Collagen, type VII, alpha 1

Collagen, type VII, alpha 1
Collagen, type VII, alpha 1
Symbols COL7A1; EBD1; EBDCT; EBR1
External IDs OMIM120120 MGI88462 HomoloGene73 GeneCards: COL7A1 Gene
RNA expression pattern
PBB GE COL7A1 204136 at tn.png
PBB GE COL7A1 217312 s at tn.png
More reference expression data
Species Human Mouse
Entrez 1294 12836
Ensembl ENSG00000114270 ENSMUSG00000025650
UniProt Q02388 n/a
RefSeq (mRNA) NM_000094 NM_007738.3
RefSeq (protein) NP_000085 NP_031764.2
Location (UCSC) Chr 3:
48.6 – 48.63 Mb
Chr 9:
108.86 – 108.89 Mb
PubMed search [1] [2]

Collagen alpha-1(VII) chain is a protein that in humans is encoded by the COL7A1 gene.[1]



This gene encodes the alpha chain of type VII collagen. The type VII collagen fibril, composed of three identical alpha collagen chains, is restricted to the basement zone beneath stratified squamous epithelia. It functions as an anchoring fibril between the external epithelia and the underlying stroma. Mutations in this gene are associated with all forms of dystrophic epidermolysis bullosa. In the absence of mutations, however, an autoimmune response against type VII collagen can result in an acquired form of this disease called epidermolysis bullosa acquisita.[2]

Type VII collagen is also found in the retina; its function in this organ is unknown.[3]

COL7A1 is located on the short arm of human chromosome 3, in the chromosomal region denoted 3p21.31. The gene is approximately 31,000 base pairs in size and is remarkable for the extreme fragmentation of its coding sequence into 118 exons.[4][5] COL7A1 is transcribed into an mRNA of 9,287 base pairs.[6] In the skin, the type VII collagen protein is synthesized by keratinocytes and dermal fibroblasts.[7]

The symbol for the orthologous gene in the mouse is Col7a1.

Clinical significance

The inherited disease, dystrophic epidermolysis bullosa, is caused by recessive or dominant mutations in COL7A1.[8]

Epidermolysis bullosa acquisita involves an autoimmune reaction to this form of collagen.[9]


Collagen, type VII, alpha 1 has been shown to interact with Laminin, alpha 5[10] and Fibronectin.[11][12]

See also


  1. ^ Parente MG, Chung LC, Ryynanen J, Woodley DT, Wynn KC, Bauer EA, Mattei MG, Chu ML, Uitto J (Sep 1991). "Human type VII collagen: cDNA cloning and chromosomal mapping of the gene". Proc Natl Acad Sci U S A 88 (16): 6931–5. doi:10.1073/pnas.88.16.6931. PMC 52207. PMID 1871109. 
  2. ^ "COL7A1 collagen, type VII, alpha 1 (epidermolysis bullosa, dystrophic, dominant and recessive)". NCBI Entrez Gene database. 
  3. ^ Ponsioen TL, van Luyn MJ, van der Worp RJ, et al. (2008). "Collagen distribution in the human vitreoretinal interface.". Invest. Ophthalmol. Vis. Sci. 49 (9): 4089–95. doi:10.1167/iovs.07-1456. PMID 18450587. 
  4. ^ Christiano AM, Hoffman GG, Chung-Honet LC, et al. (1994). "Structural organization of the human type VII collagen gene (COL7A1), composed of more exons than any previously characterized gene.". Genomics 21 (1): 169–79. doi:10.1006/geno.1994.1239. PMID 8088784. 
  5. ^ "COL7A1 genomic sequence". NCBI Entrez Nucleotide database. 
  6. ^ "COL7A1 mRNA sequence". NCBI Entrez Nucleotide database. 
  7. ^ Online 'Mendelian Inheritance in Man' (OMIM) COL7A1 -120120
  8. ^ Dang N, Murrell DF (2008). "Mutation analysis and characterization of COL7A1 mutations in dystrophic epidermolysis bullosa.". Exp. Dermatol. 17 (7): 553–68. doi:10.1111/j.1600-0625.2008.00723.x. PMID 18558993. 
  9. ^ Helen Chapel; Mansel Haeney; Siraj Misbah (2006). Essentials of clinical immunology. Wiley-Blackwell. pp. 207–. ISBN 9781405127615. Retrieved 25 June 2010. 
  10. ^ Rousselle, P; Keene D R, Ruggiero F, Champliaud M F, Rest M, Burgeson R E (Aug. 1997). "Laminin 5 binds the NC-1 domain of type VII collagen". J. Cell Biol. (UNITED STATES) 138 (3): 719–28. doi:10.1083/jcb.138.3.719. ISSN 0021-9525. PMC 2141627. PMID 9245798. 
  11. ^ Lapiere, J C; Chen J D, Iwasaki T, Hu L, Uitto J, Woodley D T (Nov. 1994). "Type VII collagen specifically binds fibronectin via a unique subdomain within the collagenous triple helix". J. Invest. Dermatol. (UNITED STATES) 103 (5): 637–41. doi:10.1111/1523-1747.ep12398270. ISSN 0022-202X. PMID 7963647. 
  12. ^ Chen, M; Marinkovich M P, Veis A, Cai X, Rao C N, O'Toole E A, Woodley D T (Jun. 1997). "Interactions of the amino-terminal noncollagenous (NC1) domain of type VII collagen with extracellular matrix components. A potential role in epidermal-dermal adherence in human skin". J. Biol. Chem. (UNITED STATES) 272 (23): 14516–22. doi:10.1074/jbc.272.23.14516. ISSN 0021-9258. PMID 9169408. 

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