ID ABC3G_MACMU Reviewed; 370 AA.
AC Q7YR23;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 105.
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;
DE Flags: Fragment;
GN Name=APOBEC3G;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [2]
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).
RN [3]
RP FUNCTION IN HIV-1 RESTRICTION, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
RX PubMed=21835787; DOI=10.1128/jvi.05238-11;
RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L.,
RA Brown W.L., Harris R.S.;
RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a
RT conserved capacity to restrict Vif-deficient HIV-1.";
RL J. Virol. 85:11220-11234(2011).
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
CC (SIVs). After the penetration of retroviral nucleocapsids into target
CC cells of infection and the initiation of reverse transcription, it can
CC induce the conversion of cytosine to uracil in the minus-sense single-
CC strand viral DNA, leading to G-to-A hypermutations in the subsequent
CC plus-strand viral DNA. The resultant detrimental levels of mutations in
CC the proviral genome, along with a deamination-independent mechanism
CC that 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. May inhibit the mobility of LTR
CC retrotransposons. {ECO:0000269|PubMed:12859895,
CC ECO:0000269|PubMed:21835787}.
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 simian immunodeficiency virus (SIV-mac)
CC virion infectivity factor (VIF), that prevents its incorporation into
CC progeny virions by both inhibiting its translation and/or by inducing
CC its ubiquitination and subsequent degradation by the 26S proteasome.
CC {ECO:0000269|PubMed:21835787}.
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:0000269|PubMed:21835787}. Nucleus
CC {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Note=Mainly
CC cytoplasmic, small amount are found in the nucleus.
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; AY331716; AAP85256.1; -; mRNA.
DR PDB; 8E40; EM; 3.57 A; A=1-370.
DR PDB; 8EDJ; X-ray; 1.83 A; A=1-370.
DR PDBsum; 8E40; -.
DR PDBsum; 8EDJ; -.
DR AlphaFoldDB; Q7YR23; -.
DR SMR; Q7YR23; -.
DR STRING; 9544.ENSMMUP00000069989; -.
DR PaxDb; 9544-ENSMMUP00000005357; -.
DR eggNOG; KOG4075; Eukaryota.
DR InParanoid; Q7YR23; -.
DR Proteomes; UP000006718; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IDA: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; IDA: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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Hydrolase; Immunity;
KW Innate immunity; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN <1..>370
FT /note="DNA dC->dU-editing enzyme APOBEC-3G"
FT /id="PRO_0000171764"
FT DOMAIN 22..131
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 207..320
FT /note="CMP/dCMP-type deaminase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION <1..61
FT /note="Essential for cytoplasmic localization"
FT REGION 202..328
FT /note="Necessary for homooligomerization"
FT /evidence="ECO:0000250"
FT REGION 305..312
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 252
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT SITE 237
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9HC16"
FT MOD_RES 211
FT /note="Phosphothreonine; by PKA and CAMK2"
FT /evidence="ECO:0000250|UniProtKB:Q9HC16"
FT NON_TER 1
FT NON_TER 370
SQ SEQUENCE 370 AA; 43614 MW; 16FBE5A9AFB57B90 CRC64;
MVEPMDPRTF VSNFNNRPIL SGLNTVWLCC EVKTKDPSGP PLDAKIFQGK VYSKAKYHPE
MRFLRWFHKW RQLHHDQEYK VTWYVSWSPC TRCANSVATF LAKDPKVTLT IFVARLYYFW
KPDYQQALRI LCQKRGGPHA TMKIMNYNEF QDCWNKFVDG RGKPFKPRNN LPKHYTLLQA
TLGELLRHLM DPGTFTSNFN NKPWVSGQHE TYLCYKVERL HNDTWVPLNQ HRGFLRNQAP
NIHGFPKGRH AELCFLDLIP FWKLDGQQYR VTCFTSWSPC FSCAQEMAKF ISNNEHVSLC
IFAARIYDDQ GRYQEGLRAL HRDGAKIAMM NYSEFEYCWD TFVDRQGRPF QPWDGLDEHS
QALSGRLRAI
//
