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 27-MAR-2024, entry version 202. 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 PDB; 7UXD; X-ray; 1.50 A; A=191-384. DR PDB; 8CX0; EM; 2.70 A; A=1-384. DR PDB; 8CX1; EM; 3.30 A; A/F=1-384. DR PDB; 8CX2; EM; 3.20 A; A/F=1-384. DR PDB; 8H0I; EM; 2.80 A; A/B=11-384. DR PDB; 8J62; EM; 2.50 A; A/B=11-384. 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 PDBsum; 7UXD; -. DR PDBsum; 8CX0; -. DR PDBsum; 8CX1; -. DR PDBsum; 8CX2; -. DR PDBsum; 8H0I; -. DR PDBsum; 8J62; -. DR AlphaFoldDB; Q9HC16; -. DR EMDB; EMD-34412; -. DR EMDB; EMD-35999; -. DR SASBDB; Q9HC16; -. DR SMR; Q9HC16; -. DR BioGRID; 121920; 28. 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 SwissPalm; Q9HC16; -. DR BioMuta; APOBEC3G; -. DR DMDM; 44887683; -. DR EPD; Q9HC16; -. DR jPOST; Q9HC16; -. DR MassIVE; Q9HC16; -. DR MaxQB; Q9HC16; -. DR PaxDb; 9606-ENSP00000385057; -. DR PeptideAtlas; Q9HC16; -. DR ProteomicsDB; 81623; -. [Q9HC16-1] DR ProteomicsDB; 81624; -. [Q9HC16-3] DR Pumba; Q9HC16; -. DR Antibodypedia; 34782; 671 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 AGR; HGNC:17357; -. 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 InParanoid; Q9HC16; -. DR OMA; FLCNQAP; -. DR OrthoDB; 5355962at2759; -. 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; 17 hits in 1171 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 188 other cell types or tissues. 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: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 GO; GO:0010526; P:retrotransposon silencing; IDA:UniProtKB. 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; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2. DR Genevisible; Q9HC16; HS. 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 10..12 FT /evidence="ECO:0007829|PDB:8CX1" FT HELIX 14..20 FT /evidence="ECO:0007829|PDB:8CX0" FT STRAND 32..44 FT /evidence="ECO:0007829|PDB:8CX0" FT STRAND 49..57 FT /evidence="ECO:0007829|PDB:8CX0" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:8CX0" FT HELIX 66..77 FT /evidence="ECO:0007829|PDB:8CX0" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:8CX0" FT STRAND 86..94 FT /evidence="ECO:0007829|PDB:8CX0" FT HELIX 98..110 FT /evidence="ECO:0007829|PDB:8CX0" FT STRAND 112..122 FT /evidence="ECO:0007829|PDB:8CX0" FT TURN 124..127 FT /evidence="ECO:0007829|PDB:8CX0" FT HELIX 129..138 FT /evidence="ECO:0007829|PDB:8CX0" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:8CX2" FT STRAND 147..151 FT /evidence="ECO:0007829|PDB:8CX0" FT HELIX 154..164 FT /evidence="ECO:0007829|PDB:8CX0" FT HELIX 178..193 FT /evidence="ECO:0007829|PDB:8CX0" 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 249..251 FT /evidence="ECO:0007829|PDB:8CX0" 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 //