Collagen, type V, alpha 3

COL5A3
Identifiers
Aliases	COL5A3, collagen type V alpha 3 chain
External IDs	OMIM: 120216; MGI: 1858212; HomoloGene: 9253; GeneCards: COL5A3; OMA:COL5A3 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.2 Start 9,959,561 bp End 10,010,504 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 A3 Start 20,681,346 bp End 20,726,363 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve apex of heart canal of the cervix subcutaneous adipose tissue left uterine tube putamen ectocervix amygdala right frontal lobe dorsal motor nucleus of vagus nerve Top expressed in sciatic nerve white adipose tissue ankle subcutaneous adipose tissue umbilical cord lumbar spinal ganglion trachea soleus muscle vastus lateralis muscle brown adipose tissue More reference expression data BioGPS 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 extracellular region collagen endoplasmic reticulum lumen extracellular matrix extracellular space 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: 20.68 – 20.73 Mb PubMed search
Wikidata
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Collagen alpha-3(V) chain is a protein that in humans is encoded by the COL5A3 gene.

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.

Further reading

• van der Rest M, Garrone R (1991). "Collagen family of proteins". FASEB J. 5 (13): 2814–23. doi:10.1096/fasebj.5.13.1916105. PMID 1916105. S2CID 11261357.
• 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. doi:10.1016/S0021-9258(18)89872-6. 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. S2CID 22620593.
• 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. doi:10.1016/S0174-173X(81)80010-6. 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. S2CID 19211563.
• 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.