This gene encodes an alpha chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This gene product is closely related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type with tissue-specific chain combinations. Mutations in this gene are associated with Ehlers-Danlos syndrome, classical type, formerly known as types I and II.[6]
^ abcGRCh38: Ensembl release 89: ENSG00000204262 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000026042 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Greenspan DS, Byers MG, Eddy RL, Cheng W, Jani-Sait S, Shows TB (May 1992). "Human collagen gene COL5A1 maps to the q34.2----q34.3 region of chromosome 9, near the locus for nail-patella syndrome". Genomics. 12 (4): 836–7. doi:10.1016/0888-7543(92)90320-R. PMID 1572660.
^ ab"Entrez Gene: COL5A2 collagen, type V, alpha 2".
Further readingEdit
Mann K (1992). "Isolation of the alpha 3-chain of human type V collagen and characterization by partial sequencing". Biol. Chem. Hoppe-Seyler. 373 (2): 69–75. doi:10.1515/bchm3.1992.373.1.69. PMID 1571108.
Greenspan DS, Lee ST, Lee BS, Hoffman GG (1992). "Homology between alpha 2(V) and alpha 1(III) collagen promoters and evidence for negatively acting elements in the alpha 2(V) first intron and 5' flanking sequences". Gene Expr. 1 (1): 29–39. PMC5952197. PMID 1820205.
Myers JC, Loidl HR, Seyer JM, Dion AS (1985). "Complete primary structure of the human alpha 2 type V procollagen COOH-terminal propeptide". J. Biol. Chem. 260 (20): 11216–22. doi:10.1016/S0021-9258(17)39168-8. PMID 2411731.
Woodbury D, Benson-Chanda V, Ramirez F (1989). "Amino-terminal propeptide of human pro-alpha 2(V) collagen conforms to the structural criteria of a fibrillar procollagen molecule". J. Biol. Chem. 264 (5): 2735–8. doi:10.1016/S0021-9258(19)81674-5. PMID 2914927.
Myers JC, Loidl HR, Stolle CA, Seyer JM (1985). "Partial covalent structure of the human alpha 2 type V collagen chain". J. Biol. Chem. 260 (9): 5533–41. doi:10.1016/S0021-9258(18)89055-X. PMID 2985598.
Weil D, Bernard M, Gargano S, Ramirez F (1987). "The pro alpha 2(V) collagen gene is evolutionarily related to the major fibrillar-forming collagens". Nucleic Acids Res. 15 (1): 181–98. doi:10.1093/nar/15.1.181. PMC340404. PMID 3029669.
Tsipouras P, Schwartz RC, Liddell AC, et al. (1989). "Genetic distance of two fibrillar collagen loci, COL3A1 and COL5A2, located on the long arm of human chromosome 2". Genomics. 3 (3): 275–7. doi:10.1016/0888-7543(88)90089-4. PMID 3224983.
Emanuel BS, Cannizzaro LA, Seyer JM, Myers JC (1985). "Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2". Proc. Natl. Acad. Sci. U.S.A. 82 (10): 3385–9. Bibcode:1985PNAS...82.3385E. doi:10.1073/pnas.82.10.3385. PMC397780. PMID 3858826.
Moradi-Améli M, Rousseau JC, Kleman JP, et al. (1994). "Diversity in the processing events at the N-terminus of type-V collagen". Eur. J. Biochem. 221 (3): 987–95. doi:10.1111/j.1432-1033.1994.tb18815.x. PMID 8181482.
Wright GD, Hughes AE, Regan M, Doherty M (1996). "Association of two loci on chromosome 2q with nodal osteoarthritis". Ann. Rheum. Dis. 55 (5): 317–9. doi:10.1136/ard.55.5.317. PMC1010169. PMID 8660106.
Michalickova K, Susic M, Willing MC, et al. (1998). "Mutations of the alpha2(V) chain of type V collagen impair matrix assembly and produce ehlers-danlos syndrome type I". Hum. Mol. Genet. 7 (2): 249–55. doi:10.1093/hmg/7.2.249. PMID 9425231.
Bertelli R, Valenti F, Oleggini R, et al. (1998). "Cell-specific regulation of alpha1(III) and alpha2(V) collagen by TGF-beta1 in tubulointerstitial cell models". Nephrol. Dial. Transplant. 13 (3): 573–9. doi:10.1093/ndt/13.3.573. PMID 9550630.
Shrivastava A, Radziejewski C, Campbell E, et al. (1998). "An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors". Mol. Cell. 1 (1): 25–34. doi:10.1016/S1097-2765(00)80004-0. PMID 9659900.
Richards AJ, Martin S, Nicholls AC, et al. (1999). "A single base mutation in COL5A2 causes Ehlers-Danlos syndrome type II". J. Med. Genet. 35 (10): 846–8. doi:10.1136/jmg.35.10.846. PMC1051462. PMID 9783710.
Wenstrup RJ, Florer JB, Willing MC, et al. (2001). "COL5A1 haploinsufficiency is a common molecular mechanism underlying the classical form of EDS". Am. J. Hum. Genet. 66 (6): 1766–76. doi:10.1086/302930. PMC1378044. PMID 10777716.
