Biology:A1CF

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

APOBEC1 complementation factor is a protein that in humans is encoded by the A1CF gene.

Gene

Alternative splicing occurs at this locus and three full-length transcript variants, encoding three distinct isoforms, have been described. Additional splicing has been observed but the full-length nature of these variants has not been determined.

Function

Mammalian apolipoprotein B mRNA undergoes site-specific C to U deamination, which is mediated by a multi-component enzyme complex containing a minimal core composed of APOBEC1 and a complementation factor encoded by this gene. The gene product has three non-identical RNA recognition motifs and belongs to the hnRNP R family of RNA-binding proteins. It has been proposed that this complementation factor functions as an RNA-binding subunit and docks APOBEC1 to deaminate the upstream cytidine. Studies suggest that the protein may also be involved in other RNA editing or RNA processing events.

Its deletion results in lethality in mice.

Interactions

A1CF has been shown to interact with APOBEC1, CUGBP2, and SYNCRIP.

External links

• Human A1CF genome location and A1CF gene details page in the UCSC Genome Browser.

Further reading

• "Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA". Mol. Cell. Biol. 20 (5): 1846–54. 2000. doi:10.1128/MCB.20.5.1846-1854.2000. PMID 10669759. 
• "Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex". J. Biol. Chem. 275 (26): 19848–56. 2000. doi:10.1074/jbc.M001786200. PMID 10781591. 
• "Induction of cytidine to uridine editing on cytoplasmic apolipoprotein B mRNA by overexpressing APOBEC-1". J. Biol. Chem. 275 (30): 22663–9. 2000. doi:10.1074/jbc.M910406199. PMID 10833526. 
• "Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing". J. Biol. Chem. 276 (13): 10272–83. 2001. doi:10.1074/jbc.M006435200. PMID 11134005. 
• "Creation of genome-wide protein expression libraries using random activation of gene expression". Nat. Biotechnol. 19 (5): 440–5. 2001. doi:10.1038/88107. PMID 11329013. 
• "Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a component of apobec-1 editosome". Biochem. Biophys. Res. Commun. 282 (4): 977–83. 2001. doi:10.1006/bbrc.2001.4679. PMID 11352648. 
• "Mutagenesis of apobec-1 complementation factor reveals distinct domains that modulate RNA binding, protein-protein interaction with apobec-1, and complementation of C to U RNA-editing activity". J. Biol. Chem. 276 (49): 46386–93. 2001. doi:10.1074/jbc.M107654200. PMID 11571303. 
• "Novel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 modulates C to U editing of apolipoprotein B mRNA by interacting with apobec-1 and ACF, the apobec-1 complementation factor". J. Biol. Chem. 276 (50): 47338–51. 2001. doi:10.1074/jbc.M104911200. PMID 11577082. 
• "Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene". Biochim. Biophys. Acta 1522 (1): 22–30. 2001. doi:10.1016/S0167-4781(01)00295-0. PMID 11718896. 
• "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15089–94. 2001. doi:10.1073/pnas.241522398. PMID 11752456. Bibcode: 2001PNAS...9815089X. 
• "Identification of domains in apobec-1 complementation factor required for RNA binding and apolipoprotein-B mRNA editing". RNA 8 (1): 69–82. 2002. doi:10.1017/S1355838202015649. PMID 11871661. 
• "The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay". EMBO J. 22 (15): 3971–82. 2003. doi:10.1093/emboj/cdg369. PMID 12881431. 
• "A novel nuclear localization signal in the auxiliary domain of apobec-1 complementation factor regulates nucleocytoplasmic import and shuttling". J. Biol. Chem. 278 (42): 41198–204. 2003. doi:10.1074/jbc.M302951200. PMID 12896982. 
• "The structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1". Proc. Natl. Acad. Sci. U.S.A. 101 (21): 8114–9. 2004. doi:10.1073/pnas.0400493101. PMID 15148397. Bibcode: 2004PNAS..101.8114X.