ABC3G_LAGLA
ID ABC3G_LAGLA Reviewed; 381 AA.
AC Q694B8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G {ECO:0000250|UniProtKB:Q9HC16};
DE EC=3.5.4.38 {ECO:0000250|UniProtKB:Q9HC16};
DE AltName: Full=Deoxycytidine deaminase;
GN Name=APOBEC3G;
OS Lagothrix lagotricha (Brown woolly monkey) (Humboldt's woolly monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Atelidae;
OC Atelinae; Lagothrix.
OX NCBI_TaxID=9519;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15269786; DOI=10.1371/journal.pbio.0020275;
RA Sawyer S.L., Emerman M., Malik H.S.;
RT "Ancient adaptive evolution of the primate antiviral DNA-editing enzyme
RT APOBEC3G.";
RL PLoS Biol. 2:1278-1285(2004).
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 (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q9HC16};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9HC16};
CC -!- ACTIVITY REGULATION: Assembly into ribonucleoprotein complexes of high-
CC molecular-mass (HMM) inhibits its enzymatic activity. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Homooligomer. Can bind RNA to form
CC ribonucleoprotein complexes of high-molecular-mass (HMM) or low-
CC molecular-mass (LMM). HMM is inactive and heterogeneous in protein
CC composition because of binding nonselectively to cellular RNAs, which
CC in turn are associated with variety of cellular proteins. The LMM form
CC which is enzymatically active has few or no RNAs associated. Its
CC ability to form homooligomer is distinct from its ability to assemble
CC into HMM. Interacts with APOBEC3B, APOBEC3F, MOV10, AGO2, EIF4E,
CC EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent manner. Interacts with
CC AGO1, AGO3 and PKA/PRKACA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, P-body {ECO:0000250}. Note=Mainly cytoplasmic, small amount
CC are found in the nucleus. {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AY622577; AAT44397.1; -; Genomic_DNA.
DR EMBL; AY622570; AAT44397.1; JOINED; Genomic_DNA.
DR EMBL; AY622571; AAT44397.1; JOINED; Genomic_DNA.
DR EMBL; AY622572; AAT44397.1; JOINED; Genomic_DNA.
DR EMBL; AY622573; AAT44397.1; JOINED; Genomic_DNA.
DR EMBL; AY622574; AAT44397.1; JOINED; Genomic_DNA.
DR EMBL; AY622575; AAT44397.1; JOINED; Genomic_DNA.
DR EMBL; AY622576; AAT44397.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q694B8; -.
DR SMR; Q694B8; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:InterPro.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016553; P:base conversion or substitution editing; IEA:InterPro.
DR GO; GO:0009972; P:cytidine deamination; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0070383; P:DNA cytosine deamination; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR040551; APOBEC3G.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR PANTHER; PTHR13857:SF20; PTHR13857:SF20; 1.
DR SUPFAM; SSF53927; SSF53927; 2.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 2.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 3: Inferred from homology;
KW Antiviral defense; Cytoplasm; Hydrolase; Immunity; Innate immunity;
KW Metal-binding; Nucleus; Phosphoprotein; Repeat; Zinc.
FT CHAIN 1..381
FT /note="DNA dC->dU-editing enzyme APOBEC-3G"
FT /id="PRO_0000171762"
FT DOMAIN 29..143
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 211..325
FT /note="CMP/dCMP-type deaminase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 1..62
FT /note="Essential for cytoplasmic localization"
FT /evidence="ECO:0000250"
FT REGION 206..333
FT /note="Necessary for homooligomerization"
FT /evidence="ECO:0000250"
FT REGION 310..317
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT SITE 241
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9HC16"
SQ SEQUENCE 381 AA; 45164 MW; 3205FFA79F37E6DE CRC64;
MKPQTRNTVV RMDPDTFFYN FYNRPILSHR NTVWLCYEVK MKTNDPSRPP LVANIFQGQV
SFNPEHHAEM YFLSWFRGNL LPACKRSQIT WFVSWNPCLY CVAKVAEFLA EHPKVTLTVS
TARLYCYRKK DWRRALRKLS QTGARVKIMD YEEFQHCWDN FVDNQREPFE PWNALPKHYT
LLRITLGEVL RHRMDPVTFT YNFTNDPSVL GQHQSYLCYK VEHLRNGTWV PLHQHRGFIL
NEASNSVSFP EGRHAELCLL DLISFWKLKQ AQRYRVTCFI SWSPCFSCAE KVAEFLQENP
HVNLHISAAR IYDYQRGYKK GLRRLDRAGT PISMMKYSEF KHCWDTFVDH QGHPFQPWEE
LNEHSQALSG RLQAILQNQG N
