Collagen, type XVIII, alpha 1

Collagen alpha-1(XVIII) chain is a protein that in humans is encoded by the COL18A1 gene.

COL18A1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BNL, 3HON, 3HSH
Identifiers
Aliases	COL18A1, KNO, KNO1, KS, Collagen, type XVIII, alpha 1, collagen type XVIII alpha 1, collagen type XVIII alpha 1 chain, GLCC
External IDs	OMIM: 120328 MGI: 88451 HomoloGene: 7673 GeneCards: COL18A1
Gene location (Human) Chr. Chromosome 21 (human) Band 21q22.3 Start 45,405,165 bp End 45,513,720 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10 C1|10 39.72 cM Start 76,888,012 bp End 77,002,382 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right coronary artery popliteal artery right lobe of liver ascending aorta canal of the cervix left coronary artery right uterine tube left uterine tube sural nerve anterior pituitary Top expressed in left lobe of liver ascending aorta gallbladder external carotid artery internal carotid artery ciliary body medullary collecting duct semi-lunar valve aortic valve somite More reference expression data BioGPS More reference expression data
Gene ontology Molecular function structural molecule activity metal ion binding protein binding identical protein binding extracellular matrix structural constituent extracellular matrix structural constituent conferring tensile strength Cellular component collagen endoplasmic reticulum lumen extracellular matrix basement membrane extracellular exosome extracellular space extracellular region collagen-containing extracellular matrix Biological process positive regulation of cell migration endothelial cell morphogenesis response to hydrostatic pressure extracellular matrix organization positive regulation of endothelial cell apoptotic process cell adhesion angiogenesis positive regulation of cell population proliferation animal organ morphogenesis collagen catabolic process visual perception negative regulation of cell population proliferation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 80781 12822 Ensembl ENSG00000182871 ENSMUSG00000001435 UniProt P39060 P39061 RefSeq (mRNA) NM_130445 NM_030582 NM_130444 NM_001379500 NM_001109991 NM_009929 RefSeq (protein) NP_085059 NP_569711 NP_569712 NP_001366429 NP_001103461 NP_034059 NP_001393179 NP_001393180 NP_001393181 NP_001393182 NP_001393183 NP_001393184 Location (UCSC) Chr 21: 45.41 – 45.51 Mb Chr 10: 76.89 – 77 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes the alpha chain of type XVIII collagen. This collagen is one of the multiplexins, extracellular matrix proteins that contain multiple triple-helix domains (collagenous domains) interrupted by non-collagenous domains. The proteolytically produced C-terminal fragment of type XVIII collagen is endostatin, a potent antiangiogenic protein. Mutations in this gene are associated with Knobloch syndrome. The main features of this syndrome involve retinal abnormalities so type XVIII collagen may play an important role in retinal structure and in neural tube closure. Two transcript variants encoding different isoforms have been found for this gene.

