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Conserved domains on  [gi|27228976|ref|NP_079698|]
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CD302 antigen isoform b precursor [Mus musculus]

Protein Classification

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

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein similar to Homo sapiens CD302 antigen that may play roles in endocytosis and phagocytosis as well as in cell adhesion and migration

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 ...
22-151 1.10e-19

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


:

Pssm-ID: 214480  Cd Length: 124  Bit Score: 81.11  E-value: 1.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976     22 CPSStWVQFQGSCYAFLQVTinvENIEDVRKQCTDHGADMVSIHNEEENAFILDTLqKRWKGPDDLLLGMFYDTDDATFK 101
Cdd:smart00034   1 CPSG-WISYGGKCYKFSTEK---KTWEDAQAFCQSLGGHLASIHSEAENDFVASLL-KNSGSSDYYWIGLSDPDSNGSWQ 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 27228976    102 WYDHSNMT-FDKWADQDGEDLVDTCGFLYTKTGEWRKGDCEisSVEGTLCK 151
Cdd:smart00034  76 WSDGSGPVsYSNWAPGEPNNSSGDCVVLSTSGGKWNDVSCT--SKLPFVCE 124
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
22-151 1.10e-19

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


Pssm-ID: 214480  Cd Length: 124  Bit Score: 81.11  E-value: 1.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976     22 CPSStWVQFQGSCYAFLQVTinvENIEDVRKQCTDHGADMVSIHNEEENAFILDTLqKRWKGPDDLLLGMFYDTDDATFK 101
Cdd:smart00034   1 CPSG-WISYGGKCYKFSTEK---KTWEDAQAFCQSLGGHLASIHSEAENDFVASLL-KNSGSSDYYWIGLSDPDSNGSWQ 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 27228976    102 WYDHSNMT-FDKWADQDGEDLVDTCGFLYTKTGEWRKGDCEisSVEGTLCK 151
Cdd:smart00034  76 WSDGSGPVsYSNWAPGEPNNSSGDCVVLSTSGGKWNDVSCT--SKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
33-141 1.88e-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  Cd Length: 116  Bit Score: 61.48  E-value: 1.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976  33 SCYaflQVTINVENIEDVRKQCTDHGADMVSIHNEEENAFILDTLQKrwKGPDDLLLGMFYDTDDATFKWYDHS-NMTFD 111
Cdd:cd00037   1 SCY---KFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSEGTWKWSDGSpLVDYT 75
                        90       100       110
                ....*....|....*....|....*....|..
gi 27228976 112 KWA-DQDGEDLVDTCGFLY-TKTGEWRKGDCE 141
Cdd:cd00037  76 NWApGEPNPGGSEDCVVLSsSSDGKWNDVSCS 107
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
45-151 1.70e-10

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


Pssm-ID: 395013  Cd Length: 104  Bit Score: 55.94  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976    45 ENIEDVRKQCTDHGADMVSIHNEEENAFILDTLQKRwkgPDDLLLGMFYDTDDATFKWYDHSNMTFDKWADQDGEDLVDT 124
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKQS---NEYFWIGLTDRKNEGTWKWEDGSPVNYTNWAEPNNNGENED 78
                          90       100
                  ....*....|....*....|....*..
gi 27228976   125 CGFLYTKTGEWRKGDCEISSveGTLCK 151
Cdd:pfam00059  79 CVELSSSSGKWNDENCNSKN--PFVCE 103
PHA02642 PHA02642
C-type lectin-like protein; Provisional
22-107 1.36e-03

C-type lectin-like protein; Provisional


Pssm-ID: 165024  Cd Length: 216  Bit Score: 38.56  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976   22 CPSStWVQFQGSCYAFLQvtiNVENIEDVRKQCTDHGADMVSIHNEEENAFIldtlqKRWKGPDDLLLGMFYDTDDATFK 101
Cdd:PHA02642  88 CPKG-WIGFGYKCFYFSE---DSKNWTFGNTFCTSLGATLVKVETEEELNFL-----KRYKDSSDHWIGLNRESSNHPWK 158

                 ....*.
gi 27228976  102 WYDHSN 107
Cdd:PHA02642 159 WADNSN 164
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
22-151 1.10e-19

