ID A1CF_HUMAN Reviewed; 594 AA. AC Q9NQ94; A1L4F2; A8K7G7; B7ZM14; Q5SZQ0; Q9NQ93; Q9NQX8; Q9NQX9; Q9NXC9; AC Q9NZD3; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 24-JAN-2024, entry version 188. DE RecName: Full=APOBEC1 complementation factor; DE AltName: Full=APOBEC1-stimulating protein; GN Name=A1CF; Synonyms=ACF, ASP {ECO:0000312|EMBL:CAB94754.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB94754.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND INTERACTION RP WITH APOBEC1. RC TISSUE=Liver {ECO:0000312|EMBL:CAB94754.1}, and Small intestine RC {ECO:0000312|EMBL:CAB94755.1}; RX PubMed=10781591; DOI=10.1074/jbc.m001786200; RA Lellek H., Kirsten R., Diehl I., Apostel F., Buck F., Greeve J.; RT "Purification and molecular cloning of a novel essential component of the RT apolipoprotein B mRNA editing enzyme-complex."; RL J. Biol. Chem. 275:19848-19856(2000). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF34824.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH APOBEC1, RP AND TISSUE SPECIFICITY. RX PubMed=10669759; DOI=10.1128/mcb.20.5.1846-1854.2000; RA Mehta A., Kinter M.T., Sherman N.E., Driscoll D.M.; RT "Molecular cloning of APOBEC-1 complementation factor, a novel RNA-binding RT protein involved in the editing of apolipoprotein B mRNA."; RL Mol. Cell. Biol. 20:1846-1854(2000). RN [3] {ECO:0000305, ECO:0000312|EMBL:AAF76221.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Liver; RA Sowden M.P., Smith H.C.; RT "Human APOBEC-1 complementation factor related protein."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000305, ECO:0000312|EMBL:BAA91086.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] {ECO:0000312|EMBL:AL512366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] {ECO:0000305, ECO:0000312|EMBL:AAF76221.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP INTERACTION WITH SYNCRIP. RX PubMed=11134005; DOI=10.1074/jbc.m006435200; RA Blanc V., Navaratnam N., Henderson J.O., Anant S., Kennedy S., Jarmuz A., RA Scott J., Davidson N.O.; RT "Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that RT interacts with both apobec-1 and apobec-1 complementation factor to RT modulate C to U editing."; RL J. Biol. Chem. 276:10272-10283(2001). RN [9] RP INTERACTION WITH CELF2. RX PubMed=11577082; DOI=10.1074/jbc.m104911200; RA Anant S., Henderson J.O., Mukhopadhyay D., Navaratnam N., Kennedy S., RA Min J., Davidson N.O.; RT "Novel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 RT modulates C to U editing of apolipoprotein B mRNA by interacting with RT apobec-1 and ACF, the apobec-1 complementation factor."; RL J. Biol. Chem. 276:47338-47351(2001). RN [10] {ECO:0000305} RP GENE STRUCTURE, AND ALTERNATIVE SPLICING. RX PubMed=11718896; DOI=10.1016/s0167-4781(01)00295-0; RA Henderson J.O., Blanc V., Davidson N.O.; RT "Isolation, characterization and developmental regulation of the human RT apobec-1 complementation factor (ACF) gene."; RL Biochim. Biophys. Acta 1522:22-30(2001). RN [11] {ECO:0000305} RP RNA-BINDING DOMAIN, AND MUTAGENESIS OF PHE-59; PHE-100; PHE-139; PHE-183; RP TYR-234 AND PHE-270. RX PubMed=11871661; DOI=10.1017/s1355838202015649; RA Mehta A., Driscoll D.M.; RT "Identification of domains in apobec-1 complementation factor required for RT RNA binding and apolipoprotein-B mRNA editing."; RL RNA 8:69-82(2002). RN [12] {ECO:0000305} RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12881431; DOI=10.1093/emboj/cdg369; RA Chester A., Somasekaram A., Tzimina M., Jarmuz A., Gisbourne J., RA O'Keefe R., Scott J., Navaratnam N.; RT "The apolipoprotein B mRNA editing complex performs a