ACF (gene)

From Wikipedia, the free encyclopedia

Apobec-1 complementation factor

PDB rendering based on 2cpd.

Available structures: 2cpd

Identifiers

Symbol(s)

ACF; ASP; ACF64; ACF65; MGC163391; RP11-564C4.2

External IDs

MGI: 1917115 HomoloGene: 16363

Gene ontology
Molecular Function:	• nucleotide binding • nucleic acid binding • double-stranded RNA binding • single-stranded RNA binding • protein binding
Cellular Component:	• nucleus • cytoplasm • apolipoprotein B mRNA editing enzyme complex
Biological Process:	• mRNA editing • mRNA processing • cytidine to uridine editing • protein stabilization

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_014576 (mRNA)
NP_055391 (protein)

XM_001000199 (mRNA)
XP_001000199 (protein)

Location

Chr 10: 52.24 - 52.32 Mb

Chr 19: 31.93 - 32.01 Mb

Pubmed search

[1]

[2]

Apobec-1 complementation factor, also known as ACF, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: ACF apobec-1 complementation factor.

[edit] Further reading

Chester A, Scott J, Anant S, Navaratnam N (2000). "RNA editing: cytidine to uridine conversion in apolipoprotein B mRNA.". Biochim. Biophys. Acta 1494 (1-2): 1-13. PMID 11072063.
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. PMID 10669759.
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. PMID 11752456.
Dance GS, Sowden MP, Cartegni L, et al. (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.
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. PMID 11871661.
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. PMID 12477932.
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. 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.
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. PMID 15148397.
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.