位置:首页 > 蛋白库 > ABEC2_PONPY
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024