ABC3G_HUMAN
ID ABC3G_HUMAN Reviewed; 384 AA.
AC Q9HC16; B2RDR9; Q45F02; Q5TF77; Q7Z2N1; Q7Z2N4; Q9H9H8;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G;
DE EC=3.5.4.38 {ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:18288108, ECO:0000269|PubMed:18849968, ECO:0000269|PubMed:19153609};
DE AltName: Full=APOBEC-related cytidine deaminase;
DE Short=APOBEC-related protein;
DE Short=ARCD;
DE AltName: Full=APOBEC-related protein 9;
DE Short=ARP-9;
DE AltName: Full=CEM-15;
DE Short=CEM15;
DE AltName: Full=Deoxycytidine deaminase;
DE Short=A3G;
GN Name=APOBEC3G; ORFNames=MDS019;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN HIV-1 INFECTION
RP INHIBITION.
RC TISSUE=Kidney;
RX PubMed=14557625; DOI=10.1128/jvi.77.21.11398-11407.2003;
RA Kao S., Khan M.A., Miyagi E., Plishka R., Buckler-White A., Strebel K.;
RT "The human immunodeficiency virus type 1 Vif protein reduces intracellular
RT expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor
RT of virus infectivity.";
RL J. Virol. 77:11398-11407(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Synovium, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-186 AND GLU-275.
RG SeattleSNPs program for genomic applications;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP GENE FAMILY ORGANIZATION, TISSUE SPECIFICITY, SUBUNIT, RNA-BINDING, AND
RP ZINC-BINDING.
RX PubMed=11863358; DOI=10.1006/geno.2002.6718;
RA Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J.,
RA Navaratnam N.;
RT "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on
RT chromosome 22.";
RL Genomics 79:285-296(2002).
RN [10]
RP TISSUE SPECIFICITY, AND FUNCTION IN HIV-1 INFECTION INHIBITION.
RC TISSUE=T-cell lymphoma;
RX PubMed=12167863; DOI=10.1038/nature00939;
RA Sheehy A.M., Gaddis N.C., Choi J.D., Malim M.H.;
RT "Isolation of a human gene that inhibits HIV-1 infection and is suppressed
RT by the viral Vif protein.";
RL Nature 418:646-650(2002).
RN [11]
RP SUBCELLULAR LOCATION, FUNCTION IN DNA C TO U EDITING, AND MUTAGENESIS OF
RP GLU-67; HIS-81; GLU-85; CYS-97; CYS-100; CYS-221; HIS-257; GLU-259;
RP CYS-288; CYS-291 AND GLU-323.
RX PubMed=12808466; DOI=10.1038/nature01709;
RA Mangeat B., Turelli P., Caron G., Friedli M., Perrin L., Trono D.;
RT "Broad antiretroviral defence by human APOBEC3G through lethal editing of
RT nascent reverse transcripts.";
RL Nature 424:99-103(2003).
RN [12]
RP FUNCTION IN DNA C TO U EDITING, AND MLV INFECTION INHIBITION.
RX PubMed=12809610; DOI=10.1016/s0092-8674(03)00423-9;
RA Harris R.S., Bishop K.N., Sheehy A.M., Craig H.M., Petersen-Mahrt S.K.,
RA Watt I.N., Neuberger M.S., Malim M.H.;
RT "DNA deamination mediates innate immunity to retroviral infection.";
RL Cell 113:803-809(2003).
RN [13]
RP FUNCTION IN DNA C TO U EDITING, CATALYTIC ACTIVITY, COFACTOR, AND
RP MUTAGENESIS OF HIS-81; CYS-97; CYS-100; HIS-257; CYS-288 AND CYS-291.
RX PubMed=12808465; DOI=10.1038/nature01707;
RA Zhang H., Yang B., Pomerantz R.J., Zhang C., Arunachalam S.C., Gao L.;
RT "The cytidine deaminase CEM15 induces hypermutation in newly synthesized
RT HIV-1 DNA.";
RL Nature 424:94-98(2003).
RN [14]
RP FUNCTION IN DNA C TO U EDITING, AND INTERACTION WITH HIV-1 PROTEIN VIF
RP (MICROBIAL INFECTION).
RX PubMed=12859895; DOI=10.1016/s0092-8674(03)00515-4;
RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B.,
RA Muenk C., Nymark-McMahon H., Landau N.R.;
RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.";
RL Cell 114:21-31(2003).
RN [15]
RP FUNCTION IN DNA C TO U EDITING, INFECTION REGULATION OF HIV-1, AND
RP MUTAGENESIS OF GLU-67; CYS-100; GLU-259 AND CYS-291.
RC TISSUE=T-cell lymphoma;
RX PubMed=12970355; DOI=10.1074/jbc.c300376200;
RA Shindo K., Takaori-Kondo A., Kobayashi M., Abudu A., Fukunaga K.,
RA Uchiyama T.;
RT "The enzymatic activity of CEM15/Apobec-3G is essential for the regulation
RT of the infectivity of HIV-1 virion but not a sole determinant of its
RT antiviral activity.";
RL J. Biol. Chem. 278:44412-44416(2003).
RN [16]
RP INTERACTION WITH HIV-1 PROTEIN VIF (MICROBIAL INFECTION), PROTEASOME
RP MEDIATED DEGRADATION, AND TRANSLATION INHIBITION.
