ID Q09GI9_MACMU Unreviewed; 341 AA.
AC Q09GI9;
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:ABI63653.1};
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:ABI63653.1};
RN [1] {ECO:0000313|EMBL:ABI63653.1}
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; DQ913655; ABI63653.1; -; 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:ABI63653.1};
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 1..107
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT DOMAIN 183..296
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABI63653.1"
FT NON_TER 341
FT /evidence="ECO:0000313|EMBL:ABI63653.1"
SQ SEQUENCE 341 AA; 40289 MW; 45FADC5C02045D0F CRC64;
VWLCCEVKTK DPSGPPLDAK IFQGKVLRSK AKYHPEMRFL QWFREWRQLH HDQEYKVTWY
VSWSPCTRCA NSVATFLAKD PKVTLTIFVA RLYYFWKPNY QQALRILCQK RDGPHATMKI
MNYNEFQDCW NKFVDGRGKP FKPWNNLPKH YTLLQATLGE LLRHLMDPGT FTSNFNNKPW
VSGQHETYLC YKVERLHNDT WVPLNQHRGF LRNQAPNIHG FPKGRHAELC FLDLIPFWKL
DGQQYRVTCF TSWSPCFSCA QEMAKFISNN EHVSLCIFAA RIYDDQGRYQ EGLRTLHRDG
AKIAMMNYSE FEYCWDTFVD XQGCPFQPWD GLDEHSQALS G
//
