ACF (gene)

APOBEC1 complementation factor
PDB rendering based on 2cpd.
Available structures PDB 2cpd
Identifiers
Symbols	A1CF; ACF; ACF64; ACF65; APOBEC1CF; ASP; MGC163391
External IDs	MGI: 1917115 HomoloGene: 16363 GeneCards: A1CF Gene
Gene Ontology Molecular function • nucleotide binding • RNA binding • double-stranded RNA binding • single-stranded RNA binding • mRNA binding • cytosine deaminase activity • protein binding Cellular component • intracellular • nucleus • nucleoplasm • nuclear heterochromatin • cytoplasm • endoplasmic reticulum • apolipoprotein B mRNA editing enzyme complex Biological process • mRNA processing • cytidine to uridine editing • mRNA modification • protein stabilization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	29974	69865
Ensembl	ENSG00000148584	ENSMUSG00000052595
UniProt	Q9NQ94	Q5YD48
RefSeq (mRNA)	NM_001198818.1	NM_001081074.1
RefSeq (protein)	NP_001185747.1	NP_001074543.1
Location (UCSC)	Chr 10: 52.57 – 52.65 Mb	Chr 19: 31.94 – 32.02 Mb
PubMed search	[1]	[2]

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

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 APOBEC-1 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 APOBEC-1 to deaminate the upstream cytidine. Studies suggest that the protein may also be involved in other RNA editing or RNA processing events. 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.

Interactions

ACF (gene) has been shown to interact with CUGBP2, SYNCRIP and APOBEC1.

Further reading

• Mehta A, Kinter MT, Sherman NE, Driscoll DM (2000). "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. doi:10.1128/MCB.20.5.1846-1854.2000. PMC 85365. PMID 10669759. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85365. 
• Lellek H, Kirsten R, Diehl I, et al. (2000). "Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex.". J. Biol. Chem. 275 (26): 19848–56. doi:10.1074/jbc.M001786200. PMID 10781591. 
• Yang Y, Sowden MP, Smith HC (2000). "Induction of cytidine to uridine editing on cytoplasmic apolipoprotein B mRNA by overexpressing APOBEC-1.". J. Biol. Chem. 275 (30): 22663–9. doi:10.1074/jbc.M910406199. PMID 10833526. 
• Blanc V, Navaratnam N, Henderson JO, et al. (2001). "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. doi:10.1074/jbc.M006435200. PMID 11134005. 
• Harrington JJ, Sherf B, Rundlett S, et al. (2001). "Creation of genome-wide protein expression libraries using random activation of gene expression.". Nat. Biotechnol. 19 (5): 440–5. doi:10.1038/88107. PMID 11329013. 
• Lau PP, Chang BH, Chan L (2001). "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. doi:10.1006/bbrc.2001.4679. PMID 11352648. 
• Blanc V, Henderson JO, Kennedy S, Davidson NO (2002). "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. doi:10.1074/jbc.M107654200. PMID 11571303. 
• Anant S, Henderson JO, Mukhopadhyay D, et al. (2002). "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. doi:10.1074/jbc.M104911200. PMID 11577082. 
• Henderson JO, Blanc V, Davidson NO (2001). "Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene.". Biochim. Biophys. Acta 1522 (1): 22–30. PMID 11718896. 
• Xu XR, Huang J, Xu ZG, et al. (2002). "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. doi:10.1073/pnas.241522398. PMC 64988. PMID 11752456. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=64988. 
• Mehta A, Driscoll DM (2002). "Identification of domains in apobec-1 complementation factor required for RNA binding and apolipoprotein-B mRNA editing.". RNA 8 (1): 69–82. doi:10.1017/S1355838202015649. PMC 1370230. PMID 11871661. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1370230. 
• 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. 
• Chester A, Somasekaram A, Tzimina M, et al. (2003). "The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay.". EMBO J. 22 (15): 3971–82. doi:10.1093/emboj/cdg369. PMC 169042. PMID 12881431. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=169042. 
• Blanc V, Kennedy S, Davidson NO (2003). "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. doi:10.1074/jbc.M302951200. PMID 12896982. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Xie K, Sowden MP, Dance GS, et al. (2004). "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. doi:10.1073/pnas.0400493101. PMC 419566. PMID 15148397. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=419566. 
• Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10.". Nature 429 (6990): 375–81. doi:10.1038/nature02462. PMID 15164054.