RX PubMed=14527406; DOI=10.1016/s1097-2765(03)00353-8;
RA Stopak K., de Noronha C., Yonemoto W., Greene W.C.;
RT "HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its
RT translation and intracellular stability.";
RL Mol. Cell 12:591-601(2003).
RN [17]
RP INTERACTION WITH HIV-1 PROTEIN VIF (MICROBIAL INFECTION), AND
RP UBIQUITINATION.
RX PubMed=14528301; DOI=10.1038/nm946;
RA Marin M., Rose K.M., Kozak S.L., Kabat D.;
RT "HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its
RT degradation.";
RL Nat. Med. 9:1398-1403(2003).
RN [18]
RP FUNCTION IN DNA C TO U EDITING, AND UBIQUITINATION.
RX PubMed=14528300; DOI=10.1038/nm945;
RA Sheehy A.M., Gaddis N.C., Malim M.H.;
RT "The antiretroviral enzyme APOBEC3G is degraded by the proteasome in
RT response to HIV-1 Vif.";
RL Nat. Med. 9:1404-1407(2003).
RN [19]
RP REVIEW ON APOBEC FAMILY.
RX PubMed=12683974; DOI=10.1016/s0168-9525(03)00054-4;
RA Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.;
RT "Messenger RNA editing in mammals: new members of the APOBEC family seeking
RT roles in the family business.";
RL Trends Genet. 19:207-216(2003).
RN [20]
RP REVIEW.
RX PubMed=14557052; DOI=10.1016/j.molmed.2003.08.008;
RA Vartanian J.P., Sommer P., Wain-Hobson S.;
RT "Death and the retrovirus.";
RL Trends Mol. Med. 9:409-413(2003).
RN [21]
RP REVIEW.
RX PubMed=14565218; DOI=10.1016/j.ymthe.2003.08.010;
RA Cullen B.R.;
RT "HIV-1 Vif: counteracting innate antiretroviral defenses.";
RL Mol. Ther. 8:525-527(2003).
RN [22]
RP MUTAGENESIS OF ASP-128.
RX PubMed=15054139; DOI=10.1073/pnas.0400830101;
RA Xu H., Svarovskaia E.S., Barr R., Zhang Y., Khan M.A., Strebel K.,
RA Pathak V.K.;
RT "A single amino acid substitution in human APOBEC3G antiretroviral enzyme
RT confers resistance to HIV-1 virion infectivity factor-induced depletion.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5652-5657(2004).
RN [23]
RP FUNCTION IN HBV INHIBITION.
RX PubMed=15031497; DOI=10.1126/science.1092066;
RA Turelli P., Mangeat B., Jost S., Vianin S., Trono D.;
RT "Inhibition of hepatitis B virus replication by APOBEC3G.";
RL Science 303:1829-1829(2004).
RN [24]
RP FUNCTION IN RETROTRANSPOSITION, AND SUBCELLULAR LOCATION.
RX PubMed=16527742; DOI=10.1016/j.cub.2006.01.031;
RA Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., Landau N.R.,
RA Weitzman M.D.;
RT "APOBEC3A is a potent inhibitor of adeno-associated virus and
RT retrotransposons.";
RL Curr. Biol. 16:480-485(2006).
RN [25]
RP DOMAIN CMP/DCMP DEAMINASE, SUBUNIT, AND MUTAGENESIS OF GLU-67 AND GLU-259.
RX PubMed=17020885; DOI=10.1074/jbc.m604980200;
RA Hakata Y., Landau N.R.;
RT "Reversed functional organization of mouse and human APOBEC3 cytidine
RT deaminase domains.";
RL J. Biol. Chem. 281:36624-36631(2006).
RN [26]
RP FUNCTION IN SFV RESTRICTION.
RX PubMed=16378963; DOI=10.1128/jvi.80.2.605-614.2006;
RA Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A.,
RA Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O.;
RT "Restriction of foamy viruses by APOBEC cytidine deaminases.";
RL J. Virol. 80:605-614(2006).
RN [27]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH APOBEC3F; AGO2; EIF4E;
RP EIF4ENIF1; DCP2 AND DDX6.
RX PubMed=16699599; DOI=10.1371/journal.ppat.0020041;
RA Wichroski M.J., Robb G.B., Rana T.M.;
RT "Human retroviral host restriction factors APOBEC3G and APOBEC3F localize
RT to mRNA processing bodies.";
RL PLoS Pathog. 2:E41-E41(2006).
RN [28]
RP REVIEW.
RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350;
RA Chiu Y.L., Greene W.C.;
RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing
RT exogenous retroviruses and endogenous retroelements.";
RL Annu. Rev. Immunol. 26:317-353(2008).
RN [29]
RP REVIEW ON FUNCTION IN HBV RESTRICTION.
RX PubMed=18448976; DOI=10.1097/qco.0b013e3282fe1bb2;
RA Bonvin M., Greeve J.;
RT "Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine deaminases
RT as effectors in innate immunity against the hepatitis B virus.";
RL Curr. Opin. Infect. Dis. 21:298-303(2008).
RN [30]
RP SUBUNIT.
RX PubMed=18842592; DOI=10.1074/jbc.m803726200;
RA Bennett R.P., Salter J.D., Liu X., Wedekind J.E., Smith H.C.;
RT "APOBEC3G subunits self-associate via the C-terminal deaminase domain.";
RL J. Biol. Chem. 283:33329-33336(2008).
RN [31]
RP SUBCELLULAR LOCATION.
