ABEC2_PONPY
ID ABEC2_PONPY Reviewed; 224 AA.
AC Q694B4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- 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; AY622599; AAT44388.1; -; Genomic_DNA.
DR EMBL; AY622598; AAT44388.1; JOINED; Genomic_DNA.
DR EMBL; CR858504; CAH90732.1; -; mRNA.
DR AlphaFoldDB; Q694B4; -.
DR BMRB; Q694B4; -.
DR SMR; Q694B4; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Zinc.
FT CHAIN 1..224
FT /note="Probable C->U-editing enzyme APOBEC-2"
FT /id="PRO_0000171751"
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; 25735 MW; 24C9BDDE8621EEDB CRC64;
MAQKEEAAAA TEAASQNGED LENLDDPEKL KELIELPPFE IVTGERLPAN FFKFQFRNVE
YSSGRNKTFL CYVVEAQGKG GQVQASRGYL EDEHAAAHAE EAFFNTILPA FDPALRYNVT
WYVSSSPCAA CADRIIKTLS KTKNLRLLIL VGRLFMWEEL EIQDALKKLK EAGCKLRIMK
PQDFEYVWQN FVEQEEGESK AFQPWEDIQE NFLYYEEKLA DILK