COL11A2 (gene)

From Wikipedia, the free encyclopedia

Collagen, type XI, alpha 2

Identifiers

COL11A2; PARP; DFNA13; DFNB53; HKE5; STL3

External IDs

OMIM: 120290 MGI: 88447 HomoloGene: 22547

Gene ontology
Molecular Function:	• structural molecule activity • extracellular matrix structural constituent • extracellular matrix structural constituent conferring tensile strength
Cellular Component:	• collagen • collagen type XI • cytoplasm
Biological Process:	• skeletal development • phosphate transport • cell adhesion • sensory perception of sound • collagen fibril organization

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_080679 (mRNA)
NP_542410 (protein)

NM_009926 (mRNA)
NP_034056 (protein)

Location

Chr 6: 33.24 - 33.27 Mb

Chr 17: 33.65 - 33.68 Mb

Pubmed search

[1]

[2]

Collagen, type XI, alpha 2, also known as COL11A2, is a human gene.^[1]

This gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. It is located on chromosome 6 very close to but separate from the gene for retinoid X receptor beta. Type XI collagen is a heterotrimer but the third alpha chain is a post-translationally modified alpha 1 type II chain. Proteolytic processing of this type XI chain produces PARP, a proline/arginine-rich protein that is an amino terminal domain. Mutations in this gene are associated with type III Stickler syndrome, otospondylomegaepiphyseal dysplasia (OSMED syndrome), Weissenbacher-Zweymuller syndrome, and autosomal dominant nonsyndromic sensorineural 13 deafness. Three transcript variants encoding different isoforms have been identified for this gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: COL11A2 collagen, type XI, alpha 2.

[edit] Further reading

Kuivaniemi H, Tromp G, Prockop DJ (1997). "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels.". Hum. Mutat. 9 (4): 300–15. doi:10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9. PMID 9101290.
Van Camp G, Willems PJ, Smith RJ (1997). "Nonsyndromic hearing impairment: unparalleled heterogeneity.". Am. J. Hum. Genet. 60 (4): 758–64. PMID 9106521.
Hanson IM, Gorman P, Lui VC, et al. (1990). "The human alpha 2(XI) collagen gene (COL11A2) maps to the centromeric border of the major histocompatibility complex on chromosome 6.". Genomics 5 (4): 925–31. PMID 2591970.
Kimura T, Cheah KS, Chan SD, et al. (1989). "The human alpha 2(XI) collagen (COL11A2) chain. Molecular cloning of cDNA and genomic DNA reveals characteristics of a fibrillar collagen with differences in genomic organization.". J. Biol. Chem. 264 (23): 13910–6. PMID 2760050.
Vuristo MM, Pihlajamaa T, Vandenberg P, et al. (1995). "The human COL11A2 gene structure indicates that the gene has not evolved with the genes for the major fibrillar collagens.". J. Biol. Chem. 270 (39): 22873–81. PMID 7559422.
Keene DR, Oxford JT, Morris NP (1995). "Ultrastructural localization of collagen types II, IX, and XI in the growth plate of human rib and fetal bovine epiphyseal cartilage: type XI collagen is restricted to thin fibrils.". J. Histochem. Cytochem. 43 (10): 967–79. PMID 7560887.
Zhidkova NI, Justice SK, Mayne R (1995). "Alternative mRNA processing occurs in the variable region of the pro-alpha 1(XI) and pro-alpha 2(XI) collagen chains.". J. Biol. Chem. 270 (16): 9486–93. PMID 7721876.
Tsumaki N, Kimura T (1995). "Differential expression of an acidic domain in the amino-terminal propeptide of mouse pro-alpha 2(XI) collagen by complex alternative splicing.". J. Biol. Chem. 270 (5): 2372–8. PMID 7836472.
Vikkula M, Mariman EC, Lui VC, et al. (1995). "Autosomal dominant and recessive osteochondrodysplasias associated with the COL11A2 locus.". Cell 80 (3): 431–7. PMID 7859284.
Zhidkova NI, Brewton RG, Mayne R (1993). "Molecular cloning of PARP (proline/arginine-rich protein) from human cartilage and subsequent demonstration that PARP is a fragment of the NH2-terminal domain of the collagen alpha 2(XI) chain.". FEBS Lett. 326 (1-3): 25–8. PMID 8325374.
Lui VC, Ng LJ, Sat EW, et al. (1996). "Extensive alternative splicing within the amino-propeptide coding domain of alpha2(XI) procollagen mRNAs. Expression of transcripts encoding truncated pro-alpha chains.". J. Biol. Chem. 271 (28): 16945–51. PMID 8663204.
Lui VC, Ng LJ, Sat EW, Cheah KS (1997). "The human alpha 2(XI) collagen gene (COL11A2): completion of coding information, identification of the promoter sequence, and precise localization within the major histocompatibility complex reveal overlap with the KE5 gene.". Genomics 32 (3): 401–12. doi:10.1006/geno.1996.0135. PMID 8838804.
van Steensel MA, Buma P, de Waal Malefijt MC, et al. (1997). "Oto- spondylo-megaepiphyseal dysplasia (OSMED): clinical description of three patients homozygous for a missense mutation in the COL11A2 gene.". Am. J. Med. Genet. 70 (3): 315–23. PMID 9188673.
Sirko-Osadsa DA, Murray MA, Scott JA, et al. (1998). "Stickler syndrome without eye involvement is caused by mutations in COL11A2, the gene encoding the alpha2(XI) chain of type XI collagen.". J. Pediatr. 132 (2): 368–71. PMID 9506662.
Koga H, Sakou T, Taketomi E, et al. (1998). "Genetic mapping of ossification of the posterior longitudinal ligament of the spine.". Am. J. Hum. Genet. 62 (6): 1460–7. PMID 9585596.
Pihlajamaa T, Prockop DJ, Faber J, et al. (1999). "Heterozygous glycine substitution in the COL11A2 gene in the original patient with the Weissenbacher-Zweymüller syndrome demonstrates its identity with heterozygous OSMED (nonocular Stickler syndrome).". Am. J. Med. Genet. 80 (2): 115–20. PMID 9805126.
McGuirt WT, Prasad SD, Griffith AJ, et al. (1999). "Mutations in COL11A2 cause non-syndromic hearing loss (DFNA13).". Nat. Genet. 23 (4): 413–9. doi:10.1038/70516. PMID 10581026.
Melkoniemi M, Brunner HG, Manouvrier S, et al. (2000). "Autosomal recessive disorder otospondylomegaepiphyseal dysplasia is associated with loss-of-function mutations in the COL11A2 gene.". Am. J. Hum. Genet. 66 (2): 368–77. PMID 10677296.