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ABC3G_MACMU
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   03-AUG-2022, entry version 98.
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   AlphaFoldDB; Q7YR23; -.
DR   SMR; Q7YR23; -.
DR   STRING; 9544.ENSMMUP00000005357; -.
DR   eggNOG; KOG4075; Eukaryota.
DR   InParanoid; Q7YR23; -.
DR   Proteomes; UP000006718; Unplaced.
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; 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; IDA:UniProtKB.
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   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..>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
 
 
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