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A1CF
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CPD
Identifiers
Aliases	A1CF, ACF, ACF64, ACF65, APOBEC1CF, ASP, APOBEC1 complementation factor
External IDs	OMIM: 618199; MGI: 1917115; HomoloGene: 16363; GeneCards: A1CF; OMA:A1CF - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10q11.23 Start 50,799,409 bp End 50,885,675 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19|19 C1 Start 31,846,164 bp End 31,926,395 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in liver jejunal mucosa mucosa of ileum right lobe of liver buccal mucosa cell duodenum mucosa of colon mucosa of sigmoid colon oocyte pancreatic ductal cell Top expressed in right kidney proximal tubule embryo yolk sac liver duodenum left lobe of liver lumbar subsegment of spinal cord jejunum human kidney More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleic acid binding double-stranded RNA binding protein binding single-stranded RNA binding RNA binding mRNA binding Cellular component cytoplasm apolipoprotein B mRNA editing enzyme complex endoplasmic reticulum nucleus nucleoplasm Biological process mRNA processing protein stabilization cytidine to uridine editing mRNA modification mRNA localization resulting in posttranscriptional regulation of gene expression Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 29974 69865 Ensembl ENSG00000148584 ENSMUSG00000052595 UniProt Q9NQ94 Q5YD48 RefSeq (mRNA) NM_001198818 NM_001198819 NM_001198820 NM_014576 NM_138932 NM_138933 NM_001370130 NM_001370131 NM_001081074 NM_001365078 RefSeq (protein) NP_001185747 NP_001185748 NP_001185749 NP_055391 NP_620310 NP_620311 NP_001357059 NP_001357060 NP_001074543 NP_001352007 Location (UCSC) Chr 10: 50.8 – 50.89 Mb Chr 19: 31.85 – 31.93 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000148584 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000052595 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. ^ "Entrez Gene: A1CF APOBEC1 complementation factor".
8. 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.
9. 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.
10. ^ 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.
11. 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.
12. 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.
13. 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.

External links

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

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. S2CID 25064683.
• 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. Bibcode:2001PNAS...9815089X. 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. Bibcode:2004PNAS..101.8114X. doi:10.1073/pnas.0400493101. PMC 419566. PMID 15148397.

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