A1CF_RAT
ID A1CF_RAT Reviewed; 594 AA.
AC Q923K9; Q8CH55; Q8CH56; Q8CH57; Q8CH58; Q924K3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=APOBEC1 complementation factor;
DE AltName: Full=APOBEC1-stimulating protein;
GN Name=A1cf; Synonyms=Acf, Asp {ECO:0000250|UniProtKB:Q9NQ94};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK83095.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAK83095.1};
RC TISSUE=Liver {ECO:0000269|PubMed:11870221};
RX PubMed=11870221; DOI=10.1242/jcs.115.5.1027;
RA Sowden M.P., Ballatori N., de Mesy Jensen K.L., Hamilton Reed L.,
RA Smith H.C.;
RT "The editosome for cytidine to uridine mRNA editing has a native complexity
RT of 27S: identification of intracellular domains containing active and
RT inactive editing factors.";
RL J. Cell Sci. 115:1027-1039(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAO15466.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 295-594 (ISOFORM 3), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 295-409
RP (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAO15466.1};
RC TISSUE=Liver {ECO:0000269|PubMed:14570923};
RX PubMed=14570923; DOI=10.1074/jbc.m307920200;
RA Sowden M.P., Lehmann D.M., Lin X., Smith C.O., Smith H.C.;
RT "Identification of novel alternative splice variants of APOBEC-1
RT complementation factor with different capacities to support apolipoprotein
RT B mRNA editing.";
RL J. Biol. Chem. 279:197-206(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAK50145.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RA Sowden M.P., Smith H.C.;
RT "An isoform of rat APOBEC-1 complementation factor p66/ACF.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Liver {ECO:0000269|PubMed:10781591};
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).
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). {ECO:0000250|UniProtKB:Q9NQ94,
CC ECO:0000269|PubMed:10781591}.
CC -!- SUBUNIT: Part of the apolipoprotein B mRNA editing complex with
CC APOBEC1. Found in a complex with APOBEC1 and CELF2/CUGBP2. Interacts
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:0000269|PubMed:11870221}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:11870221}. Cytoplasm
CC {ECO:0000269|PubMed:11870221}. Note=Predominantly nuclear where it
CC localizes to heterochromatin. Also cytoplasmic where it is found at the
CC outer surface of the endoplasmic reticulum. Shuttles between the
CC nucleus and cytoplasm. May be transported into the nucleus by the
CC nuclear import protein TNPO2/TRN2 or by APOBEC1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:14570923}; Synonyms=ACF65
CC {ECO:0000303|PubMed:14570923};
CC IsoId=Q923K9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11870221}; Synonyms=ACF64
CC {ECO:0000303|PubMed:14570923};
CC IsoId=Q923K9-2; Sequence=VSP_051934;
CC Name=3 {ECO:0000269|PubMed:14570923}; Synonyms=ACF45
CC {ECO:0000303|PubMed:14570923};
CC IsoId=Q923K9-3; Sequence=VSP_051933, VSP_051937;
CC Name=4 {ECO:0000269|PubMed:14570923}; Synonyms=ACF43
CC {ECO:0000303|PubMed:14570923};
CC IsoId=Q923K9-4; Sequence=VSP_051935, VSP_051936;
CC -!- TISSUE SPECIFICITY: Isoforms 1 and 2 are widely expressed while
CC isoforms 3 and 4 are restricted to liver and small intestine.
CC {ECO:0000269|PubMed:14570923}.
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}.
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DR EMBL; AF290984; AAK83095.1; -; mRNA.
DR EMBL; AF442133; AAO15465.1; -; mRNA.
DR EMBL; AF442134; AAO15466.1; -; mRNA.
DR EMBL; AF442135; AAO15467.1; -; Genomic_DNA.
DR EMBL; AF442135; AAO15468.1; -; Genomic_DNA.
DR EMBL; AY028945; AAK50145.1; -; mRNA.
