A1CF_HUMAN
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 03-AUG-2022, entry version 180.
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
RC Small intestine {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] {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 [10] {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 [11] {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 [12] {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 [13]
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 [14] {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 -!- SUBUNIT: Part of the apolipoprotein B mRNA editing complex with
CC APOBEC1. Interacts with TNPO2; TNPO2 may be responsible for transport
CC of A1CF into the nucleus. Interacts with SYNCRIP. Interacts with
CC CELF2/CUGBP2 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NQ94; Q5BKX5-3: C19orf54; 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: SMRP1; 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 Endoplasmic reticulum {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:12881431}. Note=Predominantly nuclear where it
CC localizes to heterochromatin. Also cytoplasmic where it is found at the
CC outer surface of the endoplasmic reticulum (By similarity). Shuttles
CC between the nucleus and cytoplasm. May be transported into the nucleus
CC by the nuclear import protein TNPO2/TRN2 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};
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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; 35.
DR ComplexPortal; CPX-1097; C-to-U editosome complex.
DR IntAct; Q9NQ94; 24.
DR STRING; 9606.ENSP00000378868; -.
DR iPTMnet; Q9NQ94; -.
DR PhosphoSitePlus; Q9NQ94; -.
DR BioMuta; A1CF; -.
DR DMDM; 74761651; -.
DR jPOST; Q9NQ94; -.
DR MassIVE; Q9NQ94; -.
DR MaxQB; Q9NQ94; -.
DR PaxDb; Q9NQ94; -.
DR PeptideAtlas; Q9NQ94; -.
DR PRIDE; 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; 187 antibodies from 21 providers.
DR DNASU; 29974; -.
DR Ensembl; ENST00000282641.6; ENSP00000282641.3; ENSG00000148584.15. [Q9NQ94-2]
DR Ensembl; ENST00000373993.5; ENSP00000363105.1; ENSG00000148584.15. [Q9NQ94-1]
DR Ensembl; ENST00000373995.7; ENSP00000363107.3; ENSG00000148584.15. [Q9NQ94-4]
DR Ensembl; ENST00000373997.8; ENSP00000363109.3; ENSG00000148584.15. [Q9NQ94-2]
DR Ensembl; ENST00000374001.6; ENSP00000363113.1; ENSG00000148584.15. [Q9NQ94-2]
DR Ensembl; ENST00000395495.5; ENSP00000378873.2; ENSG00000148584.15. [Q9NQ94-4]
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 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; 1384330at2759; -.
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; 21 hits in 1072 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 tissues.
DR ExpressionAtlas; Q9NQ94; baseline and differential.
DR Genevisible; Q9NQ94; HS.
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; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0016554; P:cytidine to uridine editing; IEA:Ensembl.
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; IC:ComplexPortal.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR CDD; cd19900; DSRM_A1CF; 1.
DR CDD; cd12486; RRM1_ACF; 1.
DR CDD; cd12498; RRM3_ACF; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR033111; A1CF.
DR InterPro; IPR044461; A1CF_DSRM.
DR InterPro; IPR034538; ACF_RRM1.
DR InterPro; IPR034539; ACF_RRM3.
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 PANTHER; PTHR21245:SF8; PTHR21245:SF8; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR PROSITE; PS50102; RRM; 3.
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
