ID G7P3F1_MACFA Unreviewed; 224 AA.
AC G7P3F1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=single-stranded DNA cytosine deaminase {ECO:0000256|ARBA:ARBA00029489};
DE EC=3.5.4.38 {ECO:0000256|ARBA:ARBA00029489};
GN Name=APOBEC2 {ECO:0000313|Ensembl:ENSMFAP00000026392.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000026392.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000026392.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000026392.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-
CC deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948,
CC Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452,
CC ChEBI:CHEBI:133902; EC=3.5.4.38;
CC Evidence={ECO:0000256|ARBA:ARBA00029350};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
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DR AlphaFoldDB; G7P3F1; -.
DR STRING; 9541.ENSMFAP00000026392; -.
DR Ensembl; ENSMFAT00000000573.2; ENSMFAP00000026392.2; ENSMFAG00000044645.2.
DR VEuPathDB; HostDB:ENSMFAG00000044645; -.
DR eggNOG; ENOG502RABR; Eukaryota.
DR GeneTree; ENSGT00940000156616; -.
DR OrthoDB; 4187079at2759; -.
DR Proteomes; UP000233100; Chromosome 4.
DR Bgee; ENSMFAG00000044645; Expressed in skeletal muscle tissue and 10 other cell types or tissues.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0016554; P:cytidine to uridine editing; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0080111; P:DNA demethylation; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0016556; P:mRNA modification; IEA:Ensembl.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR PANTHER; PTHR13857:SF4; C-U-EDITING ENZYME APOBEC-2; 1.
DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1.
DR Pfam; PF18772; APOBEC2; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT DOMAIN 64..169
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 224 AA; 25591 MW; 1BF8CB33F0262D26 CRC64;
MAQKEEAAAA AEAASQNGED LENLDDPEKL KELIELPPFE IVTGERLPAN FFKFQFRNVE
YSSGRNKTFL CYVVEAQGKG GQVQASQGYL EDEHAAAHAE EAFFNTILPA FDPALRYNVT
WYVSSSPCAA CADRITKTLS KTKNLRLLIL VGRLFMWEEP EIQAALKKLK EAGCKLRIMK
PQDFEYVWQN FVEQEEGESK AFQPWEDVQE NFLYYEEKLA DILK
//
