COL4A5
Collagen, type IV, alpha 5
Protein-coding gene in humans
"Ca54" redirects here. For the isotope of calcium (Ca-54 or 54Ca), see Calcium-54.
Collagen alpha-5(IV) chain is a protein that in humans is encoded by the COL4A5 gene.
Quick Facts COL4A5, Identifiers ...
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| Aliases | COL4A5, ASLN, ATS, CA54, collagen type IV alpha 5, collagen type IV alpha 5 chain, ATS1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 303630 MGI: 88456 HomoloGene: 133559 GeneCards: COL4A5 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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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.[5]
ARUP COL4A5 gene variant database
LOVD Alport gene variant databases (COL4A5, COL4A3, COL4A4)[permanent dead link]
- "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- 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-#. hdl:2066/25010. PMID 9195222. S2CID 196601220.
- 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. doi:10.1007/s004410051283. PMID 10382266. S2CID 20282995.
- Kurpakus Wheater M, Kernacki KA, Hazlett LD (1999). "Corneal cell proteins and ocular surface pathology". Biotechnic & Histochemistry. 74 (3): 146–59. doi:10.3109/10520299909047967. 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. doi:10.1016/S0021-9258(18)42301-0. 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. doi:10.1093/hmg/1.2.127. 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. PMC 1682875. 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. doi:10.1002/jlb.51.6.546. PMID 1377218. S2CID 1214598.
- 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. doi:10.1016/0888-7543(91)90215-Z. 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. Bibcode:1990PNAS...87.1606H. doi:10.1073/pnas.87.4.1606. PMC 53524. 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. doi:10.1016/0888-7543(91)90214-Y. 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. PMC 1683837. 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. Bibcode:1990Sci...248.1224B. doi:10.1126/science.2349482. 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. doi:10.1016/S0021-9258(18)77414-0. PMID 2380186.
- Hernandez MR, Igoe F, Neufeld AH (1986). "Extracellular matrix of the human optic nerve head". Am. J. Ophthalmol. 102 (2): 139–48. doi:10.1016/0002-9394(86)90134-0. 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. doi:10.1007/bf00708199. PMID 3997552. S2CID 19401258.
- 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. doi:10.1159/000163256. 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. doi:10.1159/000199100. PMID 6389236.
- Sundarraj N, Willson J (1982). "Monoclonal antibody to human basement membrane collagen type IV". Immunology. 47 (1): 133–40. PMC 1555500. 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. doi:10.1136/gut.21.1.63. PMC 1419572. PMID 6988303.
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