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


Pssm-ID: 214480  Cd Length: 124  Bit Score: 81.11  E-value: 1.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976     22 CPSStWVQFQGSCYAFLQVTinvENIEDVRKQCTDHGADMVSIHNEEENAFILDTLqKRWKGPDDLLLGMFYDTDDATFK 101
Cdd:smart00034   1 CPSG-WISYGGKCYKFSTEK---KTWEDAQAFCQSLGGHLASIHSEAENDFVASLL-KNSGSSDYYWIGLSDPDSNGSWQ 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 27228976    102 WYDHSNMT-FDKWADQDGEDLVDTCGFLYTKTGEWRKGDCEisSVEGTLCK 151
Cdd:smart00034  76 WSDGSGPVsYSNWAPGEPNNSSGDCVVLSTSGGKWNDVSCT--SKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
33-141 1.88e-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  Cd Length: 116  Bit Score: 61.48  E-value: 1.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976  33 SCYaflQVTINVENIEDVRKQCTDHGADMVSIHNEEENAFILDTLQKrwKGPDDLLLGMFYDTDDATFKWYDHS-NMTFD 111
Cdd:cd00037   1 SCY---KFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSEGTWKWSDGSpLVDYT 75
                        90       100       110
                ....*....|....*....|....*....|..
gi 27228976 112 KWA-DQDGEDLVDTCGFLY-TKTGEWRKGDCE 141
Cdd:cd00037  76 NWApGEPNPGGSEDCVVLSsSSDGKWNDVSCS 107
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
45-151 1.70e-10

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


Pssm-ID: 395013  Cd Length: 104  Bit Score: 55.94  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976    45 ENIEDVRKQCTDHGADMVSIHNEEENAFILDTLQKRwkgPDDLLLGMFYDTDDATFKWYDHSNMTFDKWADQDGEDLVDT 124
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKQS---NEYFWIGLTDRKNEGTWKWEDGSPVNYTNWAEPNNNGENED 78
                          90       100
                  ....*....|....*....|....*..
gi 27228976   125 CGFLYTKTGEWRKGDCEISSveGTLCK 151
Cdd:pfam00059  79 CVELSSSSGKWNDENCNSKN--PFVCE 103
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
22-114 2.26e-10

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: 56.60  E-value: 2.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976  22 CPSsTWVQFQGSCYAFLQVTINVENIEDvrkQCTDHG-----ADMVSIHNEEENAFILDTLQKRWKG--PDDLLLGMFYD 94
Cdd:cd03589   1 CPT-FWTAFGGYCYRFFGDRLTWEEAEL---RCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPdtPYGLWIGLHDR 76
                        90       100
                ....*....|....*....|
gi 27228976  95 TDDATFKWYDHSNMTFDKWA 114
Cdd:cd03589  77 TSEGPFEWTDGSPVDFTKWA 96
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
22-129 1.27e-07

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: 48.48  E-value: 1.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976  22 CPSStWVQFQGSCYAFLQvtiNVENIEDVRKQCTDHGADMVSIHNEEEnafiLDTLQKRwKGPDDLLLGMFYDTDDATFK 101
Cdd:cd03593   1 CPKD-WICYGNKCYYFSM---EKKTWNESKEACSSKNSSLLKIDDEEE----LEFLQSQ-IGSSSYWIGLSREKSEKPWK 71
                        90       100
                ....*....|....*....|....*...
gi 27228976 102 WYDHSnmTFDKWADQDGEDLVDTCGFLY 129
Cdd:cd03593  72 WIDGS--PLNNLFNIRGSTKSGNCAYLS 97
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
27-140 1.49e-07

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: 48.34  E-value: 1.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976  27 WVQFQGSCYAFLQvtiNVENIEDVRKQCTDHGADMVSIHNEEENAFILDTLQK-RWKGPDDlllgmfyDTDDATFKWYDH 105
Cdd:cd03588   5 WDKFQGHCYRHFP---DRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDyQWIGLND-------RTIEGDFRWSDG 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 27228976 106 SNMTFDKWADQD-------GEDLVdtcGFLYTKTGEWRKGDC 140
Cdd:cd03588  75 HPLQFENWRPNQpdnffatGEDCV---VMIWHEEGEWNDVPC 113
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
22-80 9.98e-07

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  Cd Length: 126  Bit Score: 46.14  E-value: 9.98e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27228976  22 CPSStWVQFQGSCYAFLQVTinvENIEDVRKQCTDHGADMVSIHNEEENAFILDTLQKR 80
Cdd:cd03590   1 CPTN-WKSFQSSCYFFSTEK---KSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGN 55
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
44-143 1.63e-06

