Collagen, type IV, alpha 4

Collagen alpha-4(IV) chain is a protein that in humans is encoded by the COL4A4 gene.[5][6]

COL4A4
Identifiers
Aliases	COL4A4, CA44, collagen type IV alpha 4, collagen type IV alpha 4 chain, BFH, ATS2
External IDs	OMIM: 120131 MGI: 104687 HomoloGene: 20071 GeneCards: COL4A4
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q36.3 Start 227,002,714 bp[1] End 227,164,453 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 C5 Start 82,448,423 bp[2] End 82,586,849 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • extracellular matrix structural constituent • extracellular matrix structural constituent conferring tensile strength Cellular component • extracellular region • basement membrane • collagen • collagen type IV trimer • endoplasmic reticulum lumen • basal lamina • extracellular • extracellular matrix • collagen-containing extracellular matrix Biological process • extracellular matrix organization • glomerular basement membrane development • angiogenesis • endothelial cell morphogenesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	1286	12829
Ensembl	ENSG00000081052	ENSMUSG00000067158
UniProt	P53420	Q9QZR9
RefSeq (mRNA)	NM_000092	NM_007735
RefSeq (protein)	NP_000083	NP_031761
Location (UCSC)	Chr 2: 227 – 227.16 Mb	Chr 1: 82.45 – 82.59 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. This particular collagen IV subunit, however, is only found in a subset of basement membranes. 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. Mutations in this gene are associated with type II autosomal recessive Alport syndrome (hereditary glomerulonephropathy) and with familial benign hematuria (thin basement membrane disease). Two transcripts, differing only in their transcription start sites, have been identified for this gene and, as is common for collagen genes, multiple polyadenylation sites are found in the 3' UTR.[6]

Disease Database

LOVD Alport gene variant databases (COL4A4, COL4A3, COL4A5)

References

1. GRCh38: Ensembl release 89: ENSG00000081052 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000067158 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Mariyama M, Zheng K, Yang-Feng TL, Reeders ST (Aug 1992). "Colocalization of the genes for the alpha 3(IV) and alpha 4(IV) chains of type IV collagen to chromosome 2 bands q35-q37". Genomics. 13 (3): 809–13. doi:10.1016/0888-7543(92)90157-N. PMID 1639407.
6. "Entrez Gene: COL4A4 collagen, type IV, alpha 4".

Further reading

• Hinek A (1995). "Nature and the multiple functions of the 67-kD elastin-/laminin binding protein". Cell Adhes. Commun. 2 (3): 185–93. doi:10.3109/15419069409004436. PMID 7827955.
• Hudson BG, Reeders ST, Tryggvason K (1994). "Type IV collagen: structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis". J. Biol. Chem. 268 (35): 26033–6. PMID 8253711.
• 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.
• 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.
• 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.
• Pescucci C, Longo I, Bruttini M, et al. (2003). "Type-IV collagen related diseases". J. Nephrol. 16 (2): 314–6. PMID 12768082.
• Torra R, Tazón-Vega B, Ars E, Ballarín J (2005). "Collagen type IV (alpha3-alpha4) nephropathy: from isolated haematuria to renal failure". Nephrol. Dial. Transplant. 19 (10): 2429–32. doi:10.1093/ndt/gfh435. PMID 15280517.
• Rana K, Wang YY, Buzza M, et al. (2005). "The genetics of thin basement membrane nephropathy". Semin. Nephrol. 25 (3): 163–70. doi:10.1016/j.semnephrol.2005.01.008. PMID 15880327.
• Maziers N, Dahan K, Pirson Y (2006). "[From Alport syndrome to benign familial hematuria: clinical and genetic aspect]". Nephrol. Ther. 1 (2): 90–100. doi:10.1016/j.nephro.2005.03.005. PMID 16895672.
• Kamagata Y, Mattei MG, Ninomiya Y (1992). "Isolation and sequencing of cDNAs and genomic DNAs encoding the alpha 4 chain of basement membrane collagen type IV and assignment of the gene to the distal long arm of human chromosome 2". J. Biol. Chem. 267 (33): 23753–8. PMID 1429714.
• 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.
• Sanes JR, Engvall E, Butkowski R, Hunter DD (1990). "Molecular heterogeneity of basal laminae: isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere". J. Cell Biol. 111 (4): 1685–99. doi:10.1083/jcb.111.4.1685. PMC 2116223. PMID 2211832.
• Gunwar S, Saus J, Noelken ME, Hudson BG (1990). "Glomerular basement membrane. Identification of a fourth chain, alpha 4, of type IV collagen". J. Biol. Chem. 265 (10): 5466–9. PMID 2318822.
• 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.
• Murata K, Motayama T, Kotake C (1986). "Collagen types in various layers of the human aorta and their changes with the atherosclerotic process". Atherosclerosis. 60 (3): 251–62. doi:10.1016/0021-9150(86)90172-3. PMID 3089234.
• 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.
• 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.