multifunctional cycle RT and suppresses nonsense-mediated decay."; RL EMBO J. 22:3971-3982(2003). RN [13] {ECO:0000305} RP NUCLEAR LOCALIZATION SIGNAL, AND INTERACTION WITH TNPO2. RX PubMed=12896982; DOI=10.1074/jbc.m302951200; RA Blanc V., Kennedy S., Davidson N.O.; RT "A novel nuclear localization signal in the auxiliary domain of apobec-1 RT complementation factor regulates nucleocytoplasmic import and shuttling."; RL J. Biol. Chem. 278:41198-41204(2003). RN [14] RP FUNCTION, INTERACTION WITH RBM47, AND SUBCELLULAR LOCATION. RX PubMed=24916387; DOI=10.15252/embr.201438450; RA Fossat N., Tourle K., Radziewic T., Barratt K., Liebhold D., Studdert J.B., RA Power M., Jones V., Loebel D.A., Tam P.P.; RT "C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RT RBM47."; RL EMBO Rep. 15:903-910(2014). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-499, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] {ECO:0000305, ECO:0000312|EMBL:AAF76221.1} RP STRUCTURE BY NMR OF 223-308. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the RNA recognition motif of human APOBEC-1 RT complementation factor, ACF."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: Essential component of the apolipoprotein B mRNA editing CC enzyme complex which is responsible for the postranscriptional editing CC of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to CC APOB mRNA and is probably responsible for docking the catalytic CC subunit, APOBEC1, to the mRNA to allow it to deaminate its target CC cytosine. The complex also protects the edited APOB mRNA from nonsense- CC mediated decay. {ECO:0000269|PubMed:10669759, CC ECO:0000269|PubMed:10781591, ECO:0000269|PubMed:12881431, CC ECO:0000269|PubMed:24916387}. CC -!- SUBUNIT: Part of the apolipoprotein B mRNA editing complex with APOBEC1 CC (PubMed:10781591, PubMed:10669759). Interacts with TNPO2; TNPO2 may be CC responsible for transport of A1CF into the nucleus (PubMed:12896982). CC Interacts with SYNCRIP (PubMed:11134005). Interacts with CELF2/CUGBP2 CC (PubMed:11577082). Interacts with RBM47 (PubMed:24916387). CC {ECO:0000269|PubMed:10669759, ECO:0000269|PubMed:10781591, CC ECO:0000269|PubMed:11134005, ECO:0000269|PubMed:11577082, CC ECO:0000269|PubMed:12896982, ECO:0000269|PubMed:24916387}. CC -!- INTERACTION: CC Q9NQ94; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-2809489, EBI-11976299; CC Q9NQ94; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2809489, EBI-3867333; CC Q9NQ94; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-2809489, EBI-10694655; CC Q9NQ94; Q16610: ECM1; NbExp=3; IntAct=EBI-2809489, EBI-947964; CC Q9NQ94; Q04637-9: EIF4G1; NbExp=3; IntAct=EBI-2809489, EBI-12012124; CC Q9NQ94; Q14192: FHL2; NbExp=3; IntAct=EBI-2809489, EBI-701903; CC Q9NQ94; Q13643: FHL3; NbExp=3; IntAct=EBI-2809489, EBI-741101; CC Q9NQ94; Q16082: HSPB2; NbExp=3; IntAct=EBI-2809489, EBI-739395; CC Q9NQ94; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-2809489, EBI-9478422; CC Q9NQ94; Q15323: KRT31; NbExp=3; IntAct=EBI-2809489, EBI-948001; CC Q9NQ94; O76011: KRT34; NbExp=3; IntAct=EBI-2809489, EBI-1047093; CC Q9NQ94; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-2809489, EBI-8487781; CC Q9NQ94; O43482: OIP5; NbExp=3; IntAct=EBI-2809489, EBI-536879; CC Q9NQ94; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-2809489, EBI-949255; CC Q9NQ94; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-2809489, EBI-1389308; CC Q9NQ94; Q04864: REL; NbExp=3; IntAct=EBI-2809489, EBI-307352; CC Q9NQ94; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-2809489, EBI-10182375; CC Q9NQ94; Q8NCR6: