Collagen, type XXV, alpha 1

Collagen, type XXV, alpha 1
Identifiers
Symbols	COL25A1; CLAC; CLACP
External IDs	OMIM: 610004 MGI: 1924268 HomoloGene: 57111 GeneCards: COL25A1 Gene
Gene Ontology Molecular function • beta-amyloid binding • heparin binding Cellular component • extracellular region • collagen • extracellular space • integral to plasma membrane • membrane • integral to membrane Biological process • phosphate transport Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	84570	77018
Ensembl	ENSG00000188517	ENSMUSG00000058897
UniProt	Q9BXS0	Q99MQ5
RefSeq (mRNA)	NM_032518.2	NM_029838
RefSeq (protein)	NP_115907.2	NP_084114
Location (UCSC)	Chr 4: 109.73 – 110.22 Mb	Chr 3: 129.88 – 130.3 Mb
PubMed search	[1]	[2]

Collagen alpha-1(XXV) chain is a protein that in humans is encoded by the COL25A1 gene.^[1][2]

COL25A1 is a brain-specific membrane-bound collagen. Proteolytic processing releases CLAC, a soluble form of COL25A1 containing the extracellular collagen domains that associates with senile plaques in Alzheimer disease (AD; MIM 104300) brains (Osada et al., 2005).[supplied by OMIM]^[2]

Interactions

Collagen, type XXV, alpha 1 has been shown to interact with Amyloid precursor protein.^[1]

References

1. ^ ^{a b} Hashimoto T, Wakabayashi T, Watanabe A, Kowa H, Hosoda R, Nakamura A, Kanazawa I, Arai T, Takio K, Mann DM, Iwatsubo T (Apr 2002). "CLAC: a novel Alzheimer amyloid plaque component derived from a transmembrane precursor, CLAC-P/collagen type XXV". EMBO J 21 (7): 1524–34. doi:10.1093/emboj/21.7.1524. PMC 125364. PMID 11927537. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125364. 
2. ^ ^{a b} "Entrez Gene: COL25A1 collagen, type XXV, alpha 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84570. 

Further reading

• Kakuyama H, Söderberg L, Horigome K, et al. (2006). "CLAC binds to aggregated Abeta and Abeta fragments, and attenuates fibril elongation.". Biochemistry 44 (47): 15602–9. doi:10.1021/bi051263e. PMID 16300410. 
• Söderberg L, Dahlqvist C, Kakuyama H, et al. (2005). "Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates.". FEBS J. 272 (9): 2231–6. doi:10.1111/j.1742-4658.2005.04647.x. PMID 15853808. 
• Osada Y, Hashimoto T, Nishimura A, et al. (2005). "CLAC binds to amyloid beta peptides through the positively charged amino acid cluster within the collagenous domain 1 and inhibits formation of amyloid fibrils.". J. Biol. Chem. 280 (9): 8596–605. doi:10.1074/jbc.M413340200. PMID 15615705. 
• Söderberg L, Kakuyama H, Möller A, et al. (2005). "Characterization of the Alzheimer's disease-associated CLAC protein and identification of an amyloid beta-peptide-binding site.". J. Biol. Chem. 280 (2): 1007–15. doi:10.1074/jbc.M403628200. PMID 15522881. 
• Kowa H, Sakakura T, Matsuura Y, et al. (2004). "Mostly separate distributions of CLAC- versus Abeta40- or thioflavin S-reactivities in senile plaques reveal two distinct subpopulations of beta-amyloid deposits.". Am. J. Pathol. 165 (1): 273–81. PMID 15215182. 
• Söderberg L, Zhukareva V, Bogdanovic N, et al. (2004). "Molecular identification of AMY, an Alzheimer disease amyloid-associated protein.". J. Neuropathol. Exp. Neurol. 62 (11): 1108–17. PMID 14656069. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.