RX PubMed=18667511; DOI=10.1128/jvi.02471-07;
RA Stenglein M.D., Matsuo H., Harris R.S.;
RT "Two regions within the amino-terminal half of APOBEC3G cooperate to
RT determine cytoplasmic localization.";
RL J. Virol. 82:9591-9599(2008).
RN [32]
RP PHOSPHORYLATION AT THR-32, AND INTERACTION WITH PRKACA.
RX PubMed=18836454; DOI=10.1038/nsmb.1497;
RA Shirakawa K., Takaori-Kondo A., Yokoyama M., Izumi T., Matsui M., Io K.,
RA Sato T., Sato H., Uchiyama T.;
RT "Phosphorylation of APOBEC3G by protein kinase A regulates its interaction
RT with HIV-1 Vif.";
RL Nat. Struct. Mol. Biol. 15:1184-1191(2008).
RN [33]
RP FUNCTION IN EIAV RESTRICTION.
RX PubMed=19458006; DOI=10.1128/jvi.00015-09;
RA Zielonka J., Bravo I.G., Marino D., Conrad E., Perkovic M., Battenberg M.,
RA Cichutek K., Muenk C.;
RT "Restriction of equine infectious anemia virus by equine APOBEC3 cytidine
RT deaminases.";
RL J. Virol. 83:7547-7559(2009).
RN [34]
RP REVIEW.
RX PubMed=19008196; DOI=10.1098/rstb.2008.0193;
RA Chiu Y.L., Greene W.C.;
RT "APOBEC3G: an intracellular centurion.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 364:689-703(2009).
RN [35]
RP FUNCTION IN HIV-1 RESTRICTION.
RX PubMed=20219927; DOI=10.1128/jvi.02358-09;
RA Mbisa J.L., Bu W., Pathak V.K.;
RT "APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different
RT mechanisms.";
RL J. Virol. 84:5250-5259(2010).
RN [36]
RP FUNCTION IN XMRV RESTRICTION.
RX PubMed=20335265; DOI=10.1128/jvi.00134-10;
RA Paprotka T., Venkatachari N.J., Chaipan C., Burdick R.,
RA Delviks-Frankenberry K.A., Hu W.S., Pathak V.K.;
RT "Inhibition of xenotropic murine leukemia virus-related virus by APOBEC3
RT proteins and antiviral drugs.";
RL J. Virol. 84:5719-5729(2010).
RN [37]
RP TISSUE SPECIFICITY.
RX PubMed=20308164; DOI=10.1093/nar/gkq174;
RA Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L.,
RA Harris R.S.;
RT "Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes
RT and tissues: implications for HIV-1 restriction.";
RL Nucleic Acids Res. 38:4274-4284(2010).
RN [38]
RP INTERACTION WITH HEPATITIS B VIRUS CAPSID PROTEIN (MICROBIAL INFECTION).
RX PubMed=20510315; DOI=10.1016/j.virusres.2010.05.009;
RA Zhao D., Wang X., Lou G., Peng G., Li J., Zhu H., Chen F., Li S., Liu D.,
RA Chen Z., Yang Z.;
RT "APOBEC3G directly binds Hepatitis B virus core protein in cell and cell
RT free systems.";
RL Virus Res. 151:213-219(2010).
RN [39]
RP PHOSPHORYLATION AT THR-32 AND THR-218, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF THR-218.
RX PubMed=21659520; DOI=10.1074/jbc.m111.235721;
RA Demorest Z.L., Li M., Harris R.S.;
RT "Phosphorylation directly regulates the intrinsic DNA cytidine deaminase
RT activity of activation-induced deaminase and APOBEC3G protein.";
RL J. Biol. Chem. 286:26568-26575(2011).
RN [40]
RP FUNCTION IN HOST DEFENSE, AND MUTAGENESIS OF GLU-217 AND PRO-247.
RX PubMed=21123384; DOI=10.1128/jvi.01651-10;
RA Bulliard Y., Narvaiza I., Bertero A., Peddi S., Roehrig U.F., Ortiz M.,
RA Zoete V., Castro-Diaz N., Turelli P., Telenti A., Michielin O.,
RA Weitzman M.D., Trono D.;
RT "Structure-function analyses point to a polynucleotide-accommodating groove
RT essential for APOBEC3A restriction activities.";
RL J. Virol. 85:1765-1776(2011).
RN [41]
RP FUNCTION IN HIV-1 RESTRICTION, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
RX PubMed=21835787; DOI=10.1128/jvi.05238-11;
RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L.,
RA Brown W.L., Harris R.S.;
RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a
RT conserved capacity to restrict Vif-deficient HIV-1.";
RL J. Virol. 85:11220-11234(2011).
RN [42]
RP REVIEW.
RX PubMed=21239176; DOI=10.1016/j.tibs.2010.12.003;
RA Smith H.C.;
RT "APOBEC3G: a double agent in defense.";
RL Trends Biochem. Sci. 36:239-244(2011).
RN [43]
RP DOMAIN CMP/DCMP DEAMINASE.
RX PubMed=21489586; DOI=10.1016/j.virol.2011.03.014;
RA Li X., Ma J., Zhang Q., Zhou J., Yin X., Zhai C., You X., Yu L., Guo F.,
RA Zhao L., Li Z., Zeng Y., Cen S.;
RT "Functional analysis of the two cytidine deaminase domains in APOBEC3G.";
RL Virology 414:130-136(2011).
RN [44]
RP REVIEW.