SPMIP6; NbExp=3; IntAct=EBI-2809489, EBI-10269322; CC Q9NQ94; Q13077: TRAF1; NbExp=6; IntAct=EBI-2809489, EBI-359224; CC Q9NQ94-2; O95810: CAVIN2; NbExp=3; IntAct=EBI-10311892, EBI-742141; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12881431, CC ECO:0000269|PubMed:24916387}. Endoplasmic reticulum {ECO:0000250}. CC Cytoplasm {ECO:0000269|PubMed:12881431}. Note=Predominantly nuclear CC where it localizes to heterochromatin. Also cytoplasmic where it is CC found at the outer surface of the endoplasmic reticulum (By CC similarity). Shuttles between the nucleus and cytoplasm. May be CC transported into the nucleus by the nuclear import protein TNPO2/TRN2 CC or by APOBEC1. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1 {ECO:0000269|PubMed:10781591}; CC IsoId=Q9NQ94-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:10669759, ECO:0000269|PubMed:10781591}; CC IsoId=Q9NQ94-2; Sequence=VSP_051929; CC Name=3; CC IsoId=Q9NQ94-3; Sequence=VSP_051926, VSP_051929; CC Name=4 {ECO:0000305}; CC IsoId=Q9NQ94-4; Sequence=VSP_051927, VSP_051929; CC Name=5 {ECO:0000269|PubMed:11718896}; CC IsoId=Q9NQ94-5; Sequence=VSP_051925; CC Name=6 {ECO:0000269|PubMed:11718896}; CC IsoId=Q9NQ94-6; Sequence=VSP_051928; CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain, CC liver, pancreas, colon and spleen. {ECO:0000269|PubMed:10669759}. CC -!- DOMAIN: The RRM domains are necessary but not sufficient for binding to CC APOB mRNA. Additional residues in the pre-RRM and C-terminal regions CC are required for RNA-binding and for complementing APOBEC1 activity. CC {ECO:0000269|PubMed:11871661}. CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform found in 66-78% of cDNA CC clones. {ECO:0000269|PubMed:11718896}. CC -!- MISCELLANEOUS: [Isoform 4]: Does not exhibit APOBEC1 complementation CC activity. {ECO:0000269|PubMed:11718896, ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Does not exhibit APOBEC1 complementation CC activity. {ECO:0000269|PubMed:11718896}. CC -!- MISCELLANEOUS: [Isoform 6]: Minor isoform found in 2-3% of cDNA clones. CC {ECO:0000269|PubMed:11718896}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91086.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ272078; CAB94754.1; -; mRNA. DR EMBL; AJ272079; CAB94755.1; -; mRNA. DR EMBL; AF209192; AAF34824.1; -; mRNA. DR EMBL; AF271789; AAF76221.1; -; mRNA. DR EMBL; AF271790; AAF76222.1; -; mRNA. DR EMBL; AK000324; BAA91086.1; ALT_FRAME; mRNA. DR EMBL; AK291982; BAF84671.1; -; mRNA. DR EMBL; AL512366; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL589794; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471083; EAW54133.1; -; Genomic_DNA. DR EMBL; CH471083; EAW54134.1; -; Genomic_DNA. DR EMBL; CH471083; EAW54135.1; -; Genomic_DNA. DR EMBL; BC130519; AAI30520.1; -; mRNA. DR EMBL; BC144196; AAI44197.1; -; mRNA. DR CCDS; CCDS7241.1; -. [Q9NQ94-2] DR CCDS; CCDS7242.1; -. [Q9NQ94-1] DR CCDS; CCDS7243.1; -. [Q9NQ94-4] DR RefSeq; NP_001185747.1; NM_001198818.1. [Q9NQ94-2] DR RefSeq; NP_001185748.1; NM_001198819.1. DR RefSeq; NP_001185749.1; NM_001198820.1. [Q9NQ94-4] DR RefSeq; NP_055391.2; NM_014576.3. [Q9NQ94-2] DR RefSeq; NP_620310.1; NM_138932.2. [Q9NQ94-1] DR RefSeq; NP_620311.1; NM_138933.2. [Q9NQ94-4] DR RefSeq; XP_005269775.1; XM_005269718.2. [Q9NQ94-1] DR RefSeq; XP_005269777.1; XM_005269720.3. DR RefSeq; XP_016871649.1; XM_017016160.1. DR PDB; 2CPD; NMR; -; A=223-308. DR PDBsum; 2CPD; -. DR AlphaFoldDB; Q9NQ94; -. DR SMR; Q9NQ94; -. DR BioGRID; 119004; 39. DR ComplexPortal; CPX-1097; C-to-U editosome complex. DR IntAct; Q9NQ94; 24. DR STRING; 9606.ENSP00000378868; -. DR