DR RefSeq; NP_596891.1; NM_133400.1. [Q923K9-2]
DR AlphaFoldDB; Q923K9; -.
DR SMR; Q923K9; -.
DR CORUM; Q923K9; -.
DR IntAct; Q923K9; 1.
DR STRING; 10116.ENSRNOP00000062802; -.
DR iPTMnet; Q923K9; -.
DR PhosphoSitePlus; Q923K9; -.
DR PaxDb; Q923K9; -.
DR PRIDE; Q923K9; -.
DR GeneID; 170912; -.
DR KEGG; rno:170912; -.
DR UCSC; RGD:619834; rat. [Q923K9-1]
DR CTD; 29974; -.
DR RGD; 619834; A1cf.
DR eggNOG; KOG0117; Eukaryota.
DR InParanoid; Q923K9; -.
DR PhylomeDB; Q923K9; -.
DR Reactome; R-RNO-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-RNO-75094; Formation of the Editosome.
DR PRO; PR:Q923K9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0000792; C:heterochromatin; IDA:RGD.
DR GO; GO:0045293; C:mRNA editing complex; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IDA:RGD.
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; IMP:RGD.
DR GO; GO:0007566; P:embryo implantation; ISO:RGD.
DR GO; GO:0010609; P:mRNA localization resulting in post-transcriptional regulation of gene expression; ISO:RGD.
DR GO; GO:0016556; P:mRNA modification; ISO:RGD.
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:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:RGD.
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; 3.
DR TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..594
FT /note="APOBEC1 complementation factor"
FT /id="PRO_0000081485"
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 359..408
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ94"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ94"
FT VAR_SEQ 380..405
FT /note="EIYMNVPVGAAGVRGLGGRGYLAYTG -> GCSRTPSIYLCFLTAVHAGVHH
FT IHVQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14570923"
FT /id="VSP_051933"
FT VAR_SEQ 380..387
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11870221"
FT /id="VSP_051934"
FT VAR_SEQ 380..383
FT /note="EIYM -> GNIS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14570923"
FT /id="VSP_051935"
FT VAR_SEQ 384..594
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14570923"
FT /id="VSP_051936"
FT VAR_SEQ 406..594
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14570923"
FT /id="VSP_051937"
FT CONFLICT 348
FT /note="T -> A (in Ref. 2; AAO15465/AAO15466)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="G -> P (in Ref. 2; AAO15467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 65620 MW; F04D93EE25D5EF6C CRC64;
MESNHKSGDG LSGTQKEAAL RALVQRTGYS LVQENGQRKY GGPPPGWDTT PPERGCEIFI
GKLPRDLFED ELIPLCEKIG KIYEMRMMMD FNGNNRGYAF VTFSNKQEAK NAIKQLNNYE
IRNGRLLGVC ASVDNCRLFV GGIPKTKKRE EILSEMKKVT EGVVDVIVYP SAADKTKNRG
FAFVEYESHR AAAMARRRLL PGRIQLWGHP IAVDWAEPEV EVDEDTMSSV KILYVRNLML
STSEEMIEKE FNSIKPGAVE RVKKIRDYAF VHFSNREDAV EAMKALNGKV LDGSPIEVTL
AKPVDKDSYV RYTRGTGGRN TMLQEYTYPL SHVYDPTTTY LGAPVFYTPQ AYAAIPSLHF
PATKGHLSNR ALIRTPSVRE IYMNVPVGAA GVRGLGGRGY LAYTGLGRGY QVKGDKRQDK
LYDLLPGMEL TPMNTISLKP QGVKLAPQIL EEICQKNNWG QPVYQLHSAI GQDQRQLFLY
KVTIPALASQ NPAIHPFTPP KLSAYVDEAK RYAAEHTLQT LGIPTEGGDA GTTAPTATSA
TVFPGYAVPS ATAPVSTAQL KQAVTLGQDL AAYTTYEVYP TFAVTTRGDG YGTF
