ID   ABEC3_MOUSE             Reviewed;         429 AA.
AC   Q99J72; Q8C7L0; Q8C8V7;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   07-SEP-2016, entry version 117.
DE   RecName: Full=DNA dC->dU-editing enzyme APOBEC-3;
DE            EC=3.5.4.-;
DE   AltName: Full=Apolipoprotein B mRNA-editing complex 3;
DE            Short=Arp3;
DE   AltName: Full=CEM-15;
DE            Short=CEM15;
GN   Name=Apobec3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP   VARIANTS ARG-34; 37-ILE-ASP-38; 112-VAL-LEU-113; 134-ILE-ARG-135;
RP   ASN-139; LYS-181; 233-VAL-HIS-LEU-235; GLY-258; ILE-306 AND HIS-404.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 4), AND VARIANTS.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RA   Mariani R., Landau N.R.;
RL   Submitted (FEB-2004) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12466850; DOI=10.1038/nature01262;
RA   Waterston R.H., Lindblad-Toh K., Birney E., Rogers J., Abril J.F.,
RA   Agarwal P., Agarwala R., Ainscough R., Alexandersson M., An P.,
RA   Antonarakis S.E., Attwood J., Baertsch R., Bailey J., Barlow K.,
RA   Beck S., Berry E., Birren B., Bloom T., Bork P., Botcherby M.,
RA   Bray N., Brent M.R., Brown D.G., Brown S.D., Bult C., Burton J.,
RA   Butler J., Campbell R.D., Carninci P., Cawley S., Chiaromonte F.,
RA   Chinwalla A.T., Church D.M., Clamp M., Clee C., Collins F.S.,
RA   Cook L.L., Copley R.R., Coulson A., Couronne O., Cuff J., Curwen V.,
RA   Cutts T., Daly M., David R., Davies J., Delehaunty K.D., Deri J.,
RA   Dermitzakis E.T., Dewey C., Dickens N.J., Diekhans M., Dodge S.,
RA   Dubchak I., Dunn D.M., Eddy S.R., Elnitski L., Emes R.D., Eswara P.,
RA   Eyras E., Felsenfeld A., Fewell G.A., Flicek P., Foley K.,
RA   Frankel W.N., Fulton L.A., Fulton R.S., Furey T.S., Gage D.,
RA   Gibbs R.A., Glusman G., Gnerre S., Goldman N., Goodstadt L.,
RA   Grafham D., Graves T.A., Green E.D., Gregory S., Guigo R., Guyer M.,
RA   Hardison R.C., Haussler D., Hayashizaki Y., Hillier L.W., Hinrichs A.,
RA   Hlavina W., Holzer T., Hsu F., Hua A., Hubbard T., Hunt A.,
RA   Jackson I., Jaffe D.B., Johnson L.S., Jones M., Jones T.A., Joy A.,
RA   Kamal M., Karlsson E.K., Karolchik D., Kasprzyk A., Kawai J.,
RA   Keibler E., Kells C., Kent W.J., Kirby A., Kolbe D.L., Korf I.,
RA   Kucherlapati R.S., Kulbokas E.J., Kulp D., Landers T., Leger J.P.,
RA   Leonard S., Letunic I., Levine R., Li J., Li M., Lloyd C., Lucas S.,
RA   Ma B., Maglott D.R., Mardis E.R., Matthews L., Mauceli E., Mayer J.H.,
RA   McCarthy M., McCombie W.R., McLaren S., McLay K., McPherson J.D.,
RA   Meldrim J., Meredith B., Mesirov J.P., Miller W., Miner T.L.,
RA   Mongin E., Montgomery K.T., Morgan M., Mott R., Mullikin J.C.,
RA   Muzny D.M., Nash W.E., Nelson J.O., Nhan M.N., Nicol R., Ning Z.,
RA   Nusbaum C., O'Connor M.J., Okazaki Y., Oliver K., Overton-Larty E.,
RA   Pachter L., Parra G., Pepin K.H., Peterson J., Pevzner P., Plumb R.,
RA   Pohl C.S., Poliakov A., Ponce T.C., Ponting C.P., Potter S., Quail M.,
RA   Reymond A., Roe B.A., Roskin K.M., Rubin E.M., Rust A.G., Santos R.,
RA   Sapojnikov V., Schultz B., Schultz J., Schwartz M.S., Schwartz S.,
RA   Scott C., Seaman S., Searle S., Sharpe T., Sheridan A., Shownkeen R.,
RA   Sims S., Singer J.B., Slater G., Smit A., Smith D.R., Spencer B.,
RA   Stabenau A., Stange-Thomann N., Sugnet C., Suyama M., Tesler G.,
RA   Thompson J., Torrents D., Trevaskis E., Tromp J., Ucla C.,
RA   Ureta-Vidal A., Vinson J.P., Von Niederhausern A.C., Wade C.M.,
RA   Wall M., Weber R.J., Weiss R.B., Wendl M.C., West A.P.,
RA   Wetterstrand K., Wheeler R., Whelan S., Wierzbowski J., Willey D.,
RA   Williams S., Wilson R.K., Winter E., Worley K.C., Wyman D., Yang S.,
RA   Yang S.P., Zdobnov E.M., Zody M.C., Lander E.S.;
RT   "Initial sequencing and comparative analysis of the mouse genome.";
RL   Nature 420:520-562(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP   ARG-34; 37-ILE-ASP-38; 112-VAL-LEU-113; 134-ILE-ARG-135; ASN-139;
RP   LYS-181; 233-VAL-HIS-LEU-235; GLY-258; ILE-306 AND HIS-404.
