-DGDPSStvNRGNCGSLTATSEFlkWGDHHCDVELPFVCKF 172
Cdd:cd03598   75 WNYAYWaPGQPGN--RRGHCVELCTRGGH--WRRAHCKLRRPFICSY 117
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 25-173 6.47e-06

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: 45.46  E-value: 6.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411    25 GEDSQKAVPSTrtsCPMGSKAY--RSYCYTLVTTLKSWFQADLACQKRPSGHLVSILSGGEASFVSSLVTGRVnnNQDIW 102
Cdd:TIGR00864  307 GEEPAKASHPH---CPKDGEIFeeNGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSL--DRGVW 381

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225903411   103 IGLHD---PTMGQQPNGGGWEWSNSDvlnylNWDGdPSSTVNRGN-CGSLTATSEFlkwGDHHCDVELPFVCKFK 173
Cdd:TIGR00864  382 IGFSDvngAEKGPAHQGEAFEAEECE-----EGLA-GEPHPARAEhCVRLDPRGQC---NSDLCNAPHAYVCELN 447
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 50-172 8.32e-05

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: 40.64  E-value: 8.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225903411  50 CYTLV----TTLKSWFQ-ADLACqKRPSGHLVSILSGGEASFVSSLVTGRVNNNQDIWIGLHDPTMGQQPNGG---GWEW 121
Cdd:cd03595   12 CYKIAyfqdSRRRLNFEeARQAC-REDGGELLSIESENEQKLIERFIQTLRASDGDFWIGLRRSSQYNVTSSAcssLYYW 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225903411 122 SNSDVLNYLNWDGDPSStvnrgnCGSLTATSEF--------------LKWGDHHCDVELPFVCKF 172
Cdd:cd03595   91 LDGSISTFRNWYVDEPS------CGSEVCVVMYhqpsapagqggpylFQWNDDNCNMKNNFICKY 149
 
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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