ABEC1_MOUSE
ID ABEC1_MOUSE Reviewed; 229 AA.
AC P51908; Q99L67;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=C->U-editing enzyme APOBEC-1;
DE EC=3.5.4.36;
DE AltName: Full=Apolipoprotein B mRNA-editing enzyme 1;
DE AltName: Full=mRNA(cytosine(6666)) deaminase 1;
GN Name=Apobec1;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Small intestine;
RX PubMed=7768898; DOI=10.1074/jbc.270.22.13042;
RA Nakamuta M., Oka K., Krushkal J., Kobayashi K., Yamamoto M., Li W.H.,
RA Chan L.;
RT "Alternative mRNA splicing and differential promoter utilization determine
RT tissue-specific expression of the apolipoprotein B mRNA-editing protein
RT (Apobec1) gene in mice. Structure and evolution of Apobec1 and related
RT nucleoside/nucleotide deaminases.";
RL J. Biol. Chem. 270:13042-13056(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=12859895; DOI=10.1016/s0092-8674(03)00515-4;
RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B.,
RA Muenk C., Nymark-McMahon H., Landau N.R.;
RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.";
RL Cell 114:21-31(2003).
RN [4]
RP FUNCTION IN DNA DEMETHYLATION.
RX PubMed=21496894; DOI=10.1016/j.cell.2011.03.022;
RA Guo J.U., Su Y., Zhong C., Ming G.L., Song H.;
RT "Hydroxylation of 5-methylcytosine by TET1 promotes active DNA
RT demethylation in the adult brain.";
RL Cell 145:423-434(2011).
CC -!- FUNCTION: Catalytic 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 the APOB mRNA. May
CC also play a role in the epigenetic regulation of gene expression by
CC participating in DNA demethylation. {ECO:0000269|PubMed:21496894}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(6666) in apoB mRNA + H(+) + H2O = NH4(+) +
CC uridine(6666) in apoB mRNA; Xref=Rhea:RHEA:21772, Rhea:RHEA-
CC COMP:13888, Rhea:RHEA-COMP:13889, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:65315,
CC ChEBI:CHEBI:82748; EC=3.5.4.36;
CC Evidence={ECO:0000250|UniProtKB:P41238};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9Y235};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9Y235};
CC -!- SUBUNIT: Homodimer. Part of the apolipoprotein B mRNA editing complex
CC with APC. Interacts with HNRPAB and SYNCRIP.
CC {ECO:0000250|UniProtKB:P41238}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41238}.
CC -!- TISSUE SPECIFICITY: Expressed in the spleen. Expressed at lower level
CC in the kidney, testis, lung, brain and liver.
CC {ECO:0000269|PubMed:12859895}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; U21951; AAC52211.1; -; Genomic_DNA.
DR EMBL; U21947; AAC52211.1; JOINED; Genomic_DNA.
DR EMBL; U21948; AAC52211.1; JOINED; Genomic_DNA.
DR EMBL; U21949; AAC52211.1; JOINED; Genomic_DNA.
DR EMBL; U21950; AAC52211.1; JOINED; Genomic_DNA.
DR EMBL; U22262; AAC52212.1; -; mRNA.
DR EMBL; U22263; AAC52213.1; -; mRNA.
DR EMBL; U22264; AAC52214.1; -; mRNA.
DR EMBL; BC003792; AAH03792.1; -; mRNA.
DR CCDS; CCDS20498.1; -.
DR PIR; I48249; I48249.
DR RefSeq; NP_001127863.1; NM_001134391.1.
DR RefSeq; NP_112436.1; NM_031159.3.
DR RefSeq; XP_006505464.1; XM_006505401.2.
DR RefSeq; XP_011239461.1; XM_011241159.2.
DR AlphaFoldDB; P51908; -.
DR SMR; P51908; -.
DR BioGRID; 198158; 2.
DR ComplexPortal; CPX-1098; C-to-U editosome complex.
