Collagen, type XVI, alpha 1

Collagen, type XVI, alpha 1
Identifiers
Symbols	COL16A1; 447AA
External IDs	OMIM: 120326 MGI: 1095396 HomoloGene: 1397 GeneCards: COL16A1 Gene
Gene Ontology Molecular function • integrin binding • protein binding Cellular component • extracellular region • collagen type XVI • endoplasmic reticulum lumen Biological process • cell adhesion • integrin-mediated signaling pathway • female pregnancy • extracellular matrix disassembly • extracellular matrix organization • collagen catabolic process • cellular response to amino acid stimulus Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1307	107581
Ensembl	ENSG00000084636	ENSMUSG00000040690
UniProt	Q07092	Q8BLX7
RefSeq (mRNA)	NM_001856	NM_028266
RefSeq (protein)	NP_001847	NP_082542
Location (UCSC)	Chr 1: 32.12 – 32.17 Mb	Chr 4: 130.05 – 130.1 Mb
PubMed search	[1]	[2]

Collagen alpha-1(XVI) chain is a protein that in humans is encoded by the COL16A1 gene.

This gene encodes the alpha chain of type XVI collagen, a member of the FACIT collagen family (fibril-associated collagens with interrupted helices). Members of this collagen family are found in association with fibril-forming collagens such as type I and II, and serve to maintain the integrity of the extracellular matrix. High levels of type XVI collagen have been found in fibroblasts and keratinocytes, and in smooth muscle and amnion.

Further reading

• Yamaguchi N, Kimura S, McBride OW, et al. (1993). "Molecular cloning and partial characterization of a novel collagen chain, alpha 1(XVI), consisting of repetitive collagenous domains and cysteine-containing non-collagenous segments.". J. Biochem. 112 (6): 856–63. PMID 1284248. 
• Sires UI, Dublet B, Aubert-Foucher E, et al. (1995). "Degradation of the COL1 domain of type XIV collagen by 92-kDa gelatinase.". J. Biol. Chem. 270 (3): 1062–7. doi:10.1074/jbc.270.3.1062. PMID 7836360. 
• Tillet E, Mann K, Nischt R, et al. (1995). "Recombinant analysis of human alpha 1 (XVI) collagen. Evidence for processing of the N-terminal globular domain.". Eur. J. Biochem. 228 (1): 160–8. doi:10.1111/j.1432-1033.1995.tb20245.x. PMID 7882999. 
• Grässel S, Timpl R, Tan EM, Chu ML (1997). "Biosynthesis and processing of type XVI collagen in human fibroblasts and smooth muscle cells.". Eur. J. Biochem. 242 (3): 576–84. doi:10.1111/j.1432-1033.1996.0576r.x. PMID 9022684. 
• 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. 
• Kassner A, Hansen U, Miosge N, et al. (2004). "Discrete integration of collagen XVI into tissue-specific collagen fibrils or beaded microfibrils.". Matrix Biol. 22 (2): 131–43. doi:10.1016/S0945-053X(03)00008-8. PMID 12782140. 
• Kassner A, Tiedemann K, Notbohm H, et al. (2004). "Molecular structure and interaction of recombinant human type XVI collagen.". J. Mol. Biol. 339 (4): 835–53. doi:10.1016/j.jmb.2004.03.042. PMID 15165854. 
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414. 
• Eble JA, Kassner A, Niland S, et al. (2006). "Collagen XVI harbors an integrin alpha1 beta1 recognition site in its C-terminal domains.". J. Biol. Chem. 281 (35): 25745–56. doi:10.1074/jbc.M509942200. PMID 16754661.