COL4A5

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Collagen, type IV, alpha 5 (Alport syndrome)
Identifiers
Symbols COL4A5 ; ASLN; ATS; CA54; MGC42377
External IDs OMIM: 303630 MGI88456 HomoloGene22422
Orthologs

| | bgcolor="#C3FDB8" | Human | bgcolor="#C3FDB8" | Mouse |-

    | bgcolor="#C3FDB8" | Entrez 
    | bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd"| 1287
    | bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd"| 12830

|-

     | bgcolor="#C3FDB8" | Ensembl
     | bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd"| ENSG00000188153
     | bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd"| ENSMUSG00000031274

|-

    | bgcolor="#C3FDB8" | Uniprot
    | bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd"| P29400
    | bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd"| na

|-

    | bgcolor="#C3FDB8" | Refseq
    | bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd" | NM_000495 (mRNA)
NP_000486 (protein)
| bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd" |XM_623033 (mRNA)
XP_623033 (protein)

|-

    | bgcolor="#C3FDB8" | Location
    | bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd"|  Chr X: 107.57 - 107.83 Mb 
    | bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd"|  Chr X: 136.72 -  136.94 Mb 

|-

|-

    | bgcolor="#C3FDB8" | Pubmed search 
    | bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd"| [1]
| bgcolor="#eeeeee" style="border-top:2px solid #dddddd; border-right:2px solid #dddddd"| [2]
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Collagen, type IV, alpha 5 (Alport syndrome), also known as COL4A5, is a human gene.

This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. Mutations in this gene are associated with X-linked Alport syndrome, also known as hereditary nephritis. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Three transcript variants have been identified for this gene.[1]

See also

References

  1. "Entrez Gene: COL4A5 collagen, type IV, alpha 5 (Alport syndrome)".

Further reading

  • Lemmink HH, Schröder CH, Monnens LA, Smeets HJ (1997). "The clinical spectrum of type IV collagen mutations". Hum. Mutat. 9 (6): 477–99. doi:10.1002/(SICI)1098-1004(1997)9:6<477::AID-HUMU1>3.0.CO;2-#. PMID 9195222.
  • Ständer M, Naumann U, Wick W, Weller M (1999). "Transforming growth factor-beta and p-21: multiple molecular targets of decorin-mediated suppression of neoplastic growth". Cell Tissue Res. 296 (2): 221–7. PMID 10382266.
  • Kurpakus Wheater M, Kernacki KA, Hazlett LD (1999). "Corneal cell proteins and ocular surface pathology". Biotechnic & histochemistry : official publication of the Biological Stain Commission. 74 (3): 146–59. PMID 10416788.
  • Zhou J, Hertz JM, Leinonen A, Tryggvason K (1992). "Complete amino acid sequence of the human alpha 5 (IV) collagen chain and identification of a single-base mutation in exon 23 converting glycine 521 in the collagenous domain to cysteine in an Alport syndrome patient". J. Biol. Chem. 267 (18): 12475–81. PMID 1352287.
  • Renieri A, Seri M, Myers JC; et al. (1993). "De novo mutation in the COL4A5 gene converting glycine 325 to glutamic acid in Alport syndrome". Hum. Mol. Genet. 1 (2): 127–9. PMID 1363780.
  • Knebelmann B, Deschenes G, Gros F; et al. (1992). "Substitution of arginine for glycine 325 in the collagen alpha 5 (IV) chain associated with X-linked Alport syndrome: characterization of the mutation by direct sequencing of PCR-amplified lymphoblast cDNA fragments". Am. J. Hum. Genet. 51 (1): 135–42. PMID 1376965.
  • Ghebrehiwet B, Peerschke EI, Hong Y; et al. (1992). "Short amino acid sequences derived from C1q receptor (C1q-R) show homology with the alpha chains of fibronectin and vitronectin receptors and collagen type IV". J. Leukoc. Biol. 51 (6): 546–56. PMID 1377218.
  • Zhou J, Barker DF, Hostikka SL; et al. (1991). "Single base mutation in alpha 5(IV) collagen chain gene converting a conserved cysteine to serine in Alport syndrome". Genomics. 9 (1): 10–8. PMID 1672282.
  • Hostikka SL, Eddy RL, Byers MG; et al. (1990). "Identification of a distinct type IV collagen alpha chain with restricted kidney distribution and assignment of its gene to the locus of X chromosome-linked Alport syndrome". Proc. Natl. Acad. Sci. U.S.A. 87 (4): 1606–10. PMID 1689491.
  • Gupta S, Batchu RB, Datta K (1992). "Purification, partial characterization of rat kidney hyaluronic acid binding protein and its localization on the cell surface". Eur. J. Cell Biol. 56 (1): 58–67. PMID 1724753.
  • Zhou J, Hostikka SL, Chow LT, Tryggvason K (1991). "Characterization of the 3' half of the human type IV collagen alpha 5 gene that is affected in the Alport syndrome". Genomics. 9 (1): 1–9. PMID 2004755.
  • Myers JC, Jones TA, Pohjolainen ER; et al. (1990). "Molecular cloning of alpha 5(IV) collagen and assignment of the gene to the region of the X chromosome containing the Alport syndrome locus". Am. J. Hum. Genet. 46 (6): 1024–33. PMID 2339699.
  • Barker DF, Hostikka SL, Zhou J; et al. (1990). "Identification of mutations in the COL4A5 collagen gene in Alport syndrome". Science. 248 (4960): 1224–7. PMID 2349482.
  • Pihlajaniemi T, Pohjolainen ER, Myers JC (1990). "Complete primary structure of the triple-helical region and the carboxyl-terminal domain of a new type IV collagen chain, alpha 5(IV)". J. Biol. Chem. 265 (23): 13758–66. PMID 2380186.
  • Hernandez MR, Igoe F, Neufeld AH (1986). "Extracellular matrix of the human optic nerve head". Am. J. Ophthalmol. 102 (2): 139–48. PMID 2426947.
  • Glant TT, Hadházy C, Mikecz K, Sipos A (1985). "Appearance and persistence of fibronectin in cartilage. Specific interaction of fibronectin with collagen type II". Histochemistry. 82 (2): 149–58. PMID 3997552.
  • Matsubara T, Trüeb B, Fehr K; et al. (1984). "The localization and secretion of type IV collagen in synovial capillaries by immunohistochemistry using a monoclonal antibody against human type IV collagen". Exp. Cell Biol. 52 (3): 159–69. PMID 6386565.
  • Uscanga L, Kennedy RH, Stocker S; et al. (1984). "Immunolocalization of collagen types, laminin and fibronectin in the normal human pancreas". Digestion. 30 (3): 158–64. PMID 6389236.
  • Sundarraj N, Willson J (1982). "Monoclonal antibody to human basement membrane collagen type IV". Immunology. 47 (1): 133–40. PMID 6811420.
  • Hahn E, Wick G, Pencev D, Timpl R (1980). "Distribution of basement membrane proteins in normal and fibrotic human liver: collagen type IV, laminin, and fibronectin". Gut. 21 (1): 63–71. PMID 6988303.

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