MGP Database

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MGP000617

UniProt Annotations

Entry Information
Gene Namecollagen, type III, alpha 1
Protein EntryCO3A1_HUMAN
UniProt IDP02461
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P02461-1; Sequence=Displayed; Name=2; IsoId=P02461-2; Sequence=VSP_022502; Note=No experimental confirmation available.;
DiseaseAortic aneurysm, familial abdominal (AAA) [MIM:100070]: A common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells. {ECO:0000269|PubMed:2243125, ECO:0000269|PubMed:2349939, ECO:0000269|PubMed:8514866}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.
DiseaseEhlers-Danlos syndrome 3 (EDS3) [MIM:130020]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. It is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity. {ECO:0000269|PubMed:7833919}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseEhlers-Danlos syndrome 4 (EDS4) [MIM:130050]: The most severe form of Ehlers-Danlos syndrome, a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas. {ECO:0000269|PubMed:10706896, ECO:0000269|PubMed:10923041, ECO:0000269|PubMed:11168790, ECO:0000269|PubMed:12694234, ECO:0000269|PubMed:12786757, ECO:0000269|PubMed:1352273, ECO:0000269|PubMed:1357232, ECO:0000269|PubMed:1370809, ECO:0000269|PubMed:1496983, ECO:0000269|PubMed:1895316, ECO:0000269|PubMed:2492273, ECO:0000269|PubMed:2808425, ECO:0000269|PubMed:7749417, ECO:0000269|PubMed:7912131, ECO:0000269|PubMed:8019562, ECO:0000269|PubMed:8098182, ECO:0000269|PubMed:8411057, ECO:0000269|PubMed:8664902, ECO:0000269|PubMed:8680408, ECO:0000269|PubMed:8884076, ECO:0000269|PubMed:8990011, ECO:0000269|PubMed:9036918, ECO:0000269|PubMed:9147870, ECO:0000269|PubMed:9452103, ECO:0000269|Ref.44, ECO:0000269|Ref.49}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DomainThe C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function.
FunctionCollagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of GPR56 in the developing brain and binding to GPR56 inhibits neuronal migration and activates the RhoA pathway by coupling GPR56 to GNA13 and possibly GNA12.
InteractionO01949:AAEL010235 (xeno); NbExp=2; IntAct=EBI-2431491, EBI-7685554;
PtmO-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.
PtmProline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:557335, ECO:0000269|PubMed:7016180}.
SimilarityBelongs to the fibrillar collagen family. {ECO:0000255|PROSITE-ProRule:PRU00793}.
SimilarityContains 1 fibrillar collagen NC1 domain. {ECO:0000255|PROSITE-ProRule:PRU00793}.
SimilarityContains 1 VWFC domain. {ECO:0000255|PROSITE- ProRule:PRU00220}.
Subcellular LocationSecreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
SubunitTrimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines.
Web ResourceName=COL3A1; Note=Collagen type III alpha-1 chain mutations; URL="http://www.le.ac.uk/genetics/collagen/col3a1.html";
Web ResourceName=Wikipedia; Note=Type-III collagen entry; URL="http://en.wikipedia.org/wiki/Type-III_collagen";
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