collagen 18 alpha-1; contains: endostatin (COL18A1)

Function: - COLA18A probably plays a role in determining retinal structure as well as in the closure of the neural tube - cleaved to form endostatin, a potent inhibitor of endothelial cell proliferation & angiogenesis - Pro at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains Structure: - belongs to the multiplexin collagen family - contains 1 FZ (frizzled) domain - contains 1 TSP N-terminal (TSPN) domain Compartment: - secreted, extracellular space, extracellular matrix (putative) Alternative promoter usage: - isoforms produced by alternative promoter usage Alternative splicing: named isoforms=3 Expression: - present in multiple organs with highest levels in liver, lung & kidney Polymorphism: - association between polymorphism in position 1675 & prostate cancer - heterozygous Asn-1675 individuals have a 2.5-fold risk of prostate cancer compared with homozygous Asp-1675 individuals Pathology: - defects in COL18A1 are a cause of Knobloch syndrome type 1

General

collagen subunit glycoprotein

Properties

SIZE: entity length = 1754 aa MW = 178 kD MOTIF: signal sequence {1-23} N-glycosylation site {N68} N-glycosylation site {N129} N-glycosylation site {N164} frizzled domain {329-446} MOTIF: cysteine residue {C334} MODIFICATION: cysteine residue {C397} cysteine residue {C344} MODIFICATION: cysteine residue {C390} cysteine residue {C381} MODIFICATION: cysteine residue {C419} cysteine residue {C390} MODIFICATION: cysteine residue {C344} cysteine residue {C397} MODIFICATION: cysteine residue {C334} cysteine residue {C408} MODIFICATION: cysteine residue {C443} cysteine residue {C412} MODIFICATION: cysteine residue {C432} cysteine residue {C419} MODIFICATION: cysteine residue {C381} cysteine residue {C432} MODIFICATION: cysteine residue {C412} cysteine residue {C443} MODIFICATION: cysteine residue {C408} TSP N-terminal {456-644} Nonhelical region (NC1) {645-751} Triple-helical region (COL1) {752-785} Nonhelical region (NC2) {786-795} Triple-helical region (COL2) {796-875} Nonhelical region (NC3) {876-899} Triple-helical region (COL3) {900-1021} MOTIF: N-glycosylation site {N926} Nonhelical region (NC4) {1022-1044} Triple-helical region (COL4) {1045-1127} Nonhelical region (NC5) {1128-1141} Triple-helical region (COL5) {1142-1183} Nonhelical region (NC6) {1184-1196} Triple-helical region (COL6) {1197-1269} Nonhelical region (NC7) {1270-1279} Triple-helical region (COL7) {1280-1312} Nonhelical region (NC8) {1313-1324} Triple-helical region (COL8) {1325-1346} MOTIF: Cell attachment {1330-1332} Nonhelical region (NC9) {1347-1353} Triple-helical region (COL9) {1354-1411} Nonhelical region (NC10) {1412-1424} Triple-helical region (COL10) {1425-1442} Nonhelical region (NC11) {1443-1754} MOTIF: Thr glycosylation site {T1567} Zn+2-binding site SITE: 1572-1572 Zn+2-binding site SITE: 1574-1574 Zn+2-binding site SITE: 1582-1582 cysteine residue {C1604} MODIFICATION: cysteine residue {C1744} Zn+2-binding site SITE: 1647-1647 cysteine residue {C1706} MODIFICATION: cysteine residue {C1736} cysteine residue {C1736} MODIFICATION: cysteine residue {C1706} cysteine residue {C1744} MODIFICATION: cysteine residue {C1604}

Database Correlations

OMIM correlations MORBIDMAP 120328 UniProt P39060 PFAM correlations Entrez Gene 80781 Kegg hsa:80781