MGP Database

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MGP003271

UniProt Annotations

Entry Information
Gene Namecollagen, type XIV, alpha 1
Protein EntryCOEA1_HUMAN
UniProt IDQ05707
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=1 {ECO:0000269|PubMed:9427527}; Synonyms=Undulin 1 {ECO:0000303|PubMed:1716629}, Un1 {ECO:0000303|PubMed:1716629}; IsoId=Q05707-1; Sequence=Displayed; Name=2 {ECO:0000269|PubMed:9427527}; IsoId=Q05707-2; Sequence=VSP_051654; Name=3 {ECO:0000269|PubMed:1716629}; Synonyms=Undulin 2 {ECO:0000303|PubMed:1716629}, Un2 {ECO:0000303|PubMed:1716629}; IsoId=Q05707-3; Sequence=VSP_051653;
FunctionPlays an adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors (By similarity). {ECO:0000250}.
PtmLysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates. {ECO:0000250|UniProtKB:P32018}.
PtmMay contain numerous cysteine residues involved in inter- and intramolecular disulfide bonding. {ECO:0000250|UniProtKB:P32018}.
PtmProlines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P32018}.
Sequence CautionSequence=AAA36795.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305}; Sequence=AAH14640.1; Type=Frameshift; Positions=1047; Evidence={ECO:0000305};
SimilarityBelongs to the fibril-associated collagens with interrupted helices (FACIT) family. {ECO:0000255}.
SimilarityContains 1 laminin G-like domain. {ECO:0000305}.
SimilarityContains 2 VWFA domains. {ECO:0000255|PROSITE- ProRule:PRU00219}.
SimilarityContains 4 collagen-like domains. {ECO:0000305}.
SimilarityContains 8 fibronectin type-III domains. {ECO:0000255|PROSITE-ProRule:PRU00316}.
Subcellular LocationSecreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P32018}.
SubunitHomotrimer. {ECO:0000250|UniProtKB:P32018}.
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