ID   ABC3C_GORGO             Reviewed;         190 AA.
AC   Q694B5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=DNA dC->dU-editing enzyme APOBEC-3C;
DE            Short=A3C;
DE            EC=3.5.4.38;
GN   Name=APOBEC3C;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
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: DNA deaminase (cytidine deaminase) which acts as an inhibitor
CC       of retrovirus replication and retrotransposon mobility via deaminase-
CC       dependent and -independent mechanisms. May also play a role in the
CC       epigenetic regulation of gene expression through the process of active
CC       DNA demethylation (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Interacts with TRIB3 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; AY622597; AAT44387.1; -; Genomic_DNA.
DR   EMBL; AY622594; AAT44387.1; JOINED; Genomic_DNA.
DR   EMBL; AY622595; AAT44387.1; JOINED; Genomic_DNA.
DR   EMBL; AY622596; AAT44387.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q694B5; -.
DR   SMR; Q694B5; -.
DR   InParanoid; Q694B5; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
DR   GO; GO:0047844; F:deoxycytidine deaminase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009972; P:cytidine deamination; ISS:UniProtKB.
DR   GO; GO:0016554; P:cytidine to uridine editing; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR   GO; GO:0070383; P:DNA cytosine deamination; IBA:GO_Central.
DR   GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IBA:GO_Central.
DR   GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
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   Antiviral defense; Cytoplasm; Hydrolase; Immunity; Innate immunity;
KW   Metal-binding; Nucleus; Reference proteome; Zinc.
FT   CHAIN           1..190
FT                   /note="DNA dC->dU-editing enzyme APOBEC-3C"
FT                   /id="PRO_0000171754"
FT   DOMAIN          29..138
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRW3"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRW3"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRW3"
SQ   SEQUENCE   190 AA;  22888 MW;  20EC02539829E6A8 CRC64;
     MNPQIRNPMK AMYPGTFYFQ FKNLWEANDR NETWLCFTVE GIKRRSVVSW KTGVFRNQVD
     SETHCHAERC FLSWFCDDIL SPNTNYQVTW YTSWSPCPEC AGEVAEFLAR HSNVNLTIFT
     ARLYYFQDTD YQEGLRSLSQ EGVAVKIMDY KDFKYCWENF VYNDDEPFKP WKGLKYNFRF
     LKRRLQEILE