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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A        1 WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNS-ILSYSPSYYWIGIRKVNNVWVWVGTQKPLtEEAKNWAPG 79
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGfALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
1G1T_A       80 EPNNRqKDEDCVEIYIkreKDVGMWNDERCSKKKLALCYT 119
Cdd:cd03592  80 EPNNG-RNENCLEIYI---KDNGKWNDEPCSKKKSAICYT 115

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A        1 WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNS-ILSYSPSYYWIGIRKVNNVWVWVGTQKPLtEEAKNWAPG 79
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGfALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
1G1T_A       80 EPNNRqKDEDCVEIYIkreKDVGMWNDERCSKKKLALCYT 119
Cdd:cd03592  80 EPNNG-RNENCLEIYI---KDNGKWNDEPCSKKKSAICYT 115

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A           3 YNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSY--SPSYYWIGIR--KVNNVWVWVGTQKPLTeeAKNWAP 78
Cdd:smart00034  13 YKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSdpDSNGSWQWSDGSGPVS--YSNWAP 90

                           90       100       110
                   ....*....|....*....|....*....|....*....
1G1T_A          79 GEPNNRqkDEDCVEIYIKRekdvGMWNDERCSKKKLALC 117
Cdd:smart00034  91 GEPNNS--SGDCVVLSTSG----GKWNDVSCTSKLPFVC 123

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.

                          10        20
                  ....*....|....*....|....*....
1G1T_A        122 CTNTSCSGHGECVETINNYTCKCDPGFSG 150
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A        1 WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNS-ILSYSPSYYWIGIRKVNNVWVWVGTQKPLtEEAKNWAPG 79
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGfALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
1G1T_A       80 EPNNRqKDEDCVEIYIkreKDVGMWNDERCSKKKLALCYT 119
Cdd:cd03592  80 EPNNG-RNENCLEIYI---KDNGKWNDEPCSKKKSAICYT 115

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A        1 WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILS-YSPSYYWIGIRKV--NNVWVWVGTQKPLTeeAKNWA 77
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKkSSSSDVWIGLNDLssEGTWKWSDGSPLVD--YTNWA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
1G1T_A       78 PGEPNNrQKDEDCVEIYIkreKDVGMWNDERCSKKKLALCY 118
Cdd:cd00037  79 PGEPNP-GGSEDCVVLSS---SSDGKWNDVSCSSKLPFICE 115

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A           3 YNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSY--SPSYYWIGIR--KVNNVWVWVGTQKPLTeeAKNWAP 78
Cdd:smart00034  13 YKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSdpDSNGSWQWSDGSGPVS--YSNWAP 90

                           90       100       110
                   ....*....|....*....|....*....|....*....
1G1T_A          79 GEPNNRqkDEDCVEIYIKRekdvGMWNDERCSKKKLALC 117
Cdd:smart00034  91 GEPNNS--SGDCVVLSTSG----GKWNDVSCTSKLPFVC 123

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A        6 STEAMTYDEASAYCQQRYTHLVAIQNKEeIEYLNSILSYSPSY---YWIGIRKVNNV---WVWvGTQKPLTEEAKNWAPG 79
Cdd:cd03601   6 SDETMNYAKAGAFCRSRGMRLASLAMRD-SEMRDAILAFTLVKghgYWVGADNLQDGeydFLW-NDGVSLPTDSDLWAPN 83

                        90       100       110
                ....*....|....*....|....*....|....*...
1G1T_A       80 EPNNRQKDEDCVEIYIKRekdvGMWNDERCSKKKLALC 117
Cdd:cd03601  84 EPSNPQSRQLCVQLWSKY----NLLDDEYCGRAKRVIC 117

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A       11 TYDEASAYCQQ-----RYTHLVAIQNKEE----IEYLNSILSYSPSY-YWIGI--RKVNNVWVWV-GTQKPLTeeakNWA 77
Cdd:cd03589  21 TWEEAELRCRSfsipgLIAHLVSIHSQEEndfvYDLFESSRGPDTPYgLWIGLhdRTSEGPFEWTdGSPVDFT----KWA 96

                        90       100       110
                ....*....|....*....|....*....|....*
1G1T_A       78 PGEPNNRQKDEDCVEIYiKREKDVGMWNDERCSKK 112
Cdd:cd03589  97 GGQPDNYGGNEDCVQMW-RRGDAGQSWNDMPCDAV 130

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A        3 YNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNsilSYSPSYYWIGI--RKVNNVWVWVGTQKPLTEeakNWAPGE 80
Cdd:cd03588  13 YRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVN---NNAQDYQWIGLndRTIEGDFRWSDGHPLQFE---NWRPNQ 86

                        90       100       110
                ....*....|....*....|....*....|.
1G1T_A       81 PNNR-QKDEDCVeIYIKREKdvGMWNDERCS 110
Cdd:cd03588  87 PDNFfATGEDCV-VMIWHEE--GEWNDVPCN 114

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.

                          10        20
                  ....*....|....*....|....*....
1G1T_A        122 CTNTSCSGHGECVETINNYTCKCDPGFSG 150
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A        3 YNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILsySPSYYWIGIR--KVNNVWVWVGTQKPlteeaKNWapGE 80
Cdd:cd03593  13 YYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQI--GSSSYWIGLSreKSEKPWKWIDGSPL-----NNL--FN 83

                        90       100       110
                ....*....|....*....|....*....|....*..
1G1T_A       81 PNNRQKDEDCVeiYIKRekdvGMWNDERCSKKKLALC 117
Cdd:cd03593  84 IRGSTKSGNCA--YLSS----TGIYSEDCSTKKRWIC 114

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G1T_A       11 TYDEASAYCQQRY--THLVAIQNKEEIEYLNSILSYS---PSYYWIGIR--KVNNVWVWVGTQKPLTeeaKNWAPGEPNN 83
Cdd:cd03594  21 SWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSYqkaYQPVWIGLHdpQQSRGWEWSDGSKLDY---RSWDRNPPYA 97

                        90       100       110
                ....*....|....*....|....*....|....
1G1T_A       84 RQKDedCVEIyiKREKDVGMWNDERCSKKKLALC 117
Cdd:cd03594  98 RGGY--CAEL--SRSTGFLKWNDANCEERNPFIC 127

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.

                          10        20
                  ....*....|....*....|..
1G1T_A        127 CSGHGECVETINNYTCKCDPGF 148
Cdd:pfam12661   1 CQNGGTCVDGVNGYKCQCPPGY 22

Domain of unknown function (DUF3844); This presumed domain is found in fungal species. It contains 8 largely conserved cysteine residues. This domain is found in proteins that are thought to be found in the endoplasmic reticulum.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
1G1T_A        117 CYT--AACTNT--SCSGHGECVETINN------YTCKCDP 146
Cdd:pfam12955   1 CFTseDACENAtnNCSGHGECVKKYKSksgrdcFACKCKA 40