ACF (gene)

APOBEC1 complementation factor

PDB rendering based on 2cpd.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsA1CF ; ACF; ACF64; ACF65; APOBEC1CF; ASP
External IDsMGI: 1917115 HomoloGene: 16363 GeneCards: A1CF Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez2997469865
EnsemblENSG00000148584ENSMUSG00000052595
UniProtQ9NQ94Q5YD48
RefSeq (mRNA)NM_001198818NM_001081074
RefSeq (protein)NP_001185747NP_001074543
Location (UCSC)Chr 10:
52.56 – 52.65 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

ACF 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. 3.0 3.1 3.2 "Entrez Gene: ACF apobec-1 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. 6.0 6.1 Blanc V, Navaratnam N, Henderson JO, Anant S, Kennedy S, Jarmuz A et al. (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 et al. (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