RX PubMed=22787460; DOI=10.3389/fmicb.2012.00250;
RA Imahashi M., Nakashima M., Iwatani Y.;
RT "Antiviral mechanism and biochemical basis of the human APOBEC3 family.";
RL Front. Microbiol. 3:250-250(2012).
RN [45]
RP REVIEW.
RX PubMed=22912627; DOI=10.3389/fmicb.2012.00275;
RA Arias J.F., Koyama T., Kinomoto M., Tokunaga K.;
RT "Retroelements versus APOBEC3 family members: No great escape from the
RT magnificent seven.";
RL Front. Microbiol. 3:275-275(2012).
RN [46]
RP FUNCTION, AND INTERACTION WITH MOV10.
RX PubMed=22791714; DOI=10.1074/jbc.m112.354001;
RA Liu C., Zhang X., Huang F., Yang B., Li J., Liu B., Luo H., Zhang P.,
RA Zhang H.;
RT "APOBEC3G inhibits microRNA-mediated repression of translation by
RT interfering with the interaction between Argonaute-2 and MOV10.";
RL J. Biol. Chem. 287:29373-29383(2012).
RN [47]
RP INTERACTION WITH HIV-1 REVERSE TRANSCRIPTASE/RIBONUCLEASE H (MICROBIAL
RP INFECTION).
RX PubMed=22301159; DOI=10.1128/jvi.06594-11;
RA Wang X., Ao Z., Chen L., Kobinger G., Peng J., Yao X.;
RT "The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse
RT transcriptase and inhibits its function during viral replication.";
RL J. Virol. 86:3777-3786(2012).
RN [48]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AGO1; AGO2 AND AGO3.
RX PubMed=22915799; DOI=10.1128/jvi.00595-12;
RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.;
RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by P
RT bodies.";
RL J. Virol. 86:11712-11724(2012).
RN [49]
RP INTERACTION WITH HIV-1 VIF, AND MUTAGENESIS OF PHE-74; LEU-80; TYR-86;
RP PHE-107 AND ASP-128.
RX PubMed=23001005; DOI=10.1038/nsmb.2378;
RA Kitamura S., Ode H., Nakashima M., Imahashi M., Naganawa Y., Kurosawa T.,
RA Yokomaku Y., Yamane T., Watanabe N., Suzuki A., Sugiura W., Iwatani Y.;
RT "The APOBEC3C crystal structure and the interface for HIV-1 Vif binding.";
RL Nat. Struct. Mol. Biol. 19:1005-1010(2012).
RN [50]
RP FUNCTION IN HIV-1 RESTRICTION.
RX PubMed=22807680; DOI=10.1371/journal.ppat.1002800;
RA Refsland E.W., Hultquist J.F., Harris R.S.;
RT "Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the
RT nonpermissive T cell line CEM2n.";
RL PLoS Pathog. 8:E1002800-E1002800(2012).
RN [51]
RP REVIEW.
RX PubMed=22546055; DOI=10.1186/1742-4690-9-35;
RA Monajemi M., Woodworth C.F., Benkaroun J., Grant M., Larijani M.;
RT "Emerging complexities of APOBEC3G action on immunity and viral fitness
RT during HIV infection and treatment.";
RL Retrovirology 9:35-35(2012).
RN [52]
RP REVIEW.
RX PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004;
RA Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.;
RT "Functions and regulation of the APOBEC family of proteins.";
RL Semin. Cell Dev. Biol. 23:258-268(2012).
RN [53]
RP FUNCTION IN HIV-1 RESTRICTION.
RX PubMed=23097438; DOI=10.1128/jvi.00676-12;
RA Chaipan C., Smith J.L., Hu W.S., Pathak V.K.;
RT "APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE
RT in human primary CD4+ t cells and macrophages.";
RL J. Virol. 87:444-453(2013).
RN [54]
RP FUNCTION IN HIV-1 RESTRICTION.
RX PubMed=23152537; DOI=10.1128/jvi.02587-12;
RA Gillick K., Pollpeter D., Phalora P., Kim E.Y., Wolinsky S.M., Malim M.H.;
RT "The suppression of HIV-1 infection by APOBEC3 proteins in primary human
RT CD4+ T cells is associated with the inhibition of processive reverse
RT transcription as well as excessive cytidine deamination.";
RL J. Virol. 87:1508-1517(2013).
RN [55]
RP STRUCTURE BY NMR OF 198-384 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY,
RP COFACTOR, FUNCTION, AND MUTAGENESIS OF ARG-213; ARG-215; GLU-259; TRP-285;
RP ARG-313 AND ARG-320.
RX PubMed=18288108; DOI=10.1038/nature06638;
RA Chen K.M., Harjes E., Gross P.J., Fahmy A., Lu Y., Shindo K., Harris R.S.,
RA Matsuo H.;
RT "Structure of the DNA deaminase domain of the HIV-1 restriction factor
RT APOBEC3G.";
RL Nature 452:116-119(2008).
RN [56]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 197-380 IN COMPLEX WITH ZINC,
RP CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF ARG-213; ARG-215; ASN-244;
RP TRP-285 AND TYR-315.
RX PubMed=18849968; DOI=10.1038/nature07357;
RA Holden L.G., Prochnow C., Chang Y.P., Bransteitter R., Chelico L., Sen U.,
RA Stevens R.C., Goodman M.F., Chen X.S.;
RT "Crystal structure of the anti-viral APOBEC3G catalytic domain and
RT functional implications.";
RL Nature 456:121-124(2008).