Välkkilä M, Melkoniemi M, Kvist L, et al. (2002). "Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has evolved differently than the other minor fibrillar collagen genes". Matrix Biol. 20 (5–6): 357–66. doi:10.1016/S0945-053X(01)00145-7. PMID 11566270.
Unsöld C, Pappano WN, Imamura Y, et al. (2002). "Biosynthetic processing of the pro-alpha 1(V)2pro-alpha 2(V) collagen heterotrimer by bone morphogenetic protein-1 and furin-like proprotein convertases". J. Biol. Chem. 277 (7): 5596–602. doi:10.1074/jbc.M110003200. PMID 11741999.
Grond-Ginsbach C, Wigger F, Morcher M, et al. (2002). "Sequence analysis of the COL5A2 gene in patients with spontaneous cervical artery dissections". Neurology. 58 (7): 1103–5. doi:10.1212/wnl.58.7.1103. PMID 11940702. S2CID 11310943.
Takahara K, Schwarze U, Imamura Y, et al. (2002). "Order of Intron Removal Influences Multiple Splice Outcomes, Including a Two-Exon Skip, in a COL5A1 Acceptor-Site Mutation That Results in Abnormal Pro-α1(V) N-Propeptides and Ehlers-Danlos Syndrome Type I". Am. J. Hum. Genet. 71 (3): 451–65. doi:10.1086/342099. PMC379186. PMID 12145749.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
External linksEdit
Ehlers-Danlos Syndrome, Classic Type. Includes: Ehlers-Danlos Syndrome Type I, Ehlers-Danlos Syndrome Type II
This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.
collagen, type, alpha, collagen, alpha, chain, protein, that, humans, encoded, col5a2, gene, col5a2available, structurespdbortholog, search, pdbe, rcsblist, codes1a9aidentifiersaliasescol5a2, edsc, collagen, type, alpha, collagen, type, alpha, chain, edscl2ext. Collagen alpha 2 V chain is a protein that in humans is encoded by the COL5A2 gene 5 6 COL5A2Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1A9AIdentifiersAliasesCOL5A2 EDSC collagen type V alpha 2 collagen type V alpha 2 chain EDSCL2External IDsOMIM 120190 MGI 88458 HomoloGene 20119 GeneCards COL5A2Gene location Human Chr Chromosome 2 human 1 Band2q32 2Start189 031 898 bp 1 End189 225 312 bp 1 Gene location Mouse Chr Chromosome 1 mouse 2 Band1 1 C1 1Start45 413 481 bp 2 End45 542 442 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inperiodontal fiberstromal cell of endometriumtibiavisceral pleuraparietal pleurasynovial jointsmooth muscle tissuesynovial membranegallbladdersaphenous veinTop expressed incalvariabody of femurfossadermismolarcondyleinternal carotid arteryexternal carotid arteryvas deferensankleMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionmetal ion binding extracellular matrix structural constituent SMAD binding molecular function extracellular matrix structural constituent conferring tensile strengthCellular componentextracellular region endoplasmic reticulum lumen collagen collagen type V trimer extracellular matrix extracellular space collagen containing extracellular matrixBiological processeye morphogenesis skeletal system development collagen catabolic process ossification extracellular matrix organization cellular response to amino acid stimulus negative regulation of endodermal cell differentiation skin development collagen fibril organization notochord developmentSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez129012832EnsemblENSG00000204262ENSMUSG00000026042UniProtP05997Q3U962RefSeq mRNA NM 000393NM 007737NM 172972RefSeq protein NP 000384NP 031763Location UCSC Chr 2 189 03 189 23 MbChr 1 45 41 45 54 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseThis gene encodes an alpha chain for one of the low abundance fibrillar collagens Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen This gene product is closely related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type with tissue specific chain combinations Mutations in this gene are associated with Ehlers Danlos syndrome classical type formerly known as types I and II 6 Contents 1 See also 2 References 3 Further reading 4 External linksSee also EditType V collagen TSR1References Edit a b c GRCh38 Ensembl release 89 ENSG00000204262 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000026042 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Greenspan DS Byers MG Eddy RL Cheng W Jani Sait S Shows TB May 1992 Human collagen gene COL5A1 maps to the q34 2 q34 3 region of chromosome 9 near the locus for nail patella syndrome Genomics 12 4 836 7 doi 10 1016 0888 7543 92 90320 R PMID 1572660 a b Entrez Gene COL5A2 collagen type V alpha 2 Further reading EditMann K 1992 Isolation of the alpha 3 chain of human type V collagen and characterization