GlyGen; Q9NQ94; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NQ94; -. DR PhosphoSitePlus; Q9NQ94; -. DR BioMuta; A1CF; -. DR DMDM; 74761651; -. DR jPOST; Q9NQ94; -. DR MassIVE; Q9NQ94; -. DR MaxQB; Q9NQ94; -. DR PaxDb; 9606-ENSP00000378868; -. DR PeptideAtlas; Q9NQ94; -. DR ProteomicsDB; 82112; -. [Q9NQ94-1] DR ProteomicsDB; 82113; -. [Q9NQ94-2] DR ProteomicsDB; 82114; -. [Q9NQ94-3] DR ProteomicsDB; 82115; -. [Q9NQ94-4] DR ProteomicsDB; 82116; -. [Q9NQ94-5] DR ProteomicsDB; 82117; -. [Q9NQ94-6] DR Antibodypedia; 27897; 209 antibodies from 21 providers. DR DNASU; 29974; -. DR Ensembl; ENST00000373993.6; ENSP00000363105.1; ENSG00000148584.16. [Q9NQ94-1] DR Ensembl; ENST00000373995.7; ENSP00000363107.3; ENSG00000148584.16. [Q9NQ94-4] DR Ensembl; ENST00000373997.8; ENSP00000363109.3; ENSG00000148584.16. [Q9NQ94-2] DR Ensembl; ENST00000374001.6; ENSP00000363113.1; ENSG00000148584.16. [Q9NQ94-2] DR Ensembl; ENST00000395495.6; ENSP00000378873.2; ENSG00000148584.16. [Q9NQ94-4] DR Ensembl; ENST00000414883.2; ENSP00000397953.2; ENSG00000148584.16. [Q9NQ94-2] DR GeneID; 29974; -. DR KEGG; hsa:29974; -. DR MANE-Select; ENST00000373997.8; ENSP00000363109.3; NM_014576.4; NP_055391.2. [Q9NQ94-2] DR UCSC; uc001jjh.4; human. [Q9NQ94-1] DR AGR; HGNC:24086; -. DR CTD; 29974; -. DR DisGeNET; 29974; -. DR GeneCards; A1CF; -. DR HGNC; HGNC:24086; A1CF. DR HPA; ENSG00000148584; Tissue enriched (liver). DR MIM; 618199; gene. DR neXtProt; NX_Q9NQ94; -. DR OpenTargets; ENSG00000148584; -. DR PharmGKB; PA162375098; -. DR VEuPathDB; HostDB:ENSG00000148584; -. DR eggNOG; KOG0117; Eukaryota. DR GeneTree; ENSGT00940000158678; -. DR HOGENOM; CLU_022960_5_1_1; -. DR InParanoid; Q9NQ94; -. DR OrthoDB; 3184171at2759; -. DR PhylomeDB; Q9NQ94; -. DR TreeFam; TF314932; -. DR PathwayCommons; Q9NQ94; -. DR Reactome; R-HSA-72200; mRNA Editing: C to U Conversion. DR Reactome; R-HSA-75094; Formation of the Editosome. DR SignaLink; Q9NQ94; -. DR BioGRID-ORCS; 29974; 28 hits in 1151 CRISPR screens. DR ChiTaRS; A1CF; human. DR EvolutionaryTrace; Q9NQ94; -. DR GeneWiki; ACF_(gene); -. DR GenomeRNAi; 29974; -. DR Pharos; Q9NQ94; Tbio. DR PRO; PR:Q9NQ94; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9NQ94; Protein. DR Bgee; ENSG00000148584; Expressed in liver and 64 other cell types or tissues. DR ExpressionAtlas; Q9NQ94; baseline and differential. DR GO; GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0045293; C:mRNA editing complex; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0140767; F:enzyme-substrate adaptor activity; IDA:UniProt. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; TAS:ProtInc. DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0016554; P:cytidine to uridine editing; IDA:UniProtKB. DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl. DR GO; GO:0010609; P:mRNA localization resulting in post-transcriptional regulation of gene expression; IEA:Ensembl. DR GO; GO:0016556; P:mRNA modification; IDA:ComplexPortal. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:ComplexPortal. DR GO; GO:1901537; P:positive regulation of DNA demethylation; NAS:ComplexPortal. DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB. DR CDD; cd19900; DSRM_A1CF; 1. DR CDD; cd12486; RRM1_ACF; 1. DR CDD; cd12490; RRM2_ACF; 1. DR CDD; cd12498; RRM3_ACF; 1. DR Gene3D; 3.30.160.20; -; 1. DR Gene3D; 3.30.70.330; -; 3. DR InterPro; IPR044461; A1CF_DSRM. DR InterPro; IPR034538; ACF_RRM1. DR InterPro; IPR006535; HnRNP_R/Q_splicing_fac. