Conserved Protein Domain Family

cd00037: CLECT 
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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
Aligned: 852 rows
Threshold Bit Score: 32.2066
Created: 1-Nov-2000
Updated: 2-Oct-2020
Aligned Rows:
ligand binding
Conserved site includes 11 residues -Click on image for an interactive view with Cn3D
Feature 1:ligand binding surface [chemical binding site]
  • Comment:many but not all CTL domains bind ligands on this surface of the protein
  • Structure:1KCG_B, human Nkg2d homodimer bound with Ulbp3, contacts at 3.5 A.
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  • Structure:1P1Z_D, human Ly-49c bound with a MHC Class I ligand H-2kb, contacts at 3.5 A.
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  • Structure:1QO3_C, human Ly49a bound with MHC Class I ligand H-2dd, contacts at 3.5 A
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  • Structure:1YXK_B, human LOX-1 disulfide-linked dimer residues responsible for OxLDL binding defined by mutation analysis.
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  • Structure:1TDQ_B, rat aggrecan CLTD bound with fibronectin type III repeats 3-5 of rat tenascin-R, contacts at 3.5 A.
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  • Structure:1WMZ_D, Cucumaria echinata C-type lectin Cel-I bound with N-acetyl-D-galactosamine.(GalNAc), contacts at 3.5 A.
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  • Structure:1K9I_A, human DC-SIGN bound with Glcnac2man3, contacts at 3.5 A
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  • Comment:The carbohydrate cross-links two monomeric CTLDs in the DC-SIGN crystals.
  • Structure:1SL5_A, human DC-SIGN CTLD, bound with Lnfp Iii (Dextra L504), contacts at 3.5 A.
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  • Structure:1PWB_C, human lung surfactant protein D trimer, bound with maltose and calcium ions , contacts at 3.5A
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  • Structure:1KWY_A, rat mannose protein A trimer bound with Man-A13-Man, contacts at 3.5 A.
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  • Structure:1G1T_A, human E-selectin Lectin EGF domains bound with Slex and a calcium ion, contacts at 3.5 A
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  • Structure:1G1S_A, human P-selectin Lectin EGF domains bound with the glycoprotein, PSGL-1 peptide, contacts at 3.5
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  • Structure:2BRS_B, Homo sapiens, EMBP bound with heparin disaccharide, contacts at 3.5 A
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  • Structure:1TLG_A, Polyandrocarpa misakiensis, TC14 bound with a calcium ion and D-galactose.
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  • Structure:1IOD; complex between the Coagulation Factor X Binding Protein from snake venom and the Gla domain of Factor X
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  • Structure:1JZN_A, rattlesnake galactose-specific C-Type lectin, bound with galactose and calcium ions, contacts at 3.5 A.
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Sequence Alignment
Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                      
1B08_A      46 KIFKTAgf-----vKPFTEAQLLCTqag---gqLASPRSa----AENAALQqlvv-------akneAAFLSMtdsk---- 102  human
1KCG_B      17 NCYQFFde-----sKNWYESQASCMsqn---asLLKVYSk----EDQDLLKlv-----------ksYHWMGLvhip---- 69   human
AAP78680    53 HEYYYSrdhfghilVNFTTARAYCRtlg---gdLVSINSk----AENDFVFslna-------ttfdRRWIGVqynt---- 114  Monosiga brevico...
AAP78680   428 EYYYSRdyfp-sttFNFVEAMDWCDsig---ghLAYPDTr----AENEFIAsidp-------tmtnMRWLGVrynv---- 488  Monosiga brevico...
AAP78680   618 HQYFYSkdfypdipLTFAQAQDWCEtmd---ahLVYTETk----AENDFVYsisp-------ipneLRWLGAvyns---- 679  Monosiga brevico...
AAP78681   220 SYYAYVst-----sVTQPEAQTVCEadd---anLVSVDSl----AENSFVHglga--------pnqARWLGGivdysg-- 277  Monosiga brevico...
CAE70943     8 LCISSTl-------ADCPAAWKTFLn------sEMEENTangceADWKFVNrpstsilaqvpessgSLWTGLrrtkkcig 74   Caenorhabditis b...
XP_225585  940 KVSENTdls---lgPMKHETNRVSTgifdkftsYSDTHSk----GSNTFVTyhmr-------dstfNAWTGLndvn---- 1001 Norway rat
AAZ29608    67 ECFYLSkv-----kLNWNQARQYCQgmq---gdLATPRNv---yALKSFVIdtaa--------evtEAWLGAtdqs---- 123  black tiger shrimp
XP_790721  565 SCYRLAws----dpVPYAQALQLCSel----gsFPFIPNv---rAEFDFVVeflgea----dlgiqTIWLGCddtn---- 625  purple urchin
Feature 1                                                                       #   # #        
1B08_A     103 --------tegkFTYPTGes--------------lvYSNWapgepn--------------ddggsEDCVEIFtn------ 140  human
1KCG_B      70 --------tngsWQWEDGsil-------------spNLLTiie-------------------mqkGDCALYAss------ 103  human
AAP78680   115 --------sqgdFVNVDGylvddlittyytpcdpdtTCLWfkgepn--------------nafsdENCVQQGhlnpar-- 170  Monosiga brevico...
AAP78680   489 --------sllnFATLDGntinsllaeyttclpsgaGCLWrrdepn--------------gitnnELCVQMGhpkg---- 542  Monosiga brevico...
AAP78680   680 --------svdqYFFLDGtsi------------sglLAEYpvigcanggpgclwrndepngktngENCIQMGhpkg---- 735  Monosiga brevico...
AAP78681   278 -------pddyaVTWADGssfd-----------vsmTDMWlpgqpng------------dgsclaQGQLTNNlpn----- 322  Monosiga brevico...
CAE70943    75 qkitatctnltsFEWTDGsst------------gtdGFVFqagqpd--------------nknldQNCALFLasktptvv 128  Caenorhabditis b...
XP_225585 1002 --------sehtFLWTDGrg--------------vhYTNWgkgypggr---------rsslsyedVDCVVVIggns---- 1046 Norway rat
AAZ29608   124 --------segtWNWLDGrp---------------vASDWaggqpd--------------daggnEDCLDLRtkw----- 161  black tiger shrimp
XP_790721  626 --------mdgkFLCLDGkri-------------llHNPWwapgqp--------------dsyetENCLVLFlg------ 664  purple urchin
Feature 1               # ####             ###      
1B08_A     141 --------gKWNDRACg-----------EKRLVVCEF 158  human
1KCG_B     104 --------fKGYIENCs-----------TPNTYICMQ 121  human
AAP78680   171 ----asnpgGWNDADCt-----------KDRAFVCEA 192  Monosiga brevicollis
AAP78680   543 -----gqvgNWNDAVCs-----------KRRFAVCEI 563  Monosiga brevicollis
AAP78680   736 -----gqpaSWNDAVCt-----------KFRFAVCER 756  Monosiga brevicollis
AAP78681   323 ------vssLWNDVPCt-----------TSLPFVCEK 342  Monosiga brevicollis
CAE70943   129 ankgtyyaaSYEDTGCevgefseahlprKILGHVCGK 165  Caenorhabditis briggsae
XP_225585 1047 -----reagTWMDSTCd-----------SKQGYICQT 1067 Norway rat
AAZ29608   162 -------hpTLNDYQCg-----------VAQHFVCQY 180  black tiger shrimp
XP_790721  665 -------amNLHDYPCt----------lANPNTLCER 684  purple urchin

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