ID   ABEC1_MESAU             Reviewed;         229 AA.
AC   Q9EQP0;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Syrian;
RX   PubMed=10958808; DOI=10.1093/jn/130.9.2166;
RA   Reaves S.K., Wu J.Y.J., Wu Y., Fanzo J.C., Wang Y.R., Lei P.P., Lei K.Y.;
RT   "Regulation of intestinal apolipoprotein B mRNA editing levels by a zinc-
RT   deficient diet and cDNA cloning of editing protein in hamsters.";
RL   J. Nutr. 130:2166-2173(2000).
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:0000250|UniProtKB:P41238}.
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 A1CF. Interacts with HNRPAB and SYNCRIP.
CC       {ECO:0000250|UniProtKB:P41238}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41238}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; AF176577; AAG43414.1; -; mRNA.
DR   RefSeq; NP_001268585.1; NM_001281656.1.
DR   AlphaFoldDB; Q9EQP0; -.
DR   SMR; Q9EQP0; -.
DR   STRING; 10036.XP_005066090.1; -.
DR   GeneID; 101825976; -.
DR   CTD; 339; -.
DR   eggNOG; ENOG502SNW2; Eukaryota.
DR   BRENDA; 3.5.4.36; 3239.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0090310; P:negative regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   2: Evidence at transcript 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_0000171743"
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"
SQ   SEQUENCE   229 AA;  27585 MW;  E3F82BD73E31428D CRC64;
     MSSETGPVVV DPTLRRRIEP HEFDAFFDQG ELRKETCLLY EIRWGGRHNI WRHTGQNTSR
     HVEINFIEKF TSERYFYPST RCSIVWFLSW SPCGECSKAI TEFLSGHPNV TLFIYAARLY
     HHTDQRNRQG LRDLISRGVT IRIMTEQEYC YCWRNFVNYP PSNEVYWPRY PNLWMRLYAL
     ELYCIHLGLP PCLKIKRRHQ YPLTFFRLNL QSCHYQRIPP HILWATGFI