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collagen 1 alpha-1; collagen alpha-1(I) chain; alpha-1 type I collagen (COL1A1)

Function: - type 1 collagen is a member of group 1 collagen (fibrillar forming collagen) - Pro at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains - Pro at the second position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some of the chains - O-linked glycan consists of a Glc-gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group - trimers of one collagen 1 alpha-2 & two collagen 1 alpha-1 chains - interacts with MRC2 (putative) - interacts with TRAM2 Structure: - belongs to the fibrillar collagen family - contains 1 fibrillar collagen NC1 domain - contains 1 VWFC domain Compartment: - secreted, extracellular space, extracellular matrix (putative) Expression: - forms the fibrils of tendon, ligaments & bones - in bones, the fibrils are mineralized with Ca+2 hydroxyapatite Pathology: - defects in COL1A1 are the cause of: a) Caffey disease (infantile cortical hyperostosis) b) Ehlers-Danlos syndrome type 7A - defects in COL1A1 are a cause of a) Ehlers-Danlos syndrome type 1 b) osteogenesis imperfecta type 1 c) osteogenesis imperfecta type 2 d) osteogenesis imperfecta type 3 e) osteogenesis imperfecta type 4 - genetic variations in COL1A1 are a cause of susceptibility to osteoporosis - chromosomal translocation t(17;22)(q22;q13) involving COL1A1 with PDGFB is found in dermatofibrosarcoma protuberans Note: collagen type I alpha 1 (COL1A1)

Related

COL1A1 gene

General

collagen subunit

Properties

SIZE: entity length = 1464 aa MW = 139 kD MOTIF: signal sequence {1-22} VWFC domain {38-96} proteolytic site {161-162} Nonhelical region {162-178} Triple-helical region {179-1192} MOTIF: Cell attachment {745-747} proteolytic site {953-954} Cell attachment {1093-1095} Nonhelical region {1193-1218} proteolytic site {1218-1219} Fibrillar collagen NC1 {1229-1464} MOTIF: cysteine residue {C1259} MODIFICATION: cysteine residue {C-INTERCHAIN} cysteine residue {C1265} MODIFICATION: cysteine residue {C-INTERCHAIN} cysteine residue {C1282} MODIFICATION: cysteine residue {C-INTERCHAIN} cysteine residue {C1291} MODIFICATION: cysteine residue {C-INTERCHAIN} cysteine residue {C1299} MODIFICATION: cysteine residue {C1462} N-glycosylation site {N1365} cysteine residue {C1370} MODIFICATION: cysteine residue {C1415} cysteine residue {C1415} MODIFICATION: cysteine residue {C1370} cysteine residue {C1462} MODIFICATION: cysteine residue {C1299}

Database Correlations

OMIM correlations MORBIDMAP 120150 UniProt P02452 PFAM correlations Entrez Gene 1277 Kegg hsa:1277

References

  1. UniProt :accession P02452
  2. Osteogenesis imperfecta variant database http://oi.gene.le.ac.uk/home.php?select_db=COL1A1
  3. Atlas of Genetics & Cytogenetics in Oncology & Haematology http://atlasgeneticsoncology.org/genes/COL1A1ID186.html
  4. GeneReviews http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/COL1A1
  5. Wikipedia; Note: type-I collagen entry http://en.wikipedia.org/wiki/type-I_collagen
  6. Andrews BS. Is the WKS motif the tissue-factor binding site for coagulation factor VII? Trends Biochem Sci. 1991 Jan;16(1):31-6. Review. PMID: 2053135
  7. Molecular Cell Biology (2nd ed) Darnell J; Lodish H & Baltimore D (eds), Scientific American Books, WH Freeman, NY 1990, pg 906
  8. OMIM :accession 120150
  9. Entrez Gene :accession 1277

Component-of

collagen type-1