ID Q09GH2_MACMU Unreviewed; 353 AA.
AC Q09GH2;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G {ECO:0000256|ARBA:ARBA00020239, ECO:0000256|RuleBase:RU367054};
DE EC=3.5.4.- {ECO:0000256|RuleBase:RU367054};
DE AltName: Full=Deoxycytidine deaminase {ECO:0000256|ARBA:ARBA00032972, ECO:0000256|RuleBase:RU367054};
DE Flags: Fragment;
GN Name=APOBEC3G {ECO:0000313|EMBL:ABI63670.1};
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 {ECO:0000313|EMBL:ABI63670.1};
RN [1] {ECO:0000313|EMBL:ABI63670.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17106666; DOI=10.1007/s00251-006-0166-6;
RA Weiler A., May G.E., Qi Y., Wilson N., Watkins D.I.;
RT "Polymorphisms in eight host genes associated with control of HIV
RT replication do not mediate elite control of viral replication in SIV-
RT infected Indian rhesus macaques.";
RL Immunogenetics 58:1003-1009(2006).
CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor
CC of retrovirus replication and retrotransposon mobility. After the
CC penetration of retroviral nucleocapsids into target cells of infection
CC and the initiation of reverse transcription, it can induce the
CC conversion of cytosine to uracil in the minus-sense single-strand viral
CC DNA, leading to G-to-A hypermutations in the subsequent plus-strand
CC viral DNA. The resultant detrimental levels of mutations in the
CC proviral genome, along with a deamination-independent mechanism that
CC 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. {ECO:0000256|RuleBase:RU367054}.
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:0000256|ARBA:ARBA00029350};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU367054};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU367054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201,
CC ECO:0000256|RuleBase:RU367054}. Cytoplasm
CC {ECO:0000256|RuleBase:RU367054}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367054}.
CC Note=Mainly cytoplasmic, small amount are found in the nucleus.
CC {ECO:0000256|RuleBase:RU367054}.
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:0000256|RuleBase:RU367054}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576, ECO:0000256|RuleBase:RU367054}.
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DR EMBL; DQ913672; ABI63670.1; -; mRNA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-UniRule.
DR GO; GO:0070383; P:DNA cytosine deamination; IEA:UniProtKB-UniRule.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-UniRule.
DR GO; GO:0010526; P:retrotransposon silencing; IEA:UniProtKB-UniRule.
DR CDD; cd01283; cytidine_deaminase; 2.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 2.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR PANTHER; PTHR13857:SF20; DNA DC-DU-EDITING ENZYME APOBEC-3G; 1.
DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1.
DR Pfam; PF18782; NAD2; 2.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 2.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 2: Evidence at transcript level;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118,
KW ECO:0000256|RuleBase:RU367054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367054};
KW Hydrolase {ECO:0000256|RuleBase:RU367054};
KW Immunity {ECO:0000256|ARBA:ARBA00022859, ECO:0000256|RuleBase:RU367054};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588,
KW ECO:0000256|RuleBase:RU367054}; Lipoprotein {ECO:0000313|EMBL:ABI63670.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367054};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367054};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU367054};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU367054};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367054}.
FT DOMAIN 9..119
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT DOMAIN 195..308
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABI63670.1"
FT NON_TER 353
FT /evidence="ECO:0000313|EMBL:ABI63670.1"
SQ SEQUENCE 353 AA; 41617 MW; 3F236FD7F52A263F CRC64;
FNNRPILSGL NTVWLCCEVK TKDPSGPPLD AKIFQGKVLR SKAKYHPEMR FLQWFREWRQ
LHHDQEYKVT WYVSWSPCTR CANSVATFLA KDPKVTLTIF VARLYYFWKP NYQQALRILC
QKRDGPHATM KIMNYNEFQD CWNKFVDGRG KPFKPWNNLP KHYTLLQATL GELLRHLMDP
GTFTSNFNNK PWVSGQHETY LCYKVERLHN DTWVPLNQHR GFLRNQAPNI HGFPKGRHAE
LCFLDLIPFW KLDGQQYRVT CFTSWSPCFS CAQEMAKFIS NNEHVSLCIF AARIYDDQGR
YQEGLRTLHR DGAKIAMMNY SEFEYCWDTF VDXQGCPFQP WDGLDEHSQA LSG
//