DR STRING; 10090.ENSMUSP00000108205; -.
DR iPTMnet; P51908; -.
DR PhosphoSitePlus; P51908; -.
DR PaxDb; P51908; -.
DR PeptideAtlas; P51908; -.
DR PRIDE; P51908; -.
DR ProteomicsDB; 285746; -.
DR Antibodypedia; 22955; 169 antibodies from 26 providers.
DR DNASU; 11810; -.
DR Ensembl; ENSMUST00000112585; ENSMUSP00000108204; ENSMUSG00000040613.
DR Ensembl; ENSMUST00000112586; ENSMUSP00000108205; ENSMUSG00000040613.
DR Ensembl; ENSMUST00000112587; ENSMUSP00000108206; ENSMUSG00000040613.
DR GeneID; 11810; -.
DR KEGG; mmu:11810; -.
DR UCSC; uc009dpk.1; mouse.
DR CTD; 339; -.
DR MGI; MGI:103298; Apobec1.
DR VEuPathDB; HostDB:ENSMUSG00000040613; -.
DR eggNOG; ENOG502SNW2; Eukaryota.
DR GeneTree; ENSGT00940000161190; -.
DR HOGENOM; CLU_080056_3_0_1; -.
DR InParanoid; P51908; -.
DR OMA; MKLYALE; -.
DR OrthoDB; 1246623at2759; -.
DR PhylomeDB; P51908; -.
DR TreeFam; TF331356; -.
DR BRENDA; 3.5.4.1; 3474.
DR BRENDA; 3.5.4.36; 3474.
DR Reactome; R-MMU-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-MMU-75094; Formation of the Editosome.
DR BioGRID-ORCS; 11810; 0 hits in 112 CRISPR screens.
DR ChiTaRS; Apobec1; mouse.
DR PRO; PR:P51908; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P51908; protein.
DR Bgee; ENSMUSG00000040613; Expressed in granulocyte and 146 other tissues.
DR ExpressionAtlas; P51908; baseline and differential.
DR Genevisible; P51908; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0045293; C:mRNA editing complex; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004126; F:cytidine deaminase activity; ISO:MGI.
DR GO; GO:0004131; F:cytosine deaminase activity; ISO:MGI.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016554; P:cytidine to uridine editing; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0070383; P:DNA cytosine deamination; ISO:MGI.
DR GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IGI:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IMP:MGI.
DR GO; GO:0042953; P:lipoprotein transport; IGI:MGI.
DR GO; GO:0016556; P:mRNA modification; IDA:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IDA:MGI.
DR GO; GO:0090310; P:negative regulation of DNA methylation-dependent heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0090209; P:negative regulation of triglyceride metabolic process; IGI:MGI.
DR GO; GO:1901537; P:positive regulation of DNA demethylation; IC:ComplexPortal.
DR GO; GO:0090366; P:positive regulation of mRNA modification; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
DR GO; GO:0006970; P:response to osmotic stress; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; IGI:MGI.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR041547; APOBEC1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF18774; APOBEC4_like; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; mRNA processing; Reference proteome;
KW Zinc.
FT CHAIN 1..229
FT /note="C->U-editing enzyme APOBEC-1"
FT /id="PRO_0000171745"
FT DOMAIN 10..134
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 63
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT CONFLICT 106
FT /note="R -> Q (in Ref. 2; AAH03792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 27522 MW; 1CBCF9929066ABAD CRC64;
MSSETGPVAV DPTLRRRIEP HEFEVFFDPR ELRKETCLLY EINWGGRHSV WRHTSQNTSN
HVEVNFLEKF TTERYFRPNT RCSITWFLSW SPCGECSRAI TEFLSRHPYV TLFIYIARLY
HHTDQRNRQG LRDLISSGVT IQIMTEQEYC YCWRNFVNYP PSNEAYWPRY PHLWVKLYVL
ELYCIILGLP PCLKILRRKQ PQLTFFTITL QTCHYQRIPP HLLWATGLK
