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DNA dC->dU-editing enzyme APOBEC-3G (EC 3.5.4.-) (Deoxycytidine deaminase)

 ABC3G_PANTR             Reviewed;         384 AA.
Q7YR24; Q694C3;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 2.
20-DEC-2017, entry version 79.
RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G;
EC=3.5.4.-;
AltName: Full=Deoxycytidine deaminase;
Name=APOBEC3G;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15269786; DOI=10.1371/journal.pbio.0020275;
Sawyer S.L., Emerman M., Malik H.S.;
"Ancient adaptive evolution of the primate antiviral DNA-editing
enzyme APOBEC3G.";
PLoS Biol. 2:1278-1285(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-378, FUNCTION IN DNA C TO U EDITING,
AND SPECIES-SPECIFIC RESTRICTION TO HIV-1 INFECTION.
PubMed=12859895; DOI=10.1016/S0092-8674(03)00515-4;
Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R.,
Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.;
"Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.";
Cell 114:21-31(2003).
[3]
FUNCTION IN SFV RESTRICTION.
PubMed=16378963; DOI=10.1128/JVI.80.2.605-614.2006;
Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A.,
Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O.;
"Restriction of foamy viruses by APOBEC cytidine deaminases.";
J. Virol. 80:605-614(2006).
[4]
REVIEW.
PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350;
Chiu Y.L., Greene W.C.;
"The APOBEC3 cytidine deaminases: an innate defensive network opposing
exogenous retroviruses and endogenous retroelements.";
Annu. Rev. Immunol. 26:317-353(2008).
-!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an
inhibitor of retrovirus replication and retrotransposon mobility
via deaminase-dependent and -independent mechanisms. Exhibits
antiviral activity against vif-deficient: HIV-1 and simian
immunodeficiency viruses (SIVs) and also against simian foamy
virus (SFV). After the penetration of retroviral nucleocapsids
into target cells of infection and the initiation of reverse
transcription, it can induce the conversion of cytosine to uracil
in the minus-sense single-strand viral DNA, leading to G-to-A
hypermutations in the subsequent plus-strand viral DNA. The
resultant detrimental levels of mutations in the proviral genome,
along with a deamination-independent mechanism that works prior to
the proviral integration, together exert efficient antiretroviral
effects in infected target cells. Selectively targets single-
stranded DNA and does not deaminate double-stranded DNA or
single- or double-stranded RNA. May inhibit the mobility of LTR
retrotransposons. {ECO:0000269|PubMed:12859895,
ECO:0000269|PubMed:16378963}.
-!- CATALYTIC ACTIVITY: 2'-deoxycytidine in single-stranded DNA +
H(2)O = 2'-deoxyuridine in single-stranded DNA + NH(3).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Assembly into ribonucleoprotein complexes of
high-molecular-mass (HMM) inhibits its enzymatic activity.
Antiviral activity is neutralized by the HIV-1 virion infectivity
factor (VIF) and simian immunodeficiency virus (SIV-cpz) VIF, that
prevents its incorporation into progeny virions by both inhibiting
its translation and/or by inducing its ubiquitination and
subsequent degradation by the 26S proteasome (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Homodimer. Homooligomer. Can bind RNA to form
ribonucleoprotein complexes of high-molecular-mass (HMM) or low-
molecular-mass (LMM). HMM is inactive and heterogeneous in protein
composition because of binding nonselectively to cellular RNAs,
which in turn are associated with variety of cellular proteins.
The LMM form which is enzymatically active has few or no RNAs
associated. Its ability to form homooligomer is distinct from its
ability to assemble into HMM. Interacts with APOBEC3B, APOBEC3F,
MOV10, AGO2, EIF4E, EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent
manner. Interacts with AGO1, AGO3 and PKA/PRKACA (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Note=Mainly
cytoplasmic, small amount are found in the nucleus. {ECO:0000250}.
-!- DOMAIN: The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-
dependent oligomerization and virion incorporation whereas the
CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase
activity and substrate sequence specificity. {ECO:0000250}.
-!- MISCELLANEOUS: Accumulation of APOBEC3G induced non-lethal
hypermutation could contribute to the genetic variation of primate
lentiviral populations.
-!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY622537; AAT44392.1; -; Genomic_DNA.
EMBL; AY622530; AAT44392.1; JOINED; Genomic_DNA.
EMBL; AY622531; AAT44392.1; JOINED; Genomic_DNA.
EMBL; AY622532; AAT44392.1; JOINED; Genomic_DNA.
EMBL; AY622533; AAT44392.1; JOINED; Genomic_DNA.
EMBL; AY622534; AAT44392.1; JOINED; Genomic_DNA.
EMBL; AY622535; AAT44392.1; JOINED; Genomic_DNA.
EMBL; AY622536; AAT44392.1; JOINED; Genomic_DNA.
EMBL; AY331715; AAP85255.1; -; mRNA.
UniGene; Ptr.6261; -.
ProteinModelPortal; Q7YR24; -.
SMR; Q7YR24; -.
STRING; 9598.ENSPTRP00000024786; -.
PaxDb; Q7YR24; -.
eggNOG; ENOG410JBA1; Eukaryota.
eggNOG; ENOG41119MS; LUCA.
HOGENOM; HOG000033755; -.
HOVERGEN; HBG050434; -.
InParanoid; Q7YR24; -.
Proteomes; UP000002277; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0047844; F:deoxycytidine deaminase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009972; P:cytidine deamination; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0070383; P:DNA cytosine deamination; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
InterPro; IPR013158; APOBEC_N.
InterPro; IPR002125; CMP_dCMP_dom.
InterPro; IPR016193; Cytidine_deaminase-like.
Pfam; PF08210; APOBEC_N; 2.
SUPFAM; SSF53927; SSF53927; 1.
PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
1: Evidence at protein level;
Antiviral defense; Complete proteome; Cytoplasm; Hydrolase; Immunity;
Innate immunity; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Zinc.
CHAIN 1 384 DNA dC->dU-editing enzyme APOBEC-3G.
/FTId=PRO_0000171767.
DOMAIN 29 138 CMP/dCMP-type deaminase 1.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
DOMAIN 214 328 CMP/dCMP-type deaminase 2.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
REGION 1 60 Essential for cytoplasmic localization.
{ECO:0000250}.
REGION 209 336 Necessary for homooligomerization.
{ECO:0000250}.
REGION 213 215 Interaction with DNA. {ECO:0000250}.
REGION 313 320 Interaction with DNA. {ECO:0000250}.
ACT_SITE 259 259 Proton donor. {ECO:0000250}.
METAL 65 65 Zinc. {ECO:0000250}.
METAL 97 97 Zinc. {ECO:0000250}.
METAL 100 100 Zinc. {ECO:0000250}.
METAL 257 257 Zinc; catalytic. {ECO:0000250}.
METAL 288 288 Zinc; catalytic. {ECO:0000250}.
METAL 291 291 Zinc; catalytic. {ECO:0000250}.
SITE 244 244 Interaction with DNA. {ECO:0000250}.
MOD_RES 32 32 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:Q9HC16}.
MOD_RES 218 218 Phosphothreonine; by PKA and CAMK2.
{ECO:0000250|UniProtKB:Q9HC16}.
CONFLICT 4 4 H -> Q (in Ref. 2; AAP85255).
{ECO:0000305}.
CONFLICT 373 373 G -> E (in Ref. 2; AAP85255).
{ECO:0000305}.
CONFLICT 376 376 R -> Q (in Ref. 2; AAP85255).
{ECO:0000305}.
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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