RN [57]
RP STRUCTURE BY NMR OF 193-384 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RX PubMed=19153609; DOI=10.1038/emboj.2008.290;
RA Furukawa A., Nagata T., Matsugami A., Habu Y., Sugiyama R., Hayashi F.,
RA Kobayashi N., Yokoyama S., Takaku H., Katahira M.;
RT "Structure, interaction and real-time monitoring of the enzymatic reaction
RT of wild-type APOBEC3G.";
RL EMBO J. 28:440-451(2009).
RN [58]
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 191-380.
RX PubMed=22181350; DOI=10.1021/cb200440y;
RA Li M., Shandilya S.M., Carpenter M.A., Rathore A., Brown W.L.,
RA Perkins A.L., Harki D.A., Solberg J., Hook D.J., Pandey K.K., Parniak M.A.,
RA Johnson J.R., Krogan N.J., Somasundaran M., Ali A., Schiffer C.A.,
RA Harris R.S.;
RT "First-in-class small molecule inhibitors of the single-strand DNA cytosine
RT deaminase APOBEC3G.";
RL ACS Chem. Biol. 7:506-517(2012).
CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor
CC of retrovirus replication and retrotransposon mobility via deaminase-
CC dependent and -independent mechanisms. Exhibits potent antiviral
CC activity against Vif-deficient HIV-1. After the penetration of
CC retroviral nucleocapsids into target cells of infection and the
CC initiation of reverse transcription, it can induce the conversion of
CC cytosine to uracil in the minus-sense single-strand viral DNA, leading
CC to G-to-A hypermutations in the subsequent plus-strand viral DNA. The
CC resultant detrimental levels of mutations in the proviral genome, along
CC with a deamination-independent mechanism that works prior to the
CC proviral integration, together exert efficient antiretroviral effects
CC in infected target cells. Selectively targets single-stranded DNA and
CC does not deaminate double-stranded DNA or single- or double-stranded
CC RNA. Exhibits antiviral activity also against simian immunodeficiency
CC viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus
CC (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus
CC (SFV). May inhibit the mobility of LTR and non-LTR retrotransposons.
CC {ECO:0000269|PubMed:12167863, ECO:0000269|PubMed:12808465,
CC ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12809610,
CC ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:12970355,
CC ECO:0000269|PubMed:14528300, ECO:0000269|PubMed:14557625,
CC ECO:0000269|PubMed:15031497, ECO:0000269|PubMed:16378963,
CC ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:18288108,
CC ECO:0000269|PubMed:19458006, ECO:0000269|PubMed:20219927,
CC ECO:0000269|PubMed:20335265, ECO:0000269|PubMed:21123384,
CC ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22791714,
CC ECO:0000269|PubMed:22807680, ECO:0000269|PubMed:22915799,
CC ECO:0000269|PubMed:23097438, ECO:0000269|PubMed:23152537}.
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:0000269|PubMed:12808465, ECO:0000269|PubMed:18288108,
CC ECO:0000269|PubMed:18849968, ECO:0000269|PubMed:19153609};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:18288108,
CC ECO:0000269|PubMed:18849968, ECO:0000269|PubMed:19153609};
CC -!- ACTIVITY REGULATION: Assembly into ribonucleoprotein complexes of high-
CC molecular-mass (HMM) inhibits its enzymatic activity. Antiviral
CC activity is neutralized by the HIV-1 virion infectivity factor (Vif),
CC that prevents its incorporation into progeny HIV-1 virions by both
CC inhibiting its translation and/or by inducing its ubiquitination and
CC subsequent degradation by the 26S proteasome. Can also be neutralized
CC by simian immunodeficiency virus sooty mangabey monkey virus (SIV-sm)
CC and chimpanzee immunodeficiency virus (SIV-cpz) Vif.
CC {ECO:0000269|PubMed:21835787}.
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. {ECO:0000269|PubMed:11863358,
CC ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:17020885,
CC ECO:0000269|PubMed:18288108, ECO:0000269|PubMed:18836454,
CC ECO:0000269|PubMed:18842592, ECO:0000269|PubMed:18849968,
CC ECO:0000269|PubMed:19153609, ECO:0000269|PubMed:22791714,
CC ECO:0000269|PubMed:22915799}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vif.
CC {ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:14527406,
CC ECO:0000269|PubMed:14528301, ECO:0000269|PubMed:23001005}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 reverse
CC transcriptase/ribonuclease H. {ECO:0000269|PubMed:22301159}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus capsid
CC protein. {ECO:0000269|PubMed:20510315}.
CC -!- INTERACTION:
CC Q9HC16; Q9HC16: APOBEC3G; NbExp=2; IntAct=EBI-717839, EBI-717839;
CC Q9HC16; P17612: PRKACA; NbExp=6; IntAct=EBI-717839, EBI-476586;
CC Q9HC16; P69723: vif; Xeno; NbExp=3; IntAct=EBI-717839, EBI-15528966;
CC Q9HC16; Q77YG0: vif; Xeno; NbExp=2; IntAct=EBI-717839, EBI-15731903;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body.
