ABEC2_MOUSE
ID ABEC2_MOUSE Reviewed; 224 AA.
AC Q9WV35;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=C->U-editing enzyme APOBEC-2;
DE EC=3.5.4.36;
DE AltName: Full=mRNA(cytosine(6666)) deaminase 2;
GN Name=Apobec2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=10403781; DOI=10.1006/bbrc.1999.0925;
RA Liao W., Hong S.-H., Chan B.H.-J., Rudolph F.B., Clark S.C., Chan L.;
RT "APOBEC-2, a cardiac- and skeletal muscle-specific member of the cytidine
RT deaminase supergene family.";
RL Biochem. Biophys. Res. Commun. 260:398-404(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=12859895; DOI=10.1016/s0092-8674(03)00515-4;
RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B.,
RA Muenk C., Nymark-McMahon H., Landau N.R.;
RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.";
RL Cell 114:21-31(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- TISSUE SPECIFICITY: Expressed exclusively in heart and skeletal muscle.
CC {ECO:0000269|PubMed:12859895}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AF161699; AAD45361.1; -; mRNA.
DR EMBL; BC027530; AAH27530.1; -; mRNA.
DR CCDS; CCDS28868.1; -.
DR RefSeq; NP_033824.1; NM_009694.3.
DR PDB; 2RPZ; NMR; -; A=46-224.
DR PDBsum; 2RPZ; -.
DR AlphaFoldDB; Q9WV35; -.
DR BMRB; Q9WV35; -.
DR SMR; Q9WV35; -.
DR BioGRID; 198159; 4.
DR STRING; 10090.ENSMUSP00000047402; -.
DR iPTMnet; Q9WV35; -.
DR PhosphoSitePlus; Q9WV35; -.
DR EPD; Q9WV35; -.
DR MaxQB; Q9WV35; -.
DR PaxDb; Q9WV35; -.
DR PeptideAtlas; Q9WV35; -.
DR PRIDE; Q9WV35; -.
DR ProteomicsDB; 285747; -.
DR Antibodypedia; 2816; 279 antibodies from 32 providers.
DR DNASU; 11811; -.
DR Ensembl; ENSMUST00000046549; ENSMUSP00000047402; ENSMUSG00000040694.
DR GeneID; 11811; -.
DR KEGG; mmu:11811; -.
DR UCSC; uc008cxx.1; mouse.
DR CTD; 10930; -.
DR MGI; MGI:1343178; Apobec2.
DR VEuPathDB; HostDB:ENSMUSG00000040694; -.
DR eggNOG; ENOG502RABR; Eukaryota.
DR GeneTree; ENSGT00940000156616; -.
DR HOGENOM; CLU_080056_0_0_1; -.
DR InParanoid; Q9WV35; -.
DR OMA; FVHVWET; -.
DR OrthoDB; 1380685at2759; -.
DR PhylomeDB; Q9WV35; -.
DR TreeFam; TF331356; -.
DR Reactome; R-MMU-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-MMU-75094; Formation of the Editosome.
DR BioGRID-ORCS; 11811; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Apobec2; mouse.
DR EvolutionaryTrace; Q9WV35; -.
DR PRO; PR:Q9WV35; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9WV35; protein.
DR Bgee; ENSMUSG00000040694; Expressed in quadriceps femoris and 74 other tissues.
DR Genevisible; Q9WV35; MM.
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; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
DR GO; GO:0016556; P:mRNA modification; IMP:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; mRNA processing;
KW Reference proteome; Zinc.
FT CHAIN 1..224
FT /note="C->U-editing enzyme APOBEC-2"
FT /id="PRO_0000171750"
FT DOMAIN 64..169
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 1..23
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"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2RPZ"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:2RPZ"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:2RPZ"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:2RPZ"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:2RPZ"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:2RPZ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2RPZ"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:2RPZ"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:2RPZ"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:2RPZ"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:2RPZ"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2RPZ"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:2RPZ"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2RPZ"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:2RPZ"
SQ SEQUENCE 224 AA; 25660 MW; 75F98BC2CF2EBE0A CRC64;
MAQKEEAAEA AAPASQNGDD LENLEDPEKL KELIDLPPFE IVTGVRLPVN FFKFQFRNVE
YSSGRNKTFL CYVVEVQSKG GQAQATQGYL EDEHAGAHAE EAFFNTILPA FDPALKYNVT
WYVSSSPCAA CADRILKTLS KTKNLRLLIL VSRLFMWEEP EVQAALKKLK EAGCKLRIMK
PQDFEYIWQN FVEQEEGESK AFEPWEDIQE NFLYYEEKLA DILK
