ID   ABEC1_PONPY             Reviewed;         236 AA.
AC   Q694B3;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 73.
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   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15269786; DOI=10.1371/journal.pbio.0020275;
RA   Sawyer S.L., Emerman M., Malik H.S.;
RT   "Ancient adaptive evolution of the primate antiviral DNA-editing enzyme
RT   APOBEC3G.";
RL   PLoS Biol. 2:1278-1285(2004).
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. Also
CC       involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA. May also
CC       play a role in the epigenetic regulation of gene expression through the
CC       process of active 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 APC. 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT44389.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY622604; AAT44389.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY622600; AAT44389.1; JOINED; Genomic_DNA.
DR   EMBL; AY622601; AAT44389.1; JOINED; Genomic_DNA.
DR   EMBL; AY622603; AAT44389.1; JOINED; Genomic_DNA.
DR   EMBL; AY622602; AAT44389.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q694B3; -.
DR   SMR; Q694B3; -.
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; 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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; mRNA processing; Zinc.
FT   CHAIN           1..236
FT                   /note="C->U-editing enzyme APOBEC-1"
FT                   /id="PRO_0000171746"
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   236 AA;  28225 MW;  2DB53885D9BDF875 CRC64;
     MTSEKGPSTG DPTLRRRIES WEFDVFYDPR ELRKETCLLY EIKWGMSRKI WRSSGKNTTN
     HVEVNFIKKF TSERRFHSSI SCSITWFLSW SPCWECSQAI REFLSQHPGV TLVIYVARLF
     WHMDQRNRQG LRDLVNSGVT IQIMRASEYY HCWRNFVNYP PGDEAHWPQY PPLWMMLYAL
     ELHCIILSLP PCLKISRRWQ NHLAFFRLHL QNCHYQTIPP HILLATGLIH PSVTWR