COL25A1
| Collagen type XXV, alpha 1 | ||
|---|---|---|
| other names |
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| Properties of human protein | ||
| Mass / length primary structure | 654 amino acids , 64,771 Da | |
| Isoforms | 3 | |
| Identifier | ||
| Gene names | COL25A1; CFEOM5; CLAC-P; AMY; CLACP; CLAC | |
| External IDs | ||
| Occurrence | ||
| Parent taxon | Vertebrata | |
| Orthologue | ||
| human | House mouse | |
| Entrez | 84570 | 77018 |
| Ensemble | ENSG00000188517 | ENSMUSG00000058897 |
| UniProt | Q9BXS0 | Q99MQ5 |
| Refseq (mRNA) | NM_001256074 | NM_001244952 |
| Refseq (protein) | NP_115907.2 | NP_084114.2 |
| Gene locus | Chr 4: 108.81 - 109.3 Mb | Chr 3: 130.13 - 130.6 Mb |
| PubMed search | 84570 |
77018
|
Collagen type XXV, alpha 1 is a collagen with transmembrane domains that from gene COL25A1 is encoded. It forms homotrimers , which in turn form collagen fibrils of type XXV.
properties
The proteolysis of collagen XXV produces a protein called CLAC ( collagenous Alzheimer's amyloid plaque component ) that can bind to β-amyloid peptides in senile plaques . Furthermore, CLAC prefers inhibition rather than assisting elongation of amyloid fibrils. It also joins amyloid fibrils with protease- resistant aggregates and can bind heparin .
Mutations in the COL25A1 gene can lead to congenital fibrosis of the extraocular muscles (type 5) and congenital ptosis .
Web links
Individual evidence
- ↑ Hiroyoshi Kakuyama, Linda Söderberg, Kazuhiko Horigome, Bengt Winblad, Camilla Dahlqvist, Jan Näslund, Lars O. Tjernberg: CLAC binds to aggregated Abeta and Abeta fragments, and attenuates fibril elongation . In: Biochemistry . 44, No. 47, November 29, 2005, pp. 15602-15609. doi : 10.1021 / bi051263e . PMID 16300410 .