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UniProt functional annotation for P17301 | ||
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| UniProt code: P17301. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix. |
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| Function: | |
(Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human rotavirus A. {ECO:0000269|PubMed:12941907}. |
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| Function: | |
(Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human echoviruses 1 and 8. {ECO:0000269|PubMed:8411387}. |
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| Subunit: | |
Heterodimer of an alpha and a beta subunit. Alpha-2 associates with beta-1. Interacts with HPS5 and RAB21. {ECO:0000269|PubMed:16754960}. |
| Subunit: | |
(Microbial infection) Integrin ITGA2:ITGB1 interacts (via ITAG2 I-domain) with rotavirus A VP4 protein. {ECO:0000269|PubMed:12941907}. |
| Subunit: | |
(Microbial infection) Integrin ITGA2:ITGB1 interacts with human echoviruses 1 and 8 capsid proteins. {ECO:0000269|PubMed:8411387}. |
| Subcellular location: | |
Membrane; Single-pass type I membrane protein. |
| Domain: | |
The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage. |
| Polymorphism: | |
Position 534 is associated with platelet-specific alloantigen HPA-5 (Br). HPA-5B/Br(a) has Lys-534 and HPA-5A/Br(b) has Glu-534. HPA-5B is involved in neonatal alloimmune thrombocytopenia (NAIT or NATP). The Lys-534-Glu polymorphism may play a role in coronary artery disease (CAD). {ECO:0000269|PubMed:7901236}. |
| Similarity: | |
Belongs to the integrin alpha chain family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.