Collagen, type V, alpha 3, also known as COL5A3, is a human gene.cite web | title = Entrez Gene: COL5A3 collagen, type V, alpha 3| url =| accessdate = ]

section_title =
summary_text = 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.cite web | title = Entrez Gene: COL5A3 collagen, type V, alpha 3| url =| accessdate = ]


Further reading

citations =
*cite journal | author=van der Rest M, Garrone R |title=Collagen family of proteins. |journal=FASEB J. |volume=5 |issue= 13 |pages= 2814–23 |year= 1991 |pmid= 1916105 |doi=
*cite journal | author=Fichard A, Kleman JP, Ruggiero F |title=Another look at collagen V and XI molecules. |journal=Matrix Biol. |volume=14 |issue= 7 |pages= 515–31 |year= 1996 |pmid= 8535602 |doi=
*cite journal | author=Mann K |title=Isolation of the alpha 3-chain of human type V collagen and characterization by partial sequencing. |journal=Biol. Chem. Hoppe-Seyler |volume=373 |issue= 2 |pages= 69–75 |year= 1992 |pmid= 1571108 |doi=
*cite journal | author=Niyibizi C, Fietzek PP, van der Rest M |title=Human placenta type V collagens. Evidence for the existence of an alpha 1(V) alpha 2(V) alpha 3(V) collagen molecule. |journal=J. Biol. Chem. |volume=259 |issue= 22 |pages= 14170–4 |year= 1984 |pmid= 6501291 |doi=
*cite journal | author=Abedin MZ, Ayad S, Weiss JB |title=Isolation and native characterization of cysteine-rich collagens from bovine placental tissues and uterus and their relationship to types IV and V collagens. |journal=Biosci. Rep. |volume=2 |issue= 7 |pages= 493–502 |year= 1982 |pmid= 7115902 |doi=
*cite journal | author=Rhodes RK, Miller EJ |title=Evidence for the existence of an alpha 1(V) alpha 2(V) alpha 3(V) collagen molecule in human placental tissue. |journal=Coll. Relat. Res. |volume=1 |issue= 4 |pages= 337–43 |year= 1982 |pmid= 7346227 |doi=
*cite journal | author=Kypreos KE, Sonenshein GE |title=Basic fibroblast growth factor decreases type V/XI collagen expression in cultured bovine aortic smooth muscle cells. |journal=J. Cell. Biochem. |volume=68 |issue= 2 |pages= 247–58 |year= 1998 |pmid= 9443080 |doi=
*cite journal | author=Imamura Y, Scott IC, Greenspan DS |title=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. |journal=J. Biol. Chem. |volume=275 |issue= 12 |pages= 8749–59 |year= 2000 |pmid= 10722718 |doi=
*cite journal | author=Chanut-Delalande H, Fichard A, Bernocco S, "et al." |title=Control of heterotypic fibril formation by collagen V is determined by chain stoichiometry. |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 24352–9 |year= 2001 |pmid= 11423559 |doi=
*cite journal | author=Gopalakrishnan B, Wang WM, Greenspan DS |title=Biosynthetic processing of the Pro-alpha1(V)Pro-alpha2(V)Pro-alpha3(V) procollagen heterotrimer. |journal=J. Biol. Chem. |volume=279 |issue= 29 |pages= 30904–12 |year= 2004 |pmid= 15136578 |doi= 10.1074/jbc.M402252200
*cite journal | author=Nagato H, Matsuo N, Sumiyoshi H, "et al." |title=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). |journal=J. Biol. Chem. |volume=279 |issue= 45 |pages= 46373–83 |year= 2004 |pmid= 15316020 |doi= 10.1074/jbc.M406069200

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