COL4A2

Collagen, type IV, alpha 2

PDB rendering based on 1li1.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsCOL4A2 ; ICH; POREN2
External IDsOMIM: 120090 MGI: 88455 HomoloGene: 1390 GeneCards: COL4A2 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez128412827
EnsemblENSG00000134871ENSMUSG00000031503
UniProtP08572P08122
RefSeq (mRNA)NM_001846NM_009932
RefSeq (protein)NP_001837NP_034062
Location (UCSC)Chr 13:
110.96 – 111.17 Mb		Chr 8:
11.31 – 11.45 Mb
PubMed search

Collagen alpha-2(IV) chain is a protein that in humans is encoded by the COL4A2 gene.[1][2][3]

This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. The C-terminal portion of the protein, known as canstatin, is an inhibitor of angiogenesis and tumor growth. 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.[3]

References

  1. ↑ Myers JC, Howard PS, Jelen AM, Dion AS, Macarak EJ (Aug 1987). "Duplication of type IV collagen COOH-terminal repeats and species-specific expression of alpha 1(IV) and alpha 2(IV) collagen genes". J Biol Chem 262 (19): 9231–8. PMID 2439508.
  2. ↑ Griffin CA, Emanuel BS, Hansen JR, Cavenee WK, Myers JC (Feb 1987). "Human collagen genes encoding basement membrane alpha 1 (IV) and alpha 2 (IV) chains map to the distal long arm of chromosome 13". Proc Natl Acad Sci U S A 84 (2): 512–6. doi:10.1073/pnas.84.2.512. PMC 304239. PMID 3025878.
  3. ↑ 3.0 3.1 "Entrez Gene: COL4A2 collagen, type IV, alpha 2".

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.
  • 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 : official publication of the Biological Stain Commission 74 (3): 146–59. doi:10.3109/10520299909047967. PMID 10416788.
  • Kalluri R, Sukhatme VP (2000). "Fibrosis and angiogenesis.". Curr. Opin. Nephrol. Hypertens. 9 (4): 413–8. doi:10.1097/00041552-200007000-00013. PMID 10926178.
  • 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.
  • 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.
  • Paralkar VM, Nandedkar AK, Pointer RH et al. (1990). "Interaction of osteogenin, a heparin binding bone morphogenetic protein, with type IV collagen.". J. Biol. Chem. 265 (28): 17281–4. PMID 2211625.
  • 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.
  • Siebold B, Deutzmann R, Kühn K (1988). "The arrangement of intra- and intermolecular disulfide bonds in the carboxyterminal, non-collagenous aggregation and cross-linking domain of basement-membrane type IV collagen.". Eur. J. Biochem. 176 (3): 617–24. doi:10.1111/j.1432-1033.1988.tb14321.x. PMID 2844531.
  • Pöschl E, Pollner R, Kühn K (1988). "The genes for the alpha 1(IV) and alpha 2(IV) chains of human basement membrane collagen type IV are arranged head-to-head and separated by a bidirectional promoter of unique structure.". EMBO J. 7 (9): 2687–95. PMC 457057. PMID 2846280.
  • 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.
  • Soininen R, Huotari M, Hostikka SL et al. (1988). "The structural genes for alpha 1 and alpha 2 chains of human type IV collagen are divergently encoded on opposite DNA strands and have an overlapping promoter region.". J. Biol. Chem. 263 (33): 17217–20. PMID 3182844.
  • Hostikka SL, Tryggvason K (1989). "The complete primary structure of the alpha 2 chain of human type IV collagen and comparison with the alpha 1(IV) chain.". J. Biol. Chem. 263 (36): 19488–93. PMID 3198637.
  • Brazel D, Pollner R, Oberbäumer I, Kühn K (1988). "Human basement membrane collagen (type IV). The amino acid sequence of the alpha 2(IV) chain and its comparison with the alpha 1(IV) chain reveals deletions in the alpha 1(IV) chain.". Eur. J. Biochem. 172 (1): 35–42. doi:10.1111/j.1432-1033.1988.tb13852.x. PMID 3345760.
  • Hostikka SL, Kurkinen M, Tryggvason K (1987). "Nucleotide sequence coding for the human type IV collagen alpha 2 chain cDNA reveals extensive homology with the NC-1 domain of alpha 1 (IV) but not with the collagenous domain or 3'-untranslated region.". FEBS Lett. 216 (2): 281–6. doi:10.1016/0014-5793(87)80706-8. PMID 3582677.
  • Killen PD, Francomano CA, Yamada Y et al. (1988). "Partial structure of the human alpha 2(IV) collagen chain and chromosomal localization of the gene (COL4A2).". Hum. Genet. 77 (4): 318–24. doi:10.1007/BF00291418. PMID 3692475.
  • 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.