A1CF_MOUSE
ID A1CF_MOUSE Reviewed; 595 AA.
AC Q5YD48; E9QJS8; Q5FW55; Q5YD47;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=APOBEC1 complementation factor;
DE AltName: Full=APOBEC1-stimulating protein;
GN Name=A1cf; Synonyms=Acf, Asp {ECO:0000250|UniProtKB:Q9NQ94};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAT74916.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAT74916.1};
RX PubMed=15451168; DOI=10.1016/j.bbaexp.2004.07.006;
RA Duer S., Krause K., Pluntke N., Greeve J.;
RT "Gene structure and expression of the mouse APOBEC-1 complementation
RT factor: multiple transcriptional initiation sites and a spliced variant
RT with a premature stop translation codon.";
RL Biochim. Biophys. Acta 1680:11-23(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH89622.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Liver {ECO:0000312|EMBL:AAH89622.1};
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 [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=16055734; DOI=10.1128/mcb.25.16.7260-7269.2005;
RA Blanc V., Henderson J.O., Newberry E.P., Kennedy S., Luo J., Davidson N.O.;
RT "Targeted deletion of the murine apobec-1 complementation factor (acf) gene
RT results in embryonic lethality.";
RL Mol. Cell. Biol. 25:7260-7269(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 seems to protect the edited APOB mRNA from
CC nonsense-mediated decay (By similarity).
CC {ECO:0000250|UniProtKB:Q9NQ94}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly nuclear
CC where it localizes to heterochromatin. Also cytoplasmic where it is
CC found at the outer surface of the endoplasmic reticulum. Shuttles
CC between the nucleus and cytoplasm. May be transported into the nucleus
CC by the nuclear import protein TNPO2/TRN2 or by APOBEC1 (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:15451168};
CC IsoId=Q5YD48-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15451168};
CC IsoId=Q5YD48-2; Sequence=VSP_051930;
CC Name=3 {ECO:0000269|PubMed:15451168};
CC IsoId=Q5YD48-3; Sequence=VSP_051931, VSP_051932;
CC -!- TISSUE SPECIFICITY: Expressed primarily in liver, small intestine and
CC kidney. {ECO:0000269|PubMed:15451168}.
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 (By
CC similarity). {ECO:0000250|UniProtKB:Q9NQ94}.
CC -!- DISRUPTION PHENOTYPE: Mice display embryonic lethality at E3.5 due to
CC failure of embryos to implant. {ECO:0000269|PubMed:16055734}.
CC -!- MISCELLANEOUS: [Isoform 3]: Minor isoform detected in less than 10% of
CC cDNA clones. {ECO:0000269|PubMed:15451168}.
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DR EMBL; AY566862; AAT74916.1; -; mRNA.
DR EMBL; AY566863; AAT74917.1; -; mRNA.
DR EMBL; AY566864; AAT74918.1; -; mRNA.
DR EMBL; AC117816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089622; AAH89622.1; -; mRNA.
DR CCDS; CCDS37959.1; -. [Q5YD48-1]
DR CCDS; CCDS89374.1; -. [Q5YD48-2]
DR RefSeq; NP_001074543.1; NM_001081074.1. [Q5YD48-1]
DR RefSeq; XP_006527394.1; XM_006527331.1.
DR AlphaFoldDB; Q5YD48; -.
DR SMR; Q5YD48; -.
DR ComplexPortal; CPX-1098; C-to-U editosome complex.
DR STRING; 10090.ENSMUSP00000075235; -.
DR iPTMnet; Q5YD48; -.
DR PhosphoSitePlus; Q5YD48; -.
DR SwissPalm; Q5YD48; -.
DR jPOST; Q5YD48; -.
DR MaxQB; Q5YD48; -.
DR PaxDb; Q5YD48; -.
DR PeptideAtlas; Q5YD48; -.
DR PRIDE; Q5YD48; -.
DR ProteomicsDB; 296460; -. [Q5YD48-1]
DR ProteomicsDB; 296461; -. [Q5YD48-2]
DR ProteomicsDB; 296462; -. [Q5YD48-3]
DR Antibodypedia; 27897; 187 antibodies from 21 providers.
