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

 ABC3G_MACMU             Reviewed;         370 AA.
Q7YR23;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
30-AUG-2017, entry version 82.
RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G;
EC=3.5.4.-;
AltName: Full=Deoxycytidine deaminase;
Flags: Fragment;
Name=APOBEC3G;
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [MRNA], 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).
[2]
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).
[3]
FUNCTION IN HIV-1 RESTRICTION, SUBCELLULAR LOCATION, AND ENZYME
REGULATION.
PubMed=21835787; DOI=10.1128/JVI.05238-11;
Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L.,
Brown W.L., Harris R.S.;
"Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H
demonstrate a conserved capacity to restrict Vif-deficient HIV-1.";
J. Virol. 85:11220-11234(2011).
-!- 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). 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:21835787}.
-!- CATALYTIC ACTIVITY: Deoxycytidine + H(2)O = deoxyuridine + 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 simian immunodeficiency
virus (SIV-mac) virion infectivity factor (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. {ECO:0000269|PubMed:21835787}.
-!- 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:0000269|PubMed:21835787}.
Nucleus {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}.
Note=Mainly cytoplasmic, small amount are found in the nucleus.
-!- 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; AY331716; AAP85256.1; -; mRNA.
UniGene; Mmu.3692; -.
ProteinModelPortal; Q7YR23; -.
SMR; Q7YR23; -.
STRING; 9544.ENSMMUP00000005357; -.
eggNOG; ENOG410JBA1; Eukaryota.
eggNOG; ENOG41119MS; LUCA.
HOGENOM; HOG000033755; -.
HOVERGEN; HBG050434; -.
InParanoid; Q7YR23; -.
Proteomes; UP000006718; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA: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; IDA:UniProtKB.
GO; GO:0070383; P:DNA cytosine deamination; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB.
GO; GO:0010529; P:negative regulation of transposition; ISS: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; 2.
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 >370 DNA dC->dU-editing enzyme APOBEC-3G.
/FTId=PRO_0000171764.
DOMAIN 22 131 CMP/dCMP-type deaminase 1.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
DOMAIN 207 320 CMP/dCMP-type deaminase 2.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
REGION <1 61 Essential for cytoplasmic localization.
REGION 202 328 Necessary for homooligomerization.
{ECO:0000250}.
REGION 305 312 Interaction with DNA. {ECO:0000250}.
ACT_SITE 252 252 Proton donor. {ECO:0000250}.
METAL 58 58 Zinc. {ECO:0000250}.
METAL 90 90 Zinc. {ECO:0000250}.
METAL 93 93 Zinc. {ECO:0000250}.
METAL 250 250 Zinc; catalytic. {ECO:0000250}.
METAL 280 280 Zinc; catalytic. {ECO:0000250}.
METAL 283 283 Zinc; catalytic. {ECO:0000250}.
SITE 237 237 Interaction with DNA. {ECO:0000250}.
MOD_RES 25 25 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:Q9HC16}.
MOD_RES 211 211 Phosphothreonine; by PKA and CAMK2.
{ECO:0000250|UniProtKB:Q9HC16}.
NON_TER 1 1
NON_TER 370 370
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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