A1CF

APOBEC1 complementation factor
PDB rendering based on 2cpd.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2CPD​
Identifiers
Symbols	A1CF ; ACF; ACF64; ACF65; APOBEC1CF; ASP
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 • protein binding Cellular component • nucleoplasm • cytoplasm • endoplasmic reticulum • apolipoprotein B mRNA editing enzyme complex Biological process • mRNA processing • gene expression • 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	NM_001081074
RefSeq (protein)	NP_001185747	NP_001074543
Location (UCSC)	Chr 10: 50.8 – 50.89 Mb	Chr 19: 31.87 – 31.95 Mb
PubMed search

APOBEC1 complementation factor is a protein that in humans is encoded by the A1CF gene.^[1][2][3]

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.^[3]

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.^[4] 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.^[3]

Its deletion results in lethality in mice.^[5]

Interactions

A1CF has been shown to interact with APOBEC1,^[6][7] CUGBP2,^[8] and SYNCRIP.^[9][6]

References

1. Dance GS, Sowden MP, Cartegni L, Cooper E, Krainer AR, Smith HC (April 2002). "Two proteins essential for apolipoprotein B mRNA editing are expressed from a single gene through alternative splicing". J. Biol. Chem. 277 (15): 12703–9. doi:10.1074/jbc.M111337200. PMID 11815617.
2. Chester A, Scott J, Anant S, Navaratnam N (December 2000). "RNA editing: cytidine to uridine conversion in apolipoprotein B mRNA". Biochim. Biophys. Acta 1494 (1-2): 1–13. doi:10.1016/S0167-4781(00)00219-0. PMID 11072063.
3. "Entrez Gene: A1CF APOBEC1 complementation factor".
4. Henderson JO, Blanc V, Davidson NO (November 2001). "Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene". Biochim. Biophys. Acta 1522 (1): 22–30. doi:10.1016/S0167-4781(01)00295-0. PMID 11718896.
5. Blanc V, Henderson JO, Newberry EP, Kennedy S, Luo J, Davidson NO (August 2005). "Targeted deletion of the murine apobec-1 complementation factor (acf) gene results in embryonic lethality". Mol. Cell. Biol. 25 (16): 7260–9. doi:10.1128/MCB.25.16.7260-7269.2005. PMC 1190267. PMID 16055734.
6. Blanc V, Navaratnam N, Henderson JO, Anant S, Kennedy S, Jarmuz A, Scott J, Davidson NO (March 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.
7. Mehta A, Kinter MT, Sherman NE, Driscoll DM (March 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.
8. Anant S, Henderson JO, Mukhopadhyay D, Navaratnam N, Kennedy S, Min J, Davidson NO (December 2001). "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.
9. Lau PP, Chang BH, Chan L (April 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.

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.
• Lellek H, Kirsten R, Diehl I, Apostel F, Buck F, Greeve J (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, Anant S, Kennedy S, Jarmuz A, Scott J, Davidson NO (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, Jackson PD, Perry R, Cain S, Leventhal C, Thornton M, Ramachandran R, Whittington J, Lerner L, Costanzo D, McElligott K, Boozer S, Mays R, Smith E, Veloso N, Klika A, Hess J, Cothren K, Lo K, Offenbacher J, Danzig J, Ducar M (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 (2001). "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, Navaratnam N, Kennedy S, Min J, Davidson NO (2001). "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. doi:10.1016/S0167-4781(01)00295-0. PMID 11718896.
• Xu XR, Huang J, Xu ZG, Qian BZ, Zhu ZD, Yan Q, Cai T, Zhang X, Xiao HS, Qu J, Liu F, Huang QH, Cheng ZH, Li NG, Du JJ, Hu W, Shen KT, Lu G, Fu G, Zhong M, Xu SH, Gu WY, Huang W, Zhao XT, Hu GX, Gu JR, Chen Z, Han ZG (2001). "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.
• 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.
• Chester A, Somasekaram A, Tzimina M, Jarmuz A, Gisbourne J, O'Keefe R, Scott J, Navaratnam N (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.
• 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.
• Xie K, Sowden MP, Dance GS, Torelli AT, Smith HC, Wedekind JE (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.