DR Ensembl; ENSMUST00000075838; ENSMUSP00000075235; ENSMUSG00000052595. [Q5YD48-1]
DR Ensembl; ENSMUST00000224304; ENSMUSP00000153542; ENSMUSG00000052595. [Q5YD48-2]
DR Ensembl; ENSMUST00000224564; ENSMUSP00000153465; ENSMUSG00000052595. [Q5YD48-3]
DR GeneID; 69865; -.
DR KEGG; mmu:69865; -.
DR UCSC; uc008het.1; mouse. [Q5YD48-3]
DR UCSC; uc008heu.1; mouse. [Q5YD48-1]
DR UCSC; uc008hev.1; mouse. [Q5YD48-2]
DR CTD; 29974; -.
DR MGI; MGI:1917115; A1cf.
DR VEuPathDB; HostDB:ENSMUSG00000052595; -.
DR eggNOG; KOG0117; Eukaryota.
DR GeneTree; ENSGT00940000158678; -.
DR HOGENOM; CLU_022960_5_1_1; -.
DR InParanoid; Q5YD48; -.
DR OMA; VHFNKRE; -.
DR OrthoDB; 1384330at2759; -.
DR PhylomeDB; Q5YD48; -.
DR TreeFam; TF314932; -.
DR Reactome; R-MMU-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-MMU-75094; Formation of the Editosome.
DR BioGRID-ORCS; 69865; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q5YD48; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q5YD48; protein.
DR Bgee; ENSMUSG00000052595; Expressed in right kidney and 54 other tissues.
DR ExpressionAtlas; Q5YD48; baseline and differential.
DR Genevisible; Q5YD48; MM.
DR GO; GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR GO; GO:0045293; C:mRNA editing complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0016554; P:cytidine to uridine editing; IGI:MGI.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0010609; P:mRNA localization resulting in post-transcriptional regulation of gene expression; IGI:MGI.
DR GO; GO:0016556; P:mRNA modification; IGI:MGI.
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; ISO:MGI.
DR GO; GO:1901537; P:positive regulation of DNA demethylation; IC:ComplexPortal.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISS: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; 2.
DR TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; mRNA processing;
KW Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..595
FT /note="APOBEC1 complementation factor"
FT /id="PRO_0000081483"
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:0000250|UniProtKB:Q9NQ94"
FT VAR_SEQ 381..388
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15451168"
FT /id="VSP_051930"
FT VAR_SEQ 381..384
FT /note="EIYM -> GNTS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15451168,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051931"
FT VAR_SEQ 385..595
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15451168,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051932"
FT CONFLICT 140
FT /note="V -> R (in Ref. 1; AAT74916/AAT74917/AAT74918)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="I -> V (in Ref. 1; AAT74916/AAT74917)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 65682 MW; 324C2C8B853F8720 CRC64;
MESNHKSGDG LSGTQKEAAL RALVQRTGYS LVQENGQRKY GGPPPGWDST PPERGCEIFI
GKLPRDLFED ELIPLCEKIG KIYEMRLMMD FNGNNRGYAF VTFSNKQEAK NAIKQLNNYE
IRTGRLLGVC ASVDNCRLFV GGIPKTKKRE EILSEMKKVT EGVVDVIVYP SAADKTKNRG
FAFVEYESHR AAAMARRRLL PGRIQLWGHP IAVDWAEPEV EVDEDTMSSV KILYVRNLML
STSEEMIEKE FNSIKPGAVE RVKKIRDYAF VHFSNREDAV EAMKALNGKV LDGSPIEVTL
AKPVDKDSYV RYTRGTGGRN TMLQGEYTYP LSHVYDPTTT YLGAPVFYTP QAYAAIPSLH
FPATKGHLSN RALIRTPSVR EIYMNVPVGA AGVRGLGGRG YLAYTGLGRG YHVKGDKRED
KLYDLLPGME LTPMNTVSLK PQGIKLAPQI LEEICQKNNW GQPVYQLHSA IGQDQRQLFL
YKVTIPALAS QNPAIHPFIP PKLSAYVDEA KRYAAEHTLQ TLGIPTEGGD AGTTAPTATS
ATVFPGYAVP SATAPVSTAQ LKQAVTLGQD LAAYTTYEVY PTFALTTRGD AYGTF