CC Note=Mainly cytoplasmic. Small amount are found in the nucleus. During
CC HIV-1 infection, virion-encapsidated in absence of HIV-1 Vif.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HC16-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9HC16-3; Sequence=VSP_009588, VSP_009589;
CC -!- TISSUE SPECIFICITY: Expressed in spleen, testes, ovary and peripheral
CC blood leukocytes and CD4+ lymphocytes. Also expressed in non-permissive
CC peripheral blood mononuclear cells, and several tumor cell lines; no
CC expression detected in permissive lymphoid and non-lymphoid cell lines.
CC Exists only in the LMM form in peripheral blood-derived resting CD4 T-
CC cells and monocytes, both of which are refractory to HIV-1 infection.
CC LMM is converted to a HMM complex when resting CD4 T-cells are
CC activated or when monocytes are induced to differentiate into
CC macrophages. This change correlates with increased susceptibility of
CC these cells to HIV-1 infection. {ECO:0000269|PubMed:11863358,
CC ECO:0000269|PubMed:12167863, ECO:0000269|PubMed:20308164}.
CC -!- INDUCTION: Up-regulated by IFN-alpha.
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:0000269|PubMed:17020885,
CC ECO:0000269|PubMed:21489586}.
CC -!- PTM: Ubiquitinated in the presence of HIV-1 Vif. Association with Vif
CC targets the protein for proteolysis by the ubiquitin-dependent
CC proteasome pathway. {ECO:0000269|PubMed:14528301}.
CC -!- PTM: Phosphorylation at Thr-32 reduces its binding to HIV-1 Vif and
CC subsequent ubiquitination and degradation thus promoting its antiviral
CC activity. {ECO:0000269|PubMed:18836454, ECO:0000269|PubMed:21659520}.
CC -!- MISCELLANEOUS: Accumulation of APOBEC3G induced non-lethal
CC hypermutation could contribute to the genetic variation of primate
CC lentiviral populations.
CC -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes found in
CC a cluster, thought to result from gene duplication, on chromosome 22.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/apobec3g/";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein wars - Issue 45 of
CC April 2004;
CC URL="https://web.expasy.org/spotlight/back_issues/045";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK022802; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK315650; BAG38016.1; -; mRNA.
DR EMBL; AF182420; AAG14956.1; -; mRNA.
DR EMBL; CR456472; CAG30358.1; -; mRNA.
DR EMBL; DQ147772; AAZ38722.1; -; Genomic_DNA.
DR EMBL; AL022318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL078641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60292.1; -; Genomic_DNA.
DR EMBL; BC024268; AAH24268.1; -; mRNA.
DR EMBL; BC061914; AAH61914.1; -; mRNA.
DR CCDS; CCDS13984.1; -. [Q9HC16-1]
DR RefSeq; NP_068594.1; NM_021822.3. [Q9HC16-1]
DR PDB; 2JYW; NMR; -; A=198-384.
DR PDB; 2KBO; NMR; -; A=193-384.
DR PDB; 2KEM; NMR; -; A=191-384.
DR PDB; 3E1U; X-ray; 2.30 A; A=197-380.
DR PDB; 3IQS; X-ray; 2.30 A; A=197-380.
DR PDB; 3IR2; X-ray; 2.25 A; A/B=191-384.
DR PDB; 3V4J; X-ray; 2.04 A; A/B=191-384.
DR PDB; 3V4K; X-ray; 1.38 A; A/B=191-380.
DR PDB; 4ROV; X-ray; 1.80 A; A/B=193-384.
DR PDB; 4ROW; X-ray; 1.70 A; A=193-384.
DR PDB; 5ZVA; X-ray; 2.30 A; A/B=198-221.
DR PDB; 5ZVB; X-ray; 2.00 A; A/B=198-221.
DR PDB; 6BUX; X-ray; 1.86 A; A=189-384.
DR PDB; 6BWY; X-ray; 2.90 A; A/B/E/G=195-384.
DR PDB; 6K3J; NMR; -; A=197-384.
DR PDB; 6K3K; NMR; -; A=197-384.
DR PDBsum; 2JYW; -.
DR PDBsum; 2KBO; -.
DR PDBsum; 2KEM; -.
DR PDBsum; 3E1U; -.
DR PDBsum; 3IQS; -.
DR PDBsum; 3IR2; -.
DR PDBsum; 3V4J; -.
DR PDBsum; 3V4K; -.
DR PDBsum; 4ROV; -.
DR PDBsum; 4ROW; -.
DR PDBsum; 5ZVA; -.
DR PDBsum; 5ZVB; -.
DR PDBsum; 6BUX; -.
DR PDBsum; 6BWY; -.
DR PDBsum; 6K3J; -.
DR PDBsum; 6K3K; -.
DR AlphaFoldDB; Q9HC16; -.
DR SMR; Q9HC16; -.
DR BioGRID; 121920; 23.
DR DIP; DIP-37519N; -.
DR IntAct; Q9HC16; 11.
DR STRING; 9606.ENSP00000385057; -.
DR BindingDB; Q9HC16; -.
DR ChEMBL; CHEMBL1741217; -.
DR iPTMnet; Q9HC16; -.
DR PhosphoSitePlus; Q9HC16; -.
DR BioMuta; APOBEC3G; -.
DR DMDM; 44887683; -.
DR EPD; Q9HC16; -.
DR jPOST; Q9HC16; -.
DR MassIVE; Q9HC16; -.
DR MaxQB; Q9HC16; -.
DR PaxDb; Q9HC16; -.
DR PeptideAtlas; Q9HC16; -.
DR PRIDE; Q9HC16; -.
