ABC3G_GORGO
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 03-AUG-2022, entry version 81.
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}.
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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.ENSGGOP00000026801; -.
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; ISS:UniProtKB.
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:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR040551; APOBEC3G.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR PANTHER; PTHR13857:SF20; PTHR13857:SF20; 1.
DR SUPFAM; SSF53927; SSF53927; 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
