COL9A2

from Wikipedia, the free encyclopedia
Type IX collagen, alpha 2
other names
  • Alpha-2 type IX collagen
  • Collagen Alpha-2 (IX) chain
  • Collagen alpha-2 chain type IX

Existing structural data : PDB  5CTD , PDB  5CTI

Properties of human protein
Mass / length primary structure 689 amino acids , 65,131 Da
Identifier
Gene names COL9A2; DJ39G22.4, STL5, EDM2, MED
External IDs
Occurrence
Parent taxon Euteleostomi
Orthologue
human House mouse
Entrez 1298 12840
Ensemble ENSG00000049089 ENSMUSG00000028626
UniProt Q14055 Q07643
Refseq (mRNA) NM_001852 NM_007741
Refseq (protein) NP_001843.1
Gene locus Chr 1: 40.3 - 40.32 Mb Chr 4: 121.04 - 121.06 Mb
PubMed search 1298 12840

Collagen type IX, alpha 2 is a fibrillenassoziiertes collagen that the gene COL9A2 is encoded. Together with the related collagen type IX, alpha 1 and collagen type IX, alpha 3, it forms heterotrimers , which in turn form collagen fibrils of type IX.

properties

Ribbon model of the NH2 domain of collagen type IX, alpha 2 according to PDB 5CVA

Collagen type IX, alpha 2 is part of the hyaline cartilage and the vitreous body . What is special about this chain is that it contains glycosaminoglycans as a side chain. Because the glycosaminoglycans bind covalently to the protein in the form of proteoglycans , they give the fiber-forming substances a high degree of elasticity. The elasticity is due to the fact that glycosaminoglycans can absorb water.

Web links

Individual evidence

  1. ↑ Z. Zhang, J, Zhang, L. Ding, X. Teng: Meta-analysis of the association between COL9A2 genetic polymorphisms and lumbar disc disease susceptibility . In: Spine (Phila Pa 1976) . 39, No. 20, September 15, 2014, pp. 1699–1706. doi : 10.1097 / BRS.0000000000000497 . PMID 24983932 .
  2. ^ PN Bishop, M. Takanosu, M. le Goff, R. Mayne: The role of the posterior ciliary body in the biosynthesis of vitreous humor . In: Eye . 16, 2002, pp. 454-460. doi : 10.1038 / sj.eye.6700199 .
  3. ↑ Eva-Lena Stattin, Fredrik Wiklund, Karin Lindblom, Patrik Önnerfjord, Björn-Anders Jonsson, Yelverton Tegner, Takako Sasaki, André Struglics, Stefan Lohmander, Niklas Dahl, Dick Heinegård, Anders Aspberg: A Missense Mutation in the Aggrecan C-type Lectin Domain Disrupts Extracellular Matrix Interactions and Causes Dominant Familial Osteochondritis Dissecans . In: Am J Hum Genet . 86, No. 2, February 12, 2010, pp. 126-137. doi : 10.1016 / j.ajhg.2009.12.018 . PMC 2820178 (free full text).