{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P02452","secondaryAccessions":["O76045","P78441","Q13896","Q13902","Q13903","Q14037","Q14992","Q15176","Q15201","Q16050","Q59F64","Q7KZ30","Q7KZ34","Q8IVI5","Q8N473","Q9UML6","Q9UMM7"],"uniProtkbId":"CO1A1_HUMAN","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-02-23","entryVersion":271,"sequenceVersion":6},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Collagen alpha-1(I) chain"}},"alternativeNames":[{"fullName":{"value":"Alpha-1 type I collagen"}}],"flag":"Precursor"},"genes":[{"geneName":{"value":"COL1A1"}}],"comments":[{"texts":[{"value":"Type I collagen is a member of group I collagen (fibrillar forming collagen)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P02453"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P02454"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14749390"}],"value":"Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 (By similarity). Interacts with TRAM2 (PubMed:14749390). Interacts with MFAP4 in a Ca (2+)-dependent manner (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P02452","intActId":"EBI-982999"},"interactantTwo":{"uniProtKBAccession":"P08123","geneName":"COL1A2","intActId":"EBI-983038"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P02452","intActId":"EBI-982999"},"interactantTwo":{"uniProtKBAccession":"P02751","geneName":"FN1","intActId":"EBI-1220319"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P02452","intActId":"EBI-982999"},"interactantTwo":{"uniProtKBAccession":"Q14145","geneName":"KEAP1","intActId":"EBI-751001"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P02452","intActId":"EBI-982999"},"interactantTwo":{"uniProtKBAccession":"Q8TBP6","geneName":"SLC25A40","intActId":"EBI-16769620"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P02452","intActId":"EBI-982999"},"interactantTwo":{"uniProtKBAccession":"O01949","geneName":"AAEL010235","intActId":"EBI-7685554"},"numberOfExperiments":5,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00793"}],"value":"Secreted, extracellular space, extracellular matrix","id":"SL-0111"}}]},{"texts":[{"value":"Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"The 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 (By similarity)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4319110"}],"value":"Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P11087"}],"value":"Contains 3-hydroxyproline at a few sites. 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