Collagen, type V, alpha 3

Collagen alpha-3(V) chain is a protein that in humans is encoded by the COL5A3 gene.[5][6]

COL5A3
Identifiers
Aliases	COL5A3, collagen type V alpha 3 chain
External IDs	OMIM: 120216 MGI: 1858212 HomoloGene: 9253 GeneCards: COL5A3
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19p13.2 Start 9,959,561 bp[1] End 10,010,504 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 A3 Start 20,770,050 bp[2] End 20,815,067 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • heparin binding • extracellular matrix structural constituent • collagen binding • extracellular matrix structural constituent conferring tensile strength • proteoglycan binding Cellular component • collagen type V trimer • proteinaceous extracellular matrix • extracellular region • collagen • endoplasmic reticulum lumen • extracellular matrix • extracellular • collagen-containing extracellular matrix Biological process • collagen catabolic process • cell-matrix adhesion • extracellular matrix organization • skin development • collagen fibril organization • cell adhesion Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	50509	53867
Ensembl	ENSG00000080573	ENSMUSG00000004098
UniProt	P25940	Q9JLI2
RefSeq (mRNA)	NM_015719	NM_016919 NM_001317388
RefSeq (protein)	NP_056534	NP_001304317 NP_058615
Location (UCSC)	Chr 19: 9.96 – 10.01 Mb	Chr 9: 20.77 – 20.82 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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 thought to be responsible for the symptoms of a subset of patients with Ehlers-Danlos syndrome type III. Messages of several sizes can be detected in northern blots but sequence information cannot confirm the identity of the shorter messages.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000080573 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000004098 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Imamura Y, Scott IC, Greenspan DS (Apr 2000). "The pro-alpha3(V) collagen chain. Complete primary structure, expression domains in adult and developing tissues, and comparison to the structures and expression domains of the other types V and XI procollagen chains". J Biol Chem. 275 (12): 8749–59. doi:10.1074/jbc.275.12.8749. PMID 10722718.
6. "Entrez Gene: COL5A3 collagen, type V, alpha 3".

Further reading

• van der Rest M, Garrone R (1991). "Collagen family of proteins". FASEB J. 5 (13): 2814–23. PMID 1916105.
• Fichard A, Kleman JP, Ruggiero F (1996). "Another look at collagen V and XI molecules". Matrix Biol. 14 (7): 515–31. doi:10.1016/S0945-053X(05)80001-0. PMID 8535602.
• 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.
• Niyibizi C, Fietzek PP, van der Rest M (1984). "Human placenta type V collagens. Evidence for the existence of an alpha 1(V) alpha 2(V) alpha 3(V) collagen molecule". J. Biol. Chem. 259 (22): 14170–4. PMID 6501291.
• Abedin MZ, Ayad S, Weiss JB (1982). "Isolation and native characterization of cysteine-rich collagens from bovine placental tissues and uterus and their relationship to types IV and V collagens". Biosci. Rep. 2 (7): 493–502. doi:10.1007/BF01115247. PMID 7115902.
• Rhodes RK, Miller EJ (1982). "Evidence for the existence of an alpha 1(V) alpha 2(V) alpha 3(V) collagen molecule in human placental tissue". Coll. Relat. Res. 1 (4): 337–43. PMID 7346227.
• Kypreos KE, Sonenshein GE (1998). "Basic fibroblast growth factor decreases type V/XI collagen expression in cultured bovine aortic smooth muscle cells". J. Cell. Biochem. 68 (2): 247–58. doi:10.1002/(SICI)1097-4644(19980201)68:2<247::AID-JCB11>3.0.CO;2-C. PMID 9443080.
• Chanut-Delalande H, Fichard A, Bernocco S, et al. (2001). "Control of heterotypic fibril formation by collagen V is determined by chain stoichiometry". J. Biol. Chem. 276 (26): 24352–9. doi:10.1074/jbc.M101182200. PMID 11423559.
• Gopalakrishnan B, Wang WM, Greenspan DS (2004). "Biosynthetic processing of the Pro-alpha1(V)Pro-alpha2(V)Pro-alpha3(V) procollagen heterotrimer". J. Biol. Chem. 279 (29): 30904–12. doi:10.1074/jbc.M402252200. PMID 15136578.
• Nagato H, Matsuo N, Sumiyoshi H, et al. (2004). "The transcription factor CCAAT-binding factor CBF/NF-Y and two repressors regulate the core promoter of the human pro-alpha3(V) collagen gene (COL5A3)". J. Biol. Chem. 279 (45): 46373–83. doi:10.1074/jbc.M406069200. PMID 15316020.