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


Pssm-ID: 153061  Cd Length: 114  Bit Score: 45.36  E-value: 1.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976  44 VENIEDVRKQCTDHGADMVSIHNEEENAFILDtLQKrwKGPDDLLLGMfydTDDAT---FKWYDHSNMTFDKWAD----- 115
Cdd:cd03591  10 EKNFDDAQKLCSEAGGTLAMPRNAAENAAIAS-YVK--KGNTYAFIGI---TDLETegqFVYLDGGPLTYTNWKPgepnn 83
                        90       100
                ....*....|....*....|....*....
gi 27228976 116 -QDGEDlvdtCGFLYTkTGEWRKGDCEIS 143
Cdd:cd03591  84 aGGGED----CVEMYT-SGKWNDVACNLT 107
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
22-141 1.41e-05

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


Pssm-ID: 153064  Cd Length: 129  Bit Score: 43.13  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976  22 CPSStWVQFQGSCYAFLQVTINVENIEdvrKQCTDH--GADMVSIHNEEENAFILDTLQKRWKGPDDLLLGMFYDTDDAT 99
Cdd:cd03594   1 CPKG-WLPYKGNCYGYFRQPLSWSDAE---LFCQKYgpGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRG 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 27228976 100 FKWYDHSNMTFDKWADQDGEDLVDTCGFLYTKTG--EWRKGDCE 141
Cdd:cd03594  77 WEWSDGSKLDYRSWDRNPPYARGGYCAELSRSTGflKWNDANCE 120
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
49-79 2.22e-04

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: 39.28  E-value: 2.22e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 27228976  49 DVRKQCTDHGADMVSIHNEEENAFILDTLQK 79
Cdd:cd03592  14 EAVKYCKSRGTDLVAIQNAEENALLNGFALK 44
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
54-140 8.48e-04

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 37.74  E-value: 8.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976  54 CTDHGADMVSIHNEEENAFILDTLQkrwKGPDDLLLGMFYDTDdaTFKWYDHSNMTFDKWaDQDGEDLVDTCGFLYTkTG 133
Cdd:cd03602  19 CRENYTDLATVQNQEDNALLSNLSR---VSNSAAWIGLYRDVD--SWRWSDGSESSFRNW-NTFQPFGQGDCATMYS-SG 91

                ....*..
gi 27228976 134 EWRKGDC 140
Cdd:cd03602  92 RWYAALC 98
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
30-127 8.91e-04

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: 38.33  E-value: 8.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976  30 FQGSCY--AFLQVTINVENIEDVRKQCTDHGADMVSIHNEEENAFILDTLQKRWKGPDDLLLGMFYDTD--------DAT 99
Cdd:cd03595   8 TEKPCYkiAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWIGLRRSSQynvtssacSSL 87
                        90       100       110
                ....*....|....*....|....*....|
gi 27228976 100 FKWYDHSNMTFDKWadqdgedLVD--TCGF 127
Cdd:cd03595  88 YYWLDGSISTFRNW-------YVDepSCGS 110
PHA02642 PHA02642
C-type lectin-like protein; Provisional
22-107 1.36e-03

C-type lectin-like protein; Provisional


Pssm-ID: 165024  Cd Length: 216  Bit Score: 38.56  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976   22 CPSStWVQFQGSCYAFLQvtiNVENIEDVRKQCTDHGADMVSIHNEEENAFIldtlqKRWKGPDDLLLGMFYDTDDATFK 101
Cdd:PHA02642  88 CPKG-WIGFGYKCFYFSE---DSKNWTFGNTFCTSLGATLVKVETEEELNFL-----KRYKDSSDHWIGLNRESSNHPWK 158

                 ....*.
gi 27228976  102 WYDHSN 107
Cdd:PHA02642 159 WADNSN 164
PHA03097 PHA03097
C-type lectin-like protein; Provisional
22-132 3.92e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982  Cd Length: 157  Bit Score: 36.77  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27228976   22 CPSStWVQFQGSCYAFlqvtinVENIEDVRKQ---CTDHGADMVSIHNEEENAFILdtlqkRWKGPDDLLLGmfydtdDA 98
Cdd:PHA03097  46 CRSG-WVGYNNKCYTF------SENITNKHLAierCADMDGILTLIDDQKEVLFVS-----RYKGGQDLWIG------IE 107
                         90       100       110
                 ....*....|....*....|....*....|....
gi 27228976   99 TFKWYDHSNMTFDKWADQDGedlVDTCGFLYTKT 132
Cdd:PHA03097 108 KKKGDDDDREVLDKVVKPPK---SGKCAYLKDKT 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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