ABC3G_CHLAE
ID ABC3G_CHLAE Reviewed; 377 AA.
AC Q7YR25;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
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 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 [3]
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 simian foamy virus (SFV). After the penetration of retroviral
CC nucleocapsids into target cells of infection and the initiation of
CC reverse transcription, it can induce the conversion of cytosine to
CC uracil in the minus-sense single-strand viral DNA, leading to G-to-A
CC hypermutations in the subsequent plus-strand viral DNA. The resultant
CC detrimental levels of mutations in the proviral genome, along with a
CC deamination-independent mechanism that works prior to the proviral
CC integration, together exert efficient antiretroviral effects in
CC infected target cells. Selectively targets single-stranded DNA and does
CC not deaminate double-stranded DNA or single- or double-stranded RNA.
CC 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 simian immunodeficiency virus (SIV-agm)
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 (By
CC 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; AY331714; AAP85254.1; -; mRNA.
DR AlphaFoldDB; Q7YR25; -.
DR SMR; Q7YR25; -.
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; 2.
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; Repeat; Zinc.
FT CHAIN 1..>377
FT /note="DNA dC->dU-editing enzyme APOBEC-3G"
FT /id="PRO_0000171758"
FT DOMAIN 29..138
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 214..327
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..335
FT /note="Necessary for homooligomerization"
FT /evidence="ECO:0000250"
FT REGION 312..319
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 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 290
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 NON_TER 377
SQ SEQUENCE 377 AA; 44720 MW; C68093826FA89342 CRC64;
MNPQIRNMVE QMEPDIFVYY FNNRPILSGR NTVWLCYEVK TKDPSGPPLD ANIFQGKLYP
EAKDHPEMKF LHWFRKWRQL HRDQEYEVTW YVSWSPCTRC ANSVATFLAE DPKVTLTIFV
ARLYYFWKPD YQQALRILCQ ERGGPHATMK IMNYNEFQHC WNEFVDGQGK PFKPRKNLPK
HYTLLHATLG ELLRHVMDPG TFTSNFNNKP WVSGQRETYL CYKVERSHND TWVLLNQHRG
FLRNQAPDRH GFPKGRHAEL CFLDLIPFWK LDDQQYRVTC FTSWSPCFSC AQKMAKFISN
NKHVSLCIFA ARIYDDQGRC QEGLRTLHRD GAKIAVMNYS EFEYCWDTFV DRQGRPFQPW
DGLDEHSQAL SGRLRAI
