ID Q05JX5_HUMAN Unreviewed; 384 AA.
AC Q05JX5;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 71.
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};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAF34652.1};
RN [1] {ECO:0000313|EMBL:BAF34652.1}
RP NUCLEOTIDE SEQUENCE.
RA Kamada K., Igarashi T., Martin, M A., Khamsri B., Hatcho K., Yamashita T.,
RA Fujita M., Uchiyama T., Adachi A.;
RT "Generation of HIV-1 derivatives that productively infect macaque monkey
RT lymphoid cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16959-16964(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; AB266487; BAF34652.1; -; mRNA.
DR AlphaFoldDB; Q05JX5; -.
DR PeptideAtlas; Q05JX5; -.
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:BAF34652.1};
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 29..138
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT DOMAIN 214..328
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 384 AA; 46483 MW; EA6A0AD6C68E0BD2 CRC64;
MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPPLD AKIFRGQVYS
ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC TRDMATFLAE DPKVTLTIFV
ARLYYFWDPD YQEALRSLCQ KRDGPRATMK IMNYDEFQHC WNKFVYSQRE LFEPWNNLPK
YYILLHIMLG EILRHSMDPP TFTFNFNNEP WVRGRHETYL CYEVERMHND TWVLLNQRRG
FLCNQAPHKH GFLEGRHAEL CFLDVIPFWK LDLDQDYRVT CFTSWSPCFS CAQEMAKFIS
KNKHVSLCIF TARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF VDHQGCPFQP
WDGLDEHSQY LSGRLRAILQ NQEN
//
