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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
 
 
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