DR ProteomicsDB; 81623; -. [Q9HC16-1]
DR ProteomicsDB; 81624; -. [Q9HC16-3]
DR Antibodypedia; 34782; 634 antibodies from 40 providers.
DR DNASU; 60489; -.
DR Ensembl; ENST00000407997.4; ENSP00000385057.3; ENSG00000239713.9. [Q9HC16-1]
DR GeneID; 60489; -.
DR KEGG; hsa:60489; -.
DR MANE-Select; ENST00000407997.4; ENSP00000385057.3; NM_021822.4; NP_068594.1.
DR UCSC; uc003awx.3; human. [Q9HC16-1]
DR CTD; 60489; -.
DR DisGeNET; 60489; -.
DR GeneCards; APOBEC3G; -.
DR HGNC; HGNC:17357; APOBEC3G.
DR HPA; ENSG00000239713; Tissue enhanced (lymphoid).
DR MIM; 607113; gene.
DR neXtProt; NX_Q9HC16; -.
DR OpenTargets; ENSG00000239713; -.
DR PharmGKB; PA24897; -.
DR VEuPathDB; HostDB:ENSG00000239713; -.
DR eggNOG; KOG4075; Eukaryota.
DR GeneTree; ENSGT00940000161999; -.
DR HOGENOM; CLU_047918_0_0_1; -.
DR OMA; GEPFQPW; -.
DR OrthoDB; 586309at2759; -.
DR PhylomeDB; Q9HC16; -.
DR TreeFam; TF331356; -.
DR BRENDA; 3.5.4.38; 2681.
DR BRENDA; 3.5.4.B9; 2681.
DR PathwayCommons; Q9HC16; -.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
DR SignaLink; Q9HC16; -.
DR SIGNOR; Q9HC16; -.
DR BioGRID-ORCS; 60489; 13 hits in 1087 CRISPR screens.
DR ChiTaRS; APOBEC3G; human.
DR EvolutionaryTrace; Q9HC16; -.
DR GeneWiki; APOBEC3G; -.
DR GenomeRNAi; 60489; -.
DR Pharos; Q9HC16; Tchem.
DR PRO; PR:Q9HC16; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9HC16; protein.
DR Bgee; ENSG00000239713; Expressed in granulocyte and 187 other tissues.
DR Genevisible; Q9HC16; HS.
DR GO; GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; TAS:HGNC-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
DR GO; GO:0008829; F:dCTP deaminase activity; TAS:Reactome.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0016553; P:base conversion or substitution editing; TAS:HGNC-UCL.
DR GO; GO:0009972; P:cytidine deamination; IDA:UniProtKB.
DR GO; GO:0016554; P:cytidine to uridine editing; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0070383; P:DNA cytosine deamination; IDA:UniProtKB.
DR GO; GO:0080111; P:DNA demethylation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IDA:HGNC-UCL.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0048525; P:negative regulation of viral process; IDA:HGNC-UCL.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:HGNC-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense; Cytoplasm;
KW Host-virus interaction; Hydrolase; Immunity; Innate immunity;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; Zinc.
FT CHAIN 1..384
FT /note="DNA dC->dU-editing enzyme APOBEC-3G"
FT /id="PRO_0000171761"
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 REGION 209..336
FT /note="Necessary for homooligomerization"
FT REGION 213..215
FT /note="Interaction with DNA"
FT /evidence="ECO:0000305"
FT REGION 313..320
FT /note="Interaction with DNA"
FT /evidence="ECO:0000305"
FT ACT_SITE 259
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18288108,
FT ECO:0000269|PubMed:18849968, ECO:0000269|PubMed:19153609"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18288108,
FT ECO:0000269|PubMed:18849968, ECO:0000269|PubMed:19153609"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18288108,
FT ECO:0000269|PubMed:18849968, ECO:0000269|PubMed:19153609"
FT SITE 244
FT /note="Interaction with DNA"
FT /evidence="ECO:0000305"
FT MOD_RES 32
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:18836454,
FT ECO:0000269|PubMed:21659520"
FT MOD_RES 218
FT /note="Phosphothreonine; by PKA and CAMK2"
FT /evidence="ECO:0000269|PubMed:21659520"
FT VAR_SEQ 58..79
FT /note="VYSELKYHPEMRFFHWFSKWRK -> VPPGLQSLCRQELSQLGKQTTH (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009588"
FT VAR_SEQ 80..384
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009589"
FT VARIANT 186
FT /note="H -> R (in dbSNP:rs8177832)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_017837"
FT VARIANT 256
FT /note="R -> H (in dbSNP:rs17000736)"
FT /id="VAR_048723"
FT VARIANT 275
FT /note="Q -> E (in dbSNP:rs17496046)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025060"
FT MUTAGEN 67
FT /note="E->A: Loss of cytidine deaminase activity and
FT significant decrease in antiviral activity; when associated
FT with A-259."
FT /evidence="ECO:0000269|PubMed:12808466,
FT ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885"
FT MUTAGEN 67
FT /note="E->A: No effect on cytidine deaminase and antiviral
FT activity."
FT /evidence="ECO:0000269|PubMed:12808466,
FT ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885"
FT MUTAGEN 67
FT /note="E->Q: Decreases cytidine deaminase activity."
FT /evidence="ECO:0000269|PubMed:12808466,
FT ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885"
FT MUTAGEN 74
FT /note="F->W: Remains sensitive to HIV-1 Vif and able to
FT bind Vif."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 80
FT /note="L->D: Remains sensitive to HIV-1 Vif and able to
FT bind Vif."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 81
FT /note="H->A: Decreases cytidine deaminase activity."
