Collagen, type III, alpha 1

Collagen, type III, alpha 1
Rendering based on PDB 2V53.
Available structures PDB 2V53, 3DMW
Identifiers
Symbols	COL3A1; EDS4A; FLJ34534
External IDs	OMIM: 120180 MGI: 88453 HomoloGene: 55433 GeneCards: COL3A1 Gene
Gene Ontology Molecular function • integrin binding • integrin binding • extracellular matrix structural constituent • protein binding • SMAD binding • platelet-derived growth factor binding Cellular component • extracellular region • collagen • collagen type III • collagen type III • extracellular space • extracellular space • extracellular matrix Biological process • skeletal system development • blood vessel development • cell-matrix adhesion • transforming growth factor beta receptor signaling pathway • integrin-mediated signaling pathway • axon guidance • heart development • response to radiation • peptide cross-linking • platelet activation • collagen fibril organization • collagen fibril organization • collagen biosynthetic process • collagen biosynthetic process • response to cytokine stimulus • wound healing • wound healing • fibril organization • skin development • digestive tract development • negative regulation of immune response Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1281	12825
Ensembl	ENSG00000168542	ENSMUSG00000026043
UniProt	P02461	n/a
RefSeq (mRNA)	NM_000090.3	NM_009930.2
RefSeq (protein)	NP_000081.1	NP_034060.2
Location (UCSC)	Chr 2: 189.84 – 189.88 Mb	Chr 1: 45.37 – 45.41 Mb
PubMed search	[1]	[2]

Collagen alpha-1(III) chain is a protein that in humans is encoded by the COL3A1 gene^[1][2], which is located on chromosome 2.

Function

Collagen alpha-1(III) chain is a fibrillar collagen that is found in extensible connective tissues such as skin, lung, and the vascular system, frequently in association with type I collagen. Although alternate transcripts have been detected for this gene, they are the result of mutations; these mutations alter splicing, often leading to the exclusion of multiple exons.^[3]

Type-III collagen is a fibrous scleroprotein in bone, cartilage, tendon, bone marrow stroma and other connective tissue; yields gelatin on boiling.

Scleroprotein is a simple protein found in horny and cartilaginous tissues and in the lens of the eye.

Clinical significance

Mutations in this gene are associated with type III and IV Ehlers-Danlos syndrome and with aortic and arterial aneurysms.

See also

• Collagen
• Reticular fiber
• Ehlers-Danlos syndrome

References

1. ^ Janeczko RA, Ramirez F (Oct 1989). "Nucleotide and amino acid sequences of the entire human alpha 1 (III) collagen". Nucleic Acids Res 17 (16): 6742. doi:10.1093/nar/17.16.6742. PMC 318382. PMID 2780304. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=318382. 
2. ^ Superti-Furga A, Gugler E, Gitzelmann R, Steinmann B (Jun 1988). "Ehlers-Danlos syndrome type IV: a multi-exon deletion in one of the two COL3A1 alleles affecting structure, stability, and processing of type III procollagen". J Biol Chem 263 (13): 6226–32. PMID 2834369. 
3. ^ "Entrez Gene: COL3A1 collagen, type III, alpha 1 (Ehlers-Danlos syndrome type IV, autosomal dominant)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1281. 

Further reading

• Kuivaniemi H, Tromp G, Prockop DJ (1991). "Genetic causes of aortic aneurysms. Unlearning at least part of what the textbooks say.". J. Clin. Invest. 88 (5): 1441–4. doi:10.1172/JCI115452. PMC 295644. PMID 1939638. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=295644. 
• Kuivaniemi H, Tromp G, Prockop DJ (1997). "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels". Hum. Mutat. 9 (4): 300–15. doi:10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9. PMID 9101290. 

External links

• GeneReview/NCBI/NIH/UW entry on Ehlers-Danlos Syndrome Type IV
• MeSH Collagen+type+III