See also

Collagen

Further reading

• Pufe T, Kurz B, Petersen W, et al. (2006). "The influence of biomechanical parameters on the expression of VEGF and endostatin in the bone and joint system". Ann. Anat. 187 (5–6): 461–72. doi:10.1016/j.aanat.2005.06.008. PMID 16320826.
• Oh SP, Kamagata Y, Muragaki Y, et al. (1994). "Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins". Proc. Natl. Acad. Sci. U.S.A. 91 (10): 4229–33. Bibcode:1994PNAS...91.4229O. doi:10.1073/pnas.91.10.4229. PMC 43758. PMID 8183893.
• Sertié AL, Quimby M, Moreira ES, et al. (1996). "A gene which causes severe ocular alterations and occipital encephalocele (Knobloch syndrome) is mapped to 21q22.3". Hum. Mol. Genet. 5 (6): 843–7. doi:10.1093/hmg/5.6.843. PMID 8776601.
• O'Reilly MS, Boehm T, Shing Y, et al. (1997). "Endostatin: an endogenous inhibitor of angiogenesis and tumor growth". Cell. 88 (2): 277–85. doi:10.1016/S0092-8674(00)81848-6. PMID 9008168. S2CID 14851562.
• Saarela J, Ylikärppä R, Rehn M, et al. (1998). "Complete primary structure of two variant forms of human type XVIII collagen and tissue-specific differences in the expression of the corresponding transcripts". Matrix Biol. 16 (6): 319–28. doi:10.1016/S0945-053X(98)90003-8. PMID 9503365.
• Ding YH, Javaherian K, Lo KM, et al. (1998). "Zinc-dependent dimers observed in crystals of human endostatin". Proc. Natl. Acad. Sci. U.S.A. 95 (18): 10443–8. Bibcode:1998PNAS...9510443D. doi:10.1073/pnas.95.18.10443. PMC 27913. PMID 9724722.
• Sasaki T, Göhring W, Miosge N, et al. (1999). "Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins". FEBS Lett. 460 (2): 280–4. doi:10.1016/S0014-5793(99)01362-9. PMID 10544250. S2CID 25139630.
• Felbor U, Dreier L, Bryant RA, et al. (2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187–94. doi:10.1093/emboj/19.6.1187. PMC 305660. PMID 10716919.
• Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21". Nature. 405 (6784): 311–9. Bibcode:2000Natur.405..311H. doi:10.1038/35012518. PMID 10830953.
• Sertié AL, Sossi V, Camargo AA, et al. (2000). "Collagen XVIII, containing an endogenous inhibitor of angiogenesis and tumor growth, plays a critical role in the maintenance of retinal structure and in neural tube closure (Knobloch syndrome)". Hum. Mol. Genet. 9 (13): 2051–8. doi:10.1093/hmg/9.13.2051. PMID 10942434.
• Rehn M, Veikkola T, Kukk-Valdre E, et al. (2001). "Interaction of endostatin with integrins implicated in angiogenesis". Proc. Natl. Acad. Sci. U.S.A. 98 (3): 1024–9. doi:10.1073/pnas.031564998. PMC 14702. PMID 11158588.
• Karumanchi SA, Jha V, Ramchandran R, et al. (2001). "Cell surface glypicans are low-affinity endostatin receptors" (PDF). Mol. Cell. 7 (4): 811–22. doi:10.1016/S1097-2765(01)00225-8. PMID 11336704. S2CID 43358048.
• Feng Y, Cui LB, Liu CX, Ma QJ (2001). "[Inhibition effect in vitro of purified endostatin expressed in Pichia pastoris]". Sheng Wu Gong Cheng Xue Bao. 17 (3): 278–82. PMID 11517600.
• Iughetti P, Suzuki O, Godoi PH, et al. (2001). "A polymorphism in endostatin, an angiogenesis inhibitor, predisposes for the development of prostatic adenocarcinoma". Cancer Res. 61 (20): 7375–8. PMID 11606364.
• Wu P, Yonekura H, Li H, et al. (2001). "Hypoxia down-regulates endostatin production by human microvascular endothelial cells and pericytes". Biochem. Biophys. Res. Commun. 288 (5): 1149–54. doi:10.1006/bbrc.2001.5903. PMID 11700031.
• Zorick TS, Mustacchi Z, Bando SY, et al. (2002). "High serum endostatin levels in Down syndrome: implications for improved treatment and prevention of solid tumours". Eur. J. Hum. Genet. 9 (11): 811–4. doi:10.1038/sj.ejhg.5200721. PMID 11781696.
• Hanai J, Dhanabal M, Karumanchi SA, et al. (2002). "Endostatin causes G1 arrest of endothelial cells through inhibition of cyclin D1". J. Biol. Chem. 277 (19): 16464–9. doi:10.1074/jbc.M112274200. PMID 11815623.
• Ergün S, Kilic N, Wurmbach JH, et al. (2002). "Endostatin inhibits angiogenesis by stabilization of newly formed endothelial tubes". Angiogenesis. 4 (3): 193–206. doi:10.1023/A:1014027218980. PMID 11911017. S2CID 28608175.
• Tomono Y, Naito I, Ando K, et al. (2002). "Epitope-defined monoclonal antibodies against multiplexin collagens demonstrate that type XV and XVIII collagens are expressed in specialized basement membranes". Cell Struct. Funct. 27 (1): 9–20. doi:10.1247/csf.27.9. PMID 11937714.

External links

• Overview of all the structural information available in the PDB for UniProt: P39060 (Human Collagen alpha-1(XVIII) chain) at the PDBe-KB.
• Overview of all the structural information available in the PDB for UniProt: P39061 (Mouse Collagen alpha-1(XVIII) chain) at the PDBe-KB.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.