APOBEC3G (GeneName), DNA dC->dU-editing enzyme APOBEC-3G (ProteinName), ABC3G_HUMAN.
Human APOBEC3G/ DNA dC->dU-editing enzyme APOBEC-3G ELISA Kit
APOBEC-related cytidine deaminase, APOBEC-related protein, APOBEC-related protein 9, ARP-9, CEM-15, CEM15, Deoxycytidine deaminase, A3G, MDS019
Natural and recombinant human DNA dC->dU-editing enzyme APOBEC-3G
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Homodimer. Homooligomer. Can bind RNA to form ribonucleoprotein complexes of high-molecular-mass (HMM) or low-molecular-mass (LMM). HMM is inactive and heterogeneous in protein composition because of binding nonselectively to cellular RNAs, which in turn are associated with variety of cellular proteins. The LMM form which is enzymatically active has few or no RNAs associated. Its ability to form homooligomer is distinct from its ability to assemble into HMM. Interacts with APOBEC3B, APOBEC3F, MOV10, AGO2, EIF4E, EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent manner. Interacts with AGO1, AGO3 and PKA/PRKACA. Interacts with HIV-1 VIF and reverse transcriptase/ribonuclease H. Interacts with hepatitis B virus capsid protein.
DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits potent antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV). May inhibit the mobility of LTR and non-LTR retrotransposons.
Cytoplasm Nucleus Cytoplasm P-body Mainly cytoplasmic. Small amount are found in the nucleus. During HIV-1 infection, virion-encapsidated in absence of HIV-1 VIF.
MKPHFRNTVE | RMYRDTFSYN | FYNRPILSRR | NTVWLCYEVK | TKGPSRPPLD |
AKIFRGQVYS | ELKYHPEMRF | FHWFSKWRKL | HRDQEYEVTW | YISWSPCTKC |
TRDMATFLAE | DPKVTLTIFV | ARLYYFWDPD | YQEALRSLCQ | KRDGPRATMK |
IMNYDEFQHC | WSKFVYSQRE | LFEPWNNLPK | YYILLHIMLG | EILRHSMDPP |
TFTFNFNNEP | WVRGRHETYL | CYEVERMHND | TWVLLNQRRG | FLCNQAPHKH |
GFLEGRHAEL | CFLDVIPFWK | LDLDQDYRVT | CFTSWSPCFS | CAQEMAKFIS |
KNKHVSLCIF | TARIYDDQGR | CQEGLRTLAE | AGAKISIMTY | SEFKHCWDTF |
VDHQGCPFQP | WDGLDEHSQD | LSGRLRAILQ | NQEN
This product has not yet been referenced specifically in any publications.
"APOBEC3G expression is dysregulated in primary HIV-1 infection and polymorphic variants influence CD4+ T-cell counts and plasma viral load."
"Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G."
"Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G."
"[The associations between polymorphisms of APOBEC3G and different outcomes of persistent HBV infection]."
"Absence of H186R polymorphism in exon 4 of the APOBEC3G gene among North Indian individuals."
"Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif."
"Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications."
"Restriction of foamy viruses by APOBEC cytidine deaminases."
"Exhaustive genotyping of the CEM15 (APOBEC3G) gene and absence of association with AIDS progression in a French cohort."
"A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion."
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