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR NCBIfam; TIGR01648; hnRNP-R-Q; 1. DR PANTHER; PTHR21245:SF8; APOBEC1 COMPLEMENTATION FACTOR; 1. DR PANTHER; PTHR21245; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; 1. DR Pfam; PF14709; DND1_DSRM; 1. DR Pfam; PF00076; RRM_1; 3. DR SMART; SM00360; RRM; 3. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 3. DR PROSITE; PS50102; RRM; 3. DR Genevisible; Q9NQ94; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Endoplasmic reticulum; KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW RNA-binding. FT CHAIN 1..594 FT /note="APOBEC1 complementation factor" FT /id="PRO_0000081482" FT DOMAIN 56..134 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 136..218 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 231..303 FT /note="RRM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 360..409 FT /note="Required for nuclear localization" FT /evidence="ECO:0000269|PubMed:12896982" FT MOD_RES 499 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..84 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:11718896" FT /id="VSP_051925" FT VAR_SEQ 1..33 FT /note="MESNHKSGDGLSGTQKEAALRALVQRTGYSLVQ -> MLCSPSFCKLCWKRK FT K (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_051926" FT VAR_SEQ 1..33 FT /note="MESNHKSGDGLSGTQKEAALRALVQRTGYSLVQ -> MEAVCLGTCPEPEAS FT MSTAIPGLKKGNNALQSIILQTLLEK (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_051927" FT VAR_SEQ 202..256 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:11718896" FT /id="VSP_051928" FT VAR_SEQ 381..388 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:10669759, FT ECO:0000303|PubMed:10781591, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_051929" FT VARIANT 555 FT /note="V -> M (in dbSNP:rs9073)" FT /id="VAR_052201" FT VARIANT 558 FT /note="A -> S (in dbSNP:rs11817448)" FT /id="VAR_059821" FT MUTAGEN 59 FT /note="F->A: Greatly reduced RNA binding." FT /evidence="ECO:0000269|PubMed:11871661" FT MUTAGEN 100 FT /note="F->A: Greatly reduced RNA binding." FT /evidence="ECO:0000269|PubMed:11871661" FT MUTAGEN 139 FT /note="F->A: Greatly reduced RNA binding." FT /evidence="ECO:0000269|PubMed:11871661" FT MUTAGEN 183 FT /note="F->A: Greatly reduced RNA binding." FT /evidence="ECO:0000269|PubMed:11871661" FT MUTAGEN 234 FT /note="Y->A: Slightly reduced RNA binding." FT /evidence="ECO:0000269|PubMed:11871661" FT MUTAGEN 270 FT /note="F->A: Slightly reduced RNA binding." FT /evidence="ECO:0000269|PubMed:11871661" FT CONFLICT 191 FT /note="A -> T (in Ref. 2; AAF34824)" FT /evidence="ECO:0000305" FT CONFLICT 277 FT /note="E -> K (in Ref. 2 and 3)" FT /evidence="ECO:0000305" FT STRAND 232..237 FT /evidence="ECO:0007829|PDB:2CPD" FT HELIX 244..252 FT /evidence="ECO:0007829|PDB:2CPD" FT STRAND 259..264 FT /evidence="ECO:0007829|PDB:2CPD" FT STRAND 266..275 FT /evidence="ECO:0007829|PDB:2CPD" FT HELIX 276..286 FT /evidence="ECO:0007829|PDB:2CPD" FT STRAND 287..291 FT /evidence="ECO:0007829|PDB:2CPD" FT STRAND 294..299 FT /evidence="ECO:0007829|PDB:2CPD" SQ SEQUENCE 594 AA; 65202 MW; AA5EF76BD8815807 CRC64; MESNHKSGDG LSGTQKEAAL RALVQRTGYS LVQENGQRKY GGPPPGWDAA PPERGCEIFI GKLPRDLFED ELIPLCEKIG KIYEMRMMMD FNGNNRGYAF VTFSNKVEAK NAIKQLNNYE IRNGRLLGVC ASVDNCRLFV GGIPKTKKRE EILSEMKKVT EGVVDVIVYP SAADKTKNRG FAFVEYESHR AAAMARRKLL PGRIQLWGHG IAVDWAEPEV EVDEDTMSSV KILYVRNLML STSEEMIEKE FNNIKPGAVE RVKKIRDYAF VHFSNREDAV EAMKALNGKV LDGSPIEVTL AKPVDKDSYV RYTRGTGGRG TMLQGEYTYS LGQVYDPTTT YLGAPVFYAP QTYAAIPSLH FPATKGHLSN RAIIRAPSVR EIYMNVPVGA AGVRGLGGRG YLAYTGLGRG YQVKGDKRED KLYDILPGME LTPMNPVTLK PQGIKLAPQI LEEICQKNNW GQPVYQLHSA IGQDQRQLFL YKITIPALAS QNPAIHPFTP PKLSAFVDEA KTYAAEYTLQ TLGIPTDGGD GTMATAAAAA TAFPGYAVPN ATAPVSAAQL KQAVTLGQDL AAYTTYEVYP TFAVTARGDG YGTF //