FT /evidence="ECO:0000269|PubMed:12808465,
FT ECO:0000269|PubMed:12808466"
FT MUTAGEN 85
FT /note="E->Q: Does not decrease cytidine deaminase
FT activity."
FT /evidence="ECO:0000269|PubMed:12808466"
FT MUTAGEN 86
FT /note="Y->A: Remains sensitive to HIV-1 Vif and able to
FT bind Vif."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 97
FT /note="C->A: Decreases cytidine deaminase activity."
FT /evidence="ECO:0000269|PubMed:12808465,
FT ECO:0000269|PubMed:12808466"
FT MUTAGEN 100
FT /note="C->A,S: Decreases cytidine deaminase activity."
FT /evidence="ECO:0000269|PubMed:12808465,
FT ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12970355"
FT MUTAGEN 107
FT /note="F->K: Remains sensitive to HIV-1 Vif and able to
FT bind Vif."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 128
FT /note="D->K: Resistant to HIV-1 Vif with complete loss of
FT Vif-induced degradation and Vif binding."
FT /evidence="ECO:0000269|PubMed:15054139,
FT ECO:0000269|PubMed:23001005"
FT MUTAGEN 213
FT /note="R->A: Slightly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:18288108,
FT ECO:0000269|PubMed:18849968"
FT MUTAGEN 213
FT /note="R->E: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:18288108,
FT ECO:0000269|PubMed:18849968"
FT MUTAGEN 215
FT /note="R->A,E: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18288108,
FT ECO:0000269|PubMed:18849968"
FT MUTAGEN 217
FT /note="E->K: Modifies the spectrum of action against mobile
FT genetic elements; when associated with K-247."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 218
FT /note="T->A: Loss of phosphorylation. No effect on cytidine
FT deaminase activity or HIV-1 restriction activity."
FT /evidence="ECO:0000269|PubMed:21659520"
FT MUTAGEN 218
FT /note="T->E: Phosphomimetic mutant which shows loss of
FT cytidine deaminase activity and HIV-1 restriction
FT activity."
FT /evidence="ECO:0000269|PubMed:21659520"
FT MUTAGEN 221
FT /note="C->S: Does not decrease cytidine deaminase
FT activity."
FT /evidence="ECO:0000269|PubMed:12808466"
FT MUTAGEN 244
FT /note="N->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18849968"
FT MUTAGEN 247
FT /note="P->K: Modifies the spectrum of action against mobile
FT genetic elements; when associated with K-217."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 256
FT /note="R->E: Strongly reduces enzyme activity."
FT MUTAGEN 257
FT /note="H->A: Decreases cytidine deaminase activity."
FT /evidence="ECO:0000269|PubMed:12808465,
FT ECO:0000269|PubMed:12808466"
FT MUTAGEN 259
FT /note="E->A: Loss of cytidine deaminase activity and
FT significant decrease in antiviral activity."
FT /evidence="ECO:0000269|PubMed:12808466,
FT ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885,
FT ECO:0000269|PubMed:18288108"
FT MUTAGEN 259
FT /note="E->A: Loss of cytidine deaminase activity and
FT significant decrease in antiviral activity; when associated
FT with A-67."
FT /evidence="ECO:0000269|PubMed:12808466,
FT ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885,
FT ECO:0000269|PubMed:18288108"
FT MUTAGEN 259
FT /note="E->Q: Decreases cytidine deaminase activity and
FT antiviral activity."
FT /evidence="ECO:0000269|PubMed:12808466,
FT ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885,
FT ECO:0000269|PubMed:18288108"
FT MUTAGEN 285
FT /note="W->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18288108,
FT ECO:0000269|PubMed:18849968"
FT MUTAGEN 288
FT /note="C->A: Decreases cytidine deaminase activity."
FT /evidence="ECO:0000269|PubMed:12808465,
FT ECO:0000269|PubMed:12808466"
FT MUTAGEN 291
FT /note="C->A,S: Decreases cytidine deaminase activity."
FT /evidence="ECO:0000269|PubMed:12808465,
FT ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12970355"
FT MUTAGEN 313
FT /note="R->A,E: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18288108"
FT MUTAGEN 315
FT /note="Y->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18849968"
FT MUTAGEN 320
FT /note="R->A: Slightly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:18288108"
FT MUTAGEN 320
FT /note="R->E: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:18288108"
FT MUTAGEN 323
FT /note="E->Q: Does not decrease cytidine deaminase
FT activity."
FT /evidence="ECO:0000269|PubMed:12808466"
FT CONFLICT 162
FT /note="S -> N (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="D -> Y (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2KBO"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:3V4K"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6K3K"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:2JYW"
FT STRAND 219..228
FT /evidence="ECO:0007829|PDB:3V4K"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3V4K"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:3V4K"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:3V4K"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2JYW"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:3V4K"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:3V4K"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:3E1U"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:3V4K"
FT HELIX 289..301
FT /evidence="ECO:0007829|PDB:3V4K"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:3V4K"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:3V4K"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:3V4K"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:3V4K"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:3V4K"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6K3J"
FT HELIX 364..379
FT /evidence="ECO:0007829|PDB:3V4K"
SQ SEQUENCE 384 AA; 46408 MW; 60525DC3B7D903D6 CRC64;
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
