ID   ABEC2_BOVIN             Reviewed;         224 AA.
AC   Q3SYR3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Probable C->U-editing enzyme APOBEC-2;
DE            EC=3.5.4.36;
DE   AltName: Full=mRNA(cytosine(6666)) deaminase 2;
GN   Name=APOBEC2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Korean;
RA   Chung H.J., Jung K.C., Lee Y.J., Lee J.H., Yoon D.H., Lee S.H., Sang B.C.;
RT   "Characterization of apolipoprotein B mRNA editing enzyme catalytic
RT   polypeptide-like 2 (APOBEC-2) in Korean cattle.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable C to U editing enzyme whose physiological substrate
CC       is not yet known. Does not display detectable apoB mRNA editing. Has a
CC       low intrinsic cytidine deaminase activity. May play a role in the
CC       epigenetic regulation of gene expression through the process of active
CC       DNA demethylation. {ECO:0000250|UniProtKB:Q9Y235}.
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:Q9Y235};
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: Homotetramer. {ECO:0000250|UniProtKB:Q9Y235}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; DQ280381; ABB90107.1; -; mRNA.
DR   EMBL; BC103438; AAI03439.1; -; mRNA.
DR   RefSeq; NP_001029527.1; NM_001034355.1.
DR   AlphaFoldDB; Q3SYR3; -.
DR   SMR; Q3SYR3; -.
DR   STRING; 9913.ENSBTAP00000035907; -.
DR   PaxDb; Q3SYR3; -.
DR   PRIDE; Q3SYR3; -.
DR   GeneID; 509619; -.
DR   KEGG; bta:509619; -.
DR   CTD; 10930; -.
DR   eggNOG; ENOG502RABR; Eukaryota.
DR   HOGENOM; CLU_080056_0_0_1; -.
DR   InParanoid; Q3SYR3; -.
DR   OrthoDB; 1380685at2759; -.
DR   TreeFam; TF331356; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0016554; P:cytidine to uridine editing; IBA:GO_Central.
DR   GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; mRNA processing; Reference proteome; Zinc.
FT   CHAIN           1..224
FT                   /note="Probable C->U-editing enzyme APOBEC-2"
FT                   /id="PRO_0000244422"
FT   DOMAIN          64..169
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        100
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y235"
SQ   SEQUENCE   224 AA;  25962 MW;  54881038F34C504C CRC64;
     MAQKEEAAAA AEPASQNGEE VENLEDPEKL KELIELPPFE IVTGERLPAH YFKFQFRNVE
     YSSGRNKTFL CYVVEAQSKG GQVQASRGYL EDEHATNHAE EAFFNSIMPT FDPALRYMVT
     WYVSSSPCAA CADRIVKTLN KTKNLRLLIL VGRLFMWEEP EIQAALRKLK EAGCRLRIMK
     PQDFEYIWQN FVEQEEGESK AFEPWEDIQE NFLYYEEKLA DILK