ABC3G_PONPY
ID ABC3G_PONPY Reviewed; 384 AA.
AC Q694C0; Q6DVP9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15198990; DOI=10.1093/hmg/ddh183;
RA Zhang J., Webb D.M.;
RT "Rapid evolution of primate antiviral enzyme APOBEC3G.";
RL Hum. Mol. Genet. 13:1785-1791(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. {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; AY622561; AAT44395.1; -; Genomic_DNA.
DR EMBL; AY622554; AAT44395.1; JOINED; Genomic_DNA.
DR EMBL; AY622555; AAT44395.1; JOINED; Genomic_DNA.
DR EMBL; AY622556; AAT44395.1; JOINED; Genomic_DNA.
DR EMBL; AY622557; AAT44395.1; JOINED; Genomic_DNA.
DR EMBL; AY622558; AAT44395.1; JOINED; Genomic_DNA.
DR EMBL; AY622559; AAT44395.1; JOINED; Genomic_DNA.
DR EMBL; AY622560; AAT44395.1; JOINED; Genomic_DNA.
DR EMBL; AY639869; AAT72158.1; -; mRNA.
DR AlphaFoldDB; Q694C0; -.
DR SMR; Q694C0; -.
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; 1.
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; Cytoplasm; Hydrolase; Immunity; Innate immunity;
KW Metal-binding; Nucleus; Phosphoprotein; Repeat; Zinc.
FT CHAIN 1..384
FT /note="DNA dC->dU-editing enzyme APOBEC-3G"
FT /id="PRO_0000171769"
FT DOMAIN 29..138
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 214..328
FT /note="CMP/dCMP-type deaminase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 1..60
FT /note="Essential for cytoplasmic localization"
FT /evidence="ECO:0000250"
FT REGION 209..336
FT /note="Necessary for homooligomerization"
FT /evidence="ECO:0000250"
FT REGION 313..320
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 259
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 257
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 BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT SITE 244
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9HC16"
FT MOD_RES 218
FT /note="Phosphothreonine; by PKA and CAMK2"
FT /evidence="ECO:0000250|UniProtKB:Q9HC16"
FT CONFLICT 2
FT /note="N -> K (in Ref. 2; AAT72158)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="K -> T (in Ref. 2; AAT72158)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="Q -> R (in Ref. 2; AAT72158)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="C -> W (in Ref. 2; AAT72158)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="D -> S (in Ref. 2; AAT72158)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="L -> Q (in Ref. 2; AAT72158)"
FT /evidence="ECO:0000305"
FT CONFLICT 362..365
FT /note="IRLH -> DGLE (in Ref. 2; AAT72158)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="L -> W (in Ref. 2; AAT72158)"
FT /evidence="ECO:0000305"
FT CONFLICT 374..376
FT /note="RLR -> KLQ (in Ref. 2; AAT72158)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="L -> Q (in Ref. 2; AAT72158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 46078 MW; 6B151DA99FCC8A59 CRC64;
MNPQFRNMVD GMDPHKFSYN FKNRPILSRR NTVWLCYEVK TKGPSRPPLD AKIFRGQVYF
ELKNHPEMRF FHWFSKWRKL HRDQECEVTW YMSWSPCTKC TRNVATFLAE DPKVTLTIFV
ARLYYFWDPD YQEALRSLCQ ERDGPRANMK IMNYDEFQHC WNKFVYSQRE LFEPWNNLPK
YYIVLHIILG EILRHSMDPL TFTSNFNNEP CVEGRHETYL CYKVERLHND TWVLLNQRRG
FLCNQAPAIH GFPEGRHAEL CFLDVIPFWK LDGKQRYRVT CFTSWSPCFR CAQEMAKFIS
NNQHVSLCIF AARIYDDQGR CKEGLRTLDE AEAKISIMTY DEFQHCWDTF VDHQGRPFLP
WIRLHEHSEA LSGRLRAILL NQGN