by partial sequencing Biol Chem Hoppe Seyler 373 2 69 75 doi 10 1515 bchm3 1992 373 1 69 PMID 1571108 Greenspan DS Lee ST Lee BS Hoffman GG 1992 Homology between alpha 2 V and alpha 1 III collagen promoters and evidence for negatively acting elements in the alpha 2 V first intron and 5 flanking sequences Gene Expr 1 1 29 39 PMC 5952197 PMID 1820205 Myers JC Loidl HR Seyer JM Dion AS 1985 Complete primary structure of the human alpha 2 type V procollagen COOH terminal propeptide J Biol Chem 260 20 11216 22 doi 10 1016 S0021 9258 17 39168 8 PMID 2411731 Woodbury D Benson Chanda V Ramirez F 1989 Amino terminal propeptide of human pro alpha 2 V collagen conforms to the structural criteria of a fibrillar procollagen molecule J Biol Chem 264 5 2735 8 doi 10 1016 S0021 9258 19 81674 5 PMID 2914927 Myers JC Loidl HR Stolle CA Seyer JM 1985 Partial covalent structure of the human alpha 2 type V collagen chain J Biol Chem 260 9 5533 41 doi 10 1016 S0021 9258 18 89055 X PMID 2985598 Weil D Bernard M Gargano S Ramirez F 1987 The pro alpha 2 V collagen gene is evolutionarily related to the major fibrillar forming collagens Nucleic Acids Res 15 1 181 98 doi 10 1093 nar 15 1 181 PMC 340404 PMID 3029669 Tsipouras P Schwartz RC Liddell AC et al 1989 Genetic distance of two fibrillar collagen loci COL3A1 and COL5A2 located on the long arm of human chromosome 2 Genomics 3 3 275 7 doi 10 1016 0888 7543 88 90089 4 PMID 3224983 Emanuel BS Cannizzaro LA Seyer JM Myers JC 1985 Human alpha 1 III and alpha 2 V procollagen genes are located on the long arm of chromosome 2 Proc Natl Acad Sci U S A 82 10 3385 9 Bibcode 1985PNAS 82 3385E doi 10 1073 pnas 82 10 3385 PMC 397780 PMID 3858826 Moradi Ameli M Rousseau JC Kleman JP et al 1994 Diversity in the processing events at the N terminus of type V collagen Eur J Biochem 221 3 987 95 doi 10 1111 j 1432 1033 1994 tb18815 x PMID 8181482 Wright GD Hughes AE Regan M Doherty M 1996 Association of two loci on chromosome 2q with nodal osteoarthritis Ann Rheum Dis 55 5 317 9 doi 10 1136 ard 55 5 317 PMC 1010169 PMID 8660106 Michalickova K Susic M Willing MC et al 1998 Mutations of the alpha2 V chain of type V collagen impair matrix assembly and produce ehlers danlos syndrome type I Hum Mol Genet 7 2 249 55 doi 10 1093 hmg 7 2 249 PMID 9425231 Bertelli R Valenti F Oleggini R et al 1998 Cell specific regulation of alpha1 III and alpha2 V collagen by TGF beta1 in tubulointerstitial cell models Nephrol Dial Transplant 13 3 573 9 doi 10 1093 ndt 13 3 573 PMID 9550630 Shrivastava A Radziejewski C Campbell E et al 1998 An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors Mol Cell 1 1 25 34 doi 10 1016 S1097 2765 00 80004 0 PMID 9659900 Richards AJ Martin S Nicholls AC et al 1999 A single base mutation in COL5A2 causes Ehlers Danlos syndrome type II J Med Genet 35 10 846 8 doi 10 1136 jmg 35 10 846 PMC 1051462 PMID 9783710 Wenstrup RJ Florer JB Willing MC et al 2001 COL5A1 haploinsufficiency is a common molecular mechanism underlying the classical form of EDS Am J Hum Genet 66 6 1766 76 doi 10 1086 302930 PMC 1378044 PMID 10777716 Valkkila M Melkoniemi M Kvist L et al 2002 Genomic organization of the human COL3A1 and COL5A2 genes COL5A2 has evolved differently than the other minor fibrillar collagen genes Matrix Biol 20 5 6 357 66 doi 10 1016 S0945 053X 01 00145 7 PMID 11566270 Unsold C Pappano WN Imamura Y et al 2002 Biosynthetic processing of the pro alpha 1 V 2pro alpha 2 V collagen heterotrimer by bone morphogenetic protein 1 and furin like proprotein convertases J Biol Chem 277 7 5596 602 doi 10 1074 jbc M110003200 PMID 11741999 Grond Ginsbach C Wigger F Morcher M et al 2002 Sequence analysis of the COL5A2 gene in patients with spontaneous cervical artery dissections Neurology 58 7 1103 5 doi 10 1212 wnl 58 7 1103 PMID 11940702 S2CID 11310943 Takahara K Schwarze U Imamura Y et al 2002 Order of Intron Removal Influences Multiple Splice Outcomes Including a Two Exon Skip in a COL5A1 Acceptor Site Mutation That Results in Abnormal Pro a1 V N Propeptides and Ehlers Danlos Syndrome Type I Am J Hum Genet 71 3 451 65 doi 10 1086 342099 PMC 379186 PMID 12145749 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 External links EditEhlers Danlos Syndrome Classic Type Includes Ehlers Danlos Syndrome Type I Ehlers Danlos Syndrome Type II nbsp This article on a gene on human chromosome 2 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Collagen type V alpha 2 amp oldid 1170676441, wikipedia, wiki, book, books, library,
