ID ABC3G_GORGO Reviewed; 384 AA. AC Q694C1; Q6DVQ0; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 24-JAN-2024, entry version 86. DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G {ECO:0000250|UniProtKB:Q9HC16}; DE EC=3.5.4.38 {ECO:0000250|UniProtKB:Q9HC16}; DE AltName: Full=Deoxycytidine deaminase; GN Name=APOBEC3G; 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 [MRNA]. RX PubMed=15198990; DOI=10.1093/hmg/ddh183; RA Zhang J., Webb D.M.; RT "Rapid evolution of primate antiviral enzyme APOBEC3G."; RL Hum. Mol. Genet. 13:1785-1791(2004). RN [2] 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. After the CC penetration of retroviral nucleocapsids into target cells of infection CC and the initiation of reverse transcription, it can induce the CC conversion of cytosine to uracil in the minus-sense single-strand viral CC DNA, leading to G-to-A hypermutations in the subsequent plus-strand CC viral DNA. The resultant detrimental levels of mutations in the CC proviral genome, along with a deamination-independent mechanism that CC works prior to the proviral integration, together exert efficient CC antiretroviral effects in infected target cells. Selectively targets CC single-stranded DNA and does not deaminate double-stranded DNA or CC single- or double-stranded RNA (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 Evidence={ECO:0000250|UniProtKB:Q9HC16}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:Q9HC16}; CC -!- ACTIVITY REGULATION: Assembly into ribonucleoprotein complexes of high- CC molecular-mass (HMM) inhibits its enzymatic activity. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. Homooligomer. Can bind RNA to form CC ribonucleoprotein complexes of high-molecular-mass (HMM) or low- CC molecular-mass (LMM). HMM is inactive and heterogeneous in protein CC composition because of binding nonselectively to cellular RNAs, which CC in turn are associated with variety of cellular proteins. The LMM form CC which is enzymatically active has few or no RNAs associated. Its CC ability to form homooligomer is distinct from its ability to assemble CC into HMM. Interacts with APOBEC3B, APOBEC3F, MOV10, AGO2, EIF4E, CC EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent manner. Interacts with CC AGO1, AGO3 and PKA/PRKACA (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC Cytoplasm, P-body {ECO:0000250}. Note=Mainly cytoplasmic, small amount CC are found in the nucleus. {ECO:0000250}. CC -!- DOMAIN: The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA- CC dependent oligomerization and virion incorporation whereas the CMP/dCMP CC deaminase domain 2 confers deoxycytidine deaminase activity and CC substrate sequence specificity. {ECO:0000250}. 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; AY639868; AAT72157.1; -; mRNA. DR EMBL; AY622553; AAT44394.1; -; Genomic_DNA. DR EMBL; AY622546; AAT44394.1; JOINED; Genomic_DNA. DR EMBL; AY622547; AAT44394.1; JOINED; Genomic_DNA. DR EMBL; AY622548; AAT44394.1; JOINED; Genomic_DNA. DR EMBL; AY622549; AAT44394.1; JOINED; Genomic_DNA. DR EMBL; AY622550; AAT44394.1; JOINED; Genomic_DNA. DR EMBL; AY622551; AAT44394.1; JOINED; Genomic_DNA. DR EMBL; AY622552; AAT44394.1; JOINED; Genomic_DNA. DR AlphaFoldDB; Q694C1; -. DR SMR; Q694C1; -. DR STRING; 9593.ENSGGOP00000021965; -. DR eggNOG; KOG4075; Eukaryota. DR InParanoid; Q694C1; -. DR Proteomes; UP000001519; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000932; C:P-body; ISS:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central. DR GO; GO:0047844; F:deoxycytidine deaminase activity; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0070383; P:DNA cytosine deamination; IBA:GO_Central. DR GO; GO:0080111; P:DNA demethylation; IBA:GO_Central. 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:0010526; P:retrotransposon silencing; ISS:UniProtKB. DR CDD; cd01283; cytidine_deaminase; 2. DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 2. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_dom. DR InterPro; IPR016193; Cytidine_deaminase-like. DR PANTHER; PTHR13857:SF20; DNA DC-DU-EDITING ENZYME APOBEC-3G; 1. DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1. DR Pfam; PF18782; NAD2; 2. DR SUPFAM; SSF53927; Cytidine deaminase-like; 2. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2. PE 2: Evidence at transcript level; KW Antiviral defense; Cytoplasm; Hydrolase; Immunity; Innate immunity; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc. FT CHAIN 1..384 FT /note="DNA dC->dU-editing enzyme APOBEC-3G" FT /id="PRO_0000171760" FT DOMAIN 29..138 FT /note="CMP/dCMP-type deaminase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT DOMAIN 214..328 FT /note="CMP/dCMP-type deaminase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT REGION 1..60 FT /note="Essential for cytoplasmic localization" FT /evidence="ECO:0000250" FT REGION 209..336 FT /note="Necessary for homooligomerization" FT /evidence="ECO:0000250" FT REGION 213..215 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT REGION 313..320 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT ACT_SITE 259 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 257 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 288 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 291 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT SITE 244 FT /note="Interaction with DNA" FT /evidence="ECO:0000250" FT MOD_RES 32 FT /note="Phosphothreonine; by PKA" FT /evidence="ECO:0000250|UniProtKB:Q9HC16" FT MOD_RES 218 FT /note="Phosphothreonine; by PKA and CAMK2" FT /evidence="ECO:0000250|UniProtKB:Q9HC16" FT CONFLICT 3 FT /note="P -> S (in Ref. 1; AAT72157)" FT /evidence="ECO:0000305" FT CONFLICT 62 FT /note="L -> F (in Ref. 1; AAT72157)" FT /evidence="ECO:0000305" FT CONFLICT 352 FT /note="Y -> D (in Ref. 1; AAT72157)" FT /evidence="ECO:0000305" SQ SEQUENCE 384 AA; 46269 MW; 7BA709E91D3C68DA CRC64; MTPQFRNTVE RMYRDTFSYN FNNRPILSRR NTVWLCYEVK TKDPSRPPLD AKIFRGQVYS ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC TRNVATFLAE DPKVTLTIFV ARLYYFWDQD YQEALRSLCQ KRDGPRATMK IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK YYMLLHIMLG EILRHSMDPP TFTSNFNNEH WVRGRHETYL CYEVERLHND TWVLLNQRRG FLCNQAPHKH GFLEGRHAEL CFLDVIPFWK LDLHQDYRVT CFTSWSPCFS CAQEMAKFIS NKKHVSLCIF AARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF VYHQGCPFQP WDGLEEHSQA LSGRLQAILQ NQGN //