ABC3G_PANTR
ID ABC3G_PANTR Reviewed; 384 AA.
AC Q7YR24; Q694C3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 96.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-378, FUNCTION IN DNA C TO U EDITING, AND
RP SPECIES-SPECIFIC RESTRICTION TO HIV-1 INFECTION.
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 [3]
RP FUNCTION IN SFV RESTRICTION.
RX PubMed=16378963; DOI=10.1128/jvi.80.2.605-614.2006;
RA Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A.,
RA Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O.;
RT "Restriction of foamy viruses by APOBEC cytidine deaminases.";
RL J. Virol. 80:605-614(2006).
RN [4]
RP REVIEW.
RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350;
RA Chiu Y.L., Greene W.C.;
RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing
RT exogenous retroviruses and endogenous retroelements.";
RL Annu. Rev. Immunol. 26:317-353(2008).
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. Exhibits antiviral activity
CC against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs)
CC and also against simian foamy virus (SFV). After the penetration of
CC retroviral nucleocapsids into target cells of infection and the
CC initiation of reverse transcription, it can induce the conversion of
CC cytosine to uracil in the minus-sense single-strand viral DNA, leading
CC to G-to-A hypermutations in the subsequent plus-strand viral DNA. The
CC resultant detrimental levels of mutations in the proviral genome, along
CC with a deamination-independent mechanism that works prior to the
CC proviral integration, together exert efficient antiretroviral effects
CC in infected target cells. Selectively targets single-stranded DNA and
CC does not deaminate double-stranded DNA or single- or double-stranded
CC RNA. May inhibit the mobility of LTR retrotransposons.
CC {ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:16378963}.
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. Antiviral
CC activity is neutralized by the HIV-1 virion infectivity factor (VIF)
CC and simian immunodeficiency virus (SIV-cpz) VIF, that prevents its
CC incorporation into progeny virions by both inhibiting its translation
CC and/or by inducing its ubiquitination and subsequent degradation by the
CC 26S proteasome (By similarity). {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 -!- MISCELLANEOUS: Accumulation of APOBEC3G induced non-lethal
CC hypermutation could contribute to the genetic variation of primate
CC lentiviral populations.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AY622537; AAT44392.1; -; Genomic_DNA.
DR EMBL; AY622530; AAT44392.1; JOINED; Genomic_DNA.
DR EMBL; AY622531; AAT44392.1; JOINED; Genomic_DNA.
DR EMBL; AY622532; AAT44392.1; JOINED; Genomic_DNA.
DR EMBL; AY622533; AAT44392.1; JOINED; Genomic_DNA.
DR EMBL; AY622534; AAT44392.1; JOINED; Genomic_DNA.
DR EMBL; AY622535; AAT44392.1; JOINED; Genomic_DNA.
DR EMBL; AY622536; AAT44392.1; JOINED; Genomic_DNA.
DR EMBL; AY331715; AAP85255.1; -; mRNA.
DR AlphaFoldDB; Q7YR24; -.
DR SMR; Q7YR24; -.
DR STRING; 9598.ENSPTRP00000024786; -.
DR PaxDb; Q7YR24; -.
DR eggNOG; KOG4075; Eukaryota.
DR InParanoid; Q7YR24; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016553; P:base conversion or substitution editing; IEA:InterPro.
DR GO; GO:0009972; P:cytidine deamination; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0070383; P:DNA cytosine deamination; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA: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; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 1: Evidence at protein 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_0000171767"
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 4
FT /note="H -> Q (in Ref. 2; AAP85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="G -> E (in Ref. 2; AAP85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="R -> Q (in Ref. 2; AAP85255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 46089 MW; F1E45739870F0319 CRC64;
MKPHFRNPVE RMYQDTFSDN FYNRPILSHR NTVWLCYEVK TKGPSRPPLD AKIFRGQVYS
KLKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC TRDVATFLAE DPKVTLTIFV
ARLYYFWDPD YQEALRSLCQ KRDGPRATMK IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK
YYILLHIMLG EILRHSMDPP TFTSNFNNEL WVRGRHETYL CYEVERLHND TWVLLNQRRG
FLCNQAPHKH GFLEGRHAEL CFLDVIPFWK LDLHQDYRVT CFTSWSPCFS CAQEMAKFIS
NNKHVSLCIF AARIYDDQGR CQEGLRTLAK AGAKISIMTY SEFKHCWDTF VDHQGCPFQP
WDGLEEHSQA LSGRLRAILQ NQGN