RC   TISSUE=Mammary tumor;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   DNA C TO U EDITING ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=12859895; DOI=10.1016/S0092-8674(03)00515-4;
RA   Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R.,
RA   Bollman B., 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   [6]
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.,
RA   Landau N.R., Weitzman M.D.;
RT   "APOBEC3A is a potent inhibitor of adeno-associated virus and
RT   retrotransposons.";
RL   Curr. Biol. 16:480-485(2006).
RN   [7]
RP   DOMAIN CMP/DCMP DEAMINASE, SUBUNIT, AND MUTAGENESIS OF GLU-73 AND
RP   GLU-290.
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   [8]
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   [9]
RP   FUNCTION IN MMTV RESTRICTION, AND INTERACTION WITH MMTV NUCLEOCAPSID
RP   PROTEIN P14.
RX   PubMed=17259974; DOI=10.1038/nature05540;
RA   Okeoma C.M., Lovsin N., Peterlin B.M., Ross S.R.;
RT   "APOBEC3 inhibits mouse mammary tumour virus replication in vivo.";
RL   Nature 445:927-930(2007).
RN   [10]
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   [11]
RP   FUNCTION IN FRMLV RESTRICTION.
RX   PubMed=18786991; DOI=10.1128/JVI.01311-08;
RA   Takeda E., Tsuji-Kawahara S., Sakamoto M., Langlois M.A.,
RA   Neuberger M.S., Rada C., Miyazawa M.;
RT   "Mouse APOBEC3 restricts friend leukemia virus infection and
RT   pathogenesis in vivo.";
RL   J. Virol. 82:10998-11008(2008).
CC   -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an
CC       inhibitor of retrovirus replication and retrotransposon mobility
CC       via deaminase-dependent and -independent mechanisms. Selectively
CC       targets single-stranded DNA and does not deaminate double-stranded
CC       DNA or single-or double-stranded RNA. Exhibits antiviral activity
CC       against HIV-1, simian immunodeficiency viruses (SIVs), mouse
CC       mammary tumor virus (MMTV) and friend murine leukemia virus
CC       (FrMLV) and may inhibit the mobility of LTR retrotransposons.
CC       {ECO:0000269|PubMed:16378963, ECO:0000269|PubMed:16527742,
CC       ECO:0000269|PubMed:17259974, ECO:0000269|PubMed:18786991}.
CC   -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Interacts with mouse mammary tumor virus
CC       (MMTV) nucleocapsid protein p14. {ECO:0000269|PubMed:17020885,
CC       ECO:0000269|PubMed:17259974}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16527742}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q99J72-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99J72-2; Sequence=VSP_009832;
CC       Name=3;
CC         IsoId=Q99J72-3; Sequence=VSP_009831, VSP_009833;
CC       Name=4;
CC         IsoId=Q99J72-4; Sequence=VSP_009831;
CC         Note=Lacks exon V. Found in cell line MDTF.;
CC   -!- TISSUE SPECIFICITY: Expressed in spleen, node and lung.
CC       {ECO:0000269|PubMed:12859895}.
CC   -!- DOMAIN: The CMP/dCMP deaminase domain 1 confers deoxycytidine
CC       deaminase activity, whereas the CMP/dCMP deaminase domain 2
CC       mediates RNA-dependent oligomerization and virion incorporation.
CC       {ECO:0000269|PubMed:17020885}.
CC   -!- MISCELLANEOUS: Probable human APOBEC3G ortholog.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 CMP/dCMP-type deaminase domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU01083}.
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DR   EMBL; AK044394; BAC31901.1; -; mRNA.
DR   EMBL; AK049998; BAC34023.1; -; mRNA.
DR   EMBL; AC113595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003314; AAH03314.1; -; mRNA.
DR   CCDS; CCDS27654.1; -. [Q99J72-4]
DR   CCDS; CCDS49669.1; -. [Q99J72-1]
DR   UniGene; Mm.284059; -.
DR   UniGene; Mm.432615; -.
DR   ProteinModelPortal; Q99J72; -.
DR   SMR; Q99J72; 26-197, 258-404.
DR   STRING; 10090.ENSMUSP00000105249; -.
DR   iPTMnet; Q99J72; -.
DR   PhosphoSite; Q99J72; -.
DR   MaxQB; Q99J72; -.
DR   PaxDb; Q99J72; -.
DR   PRIDE; Q99J72; -.
DR   Ensembl; ENSMUST00000165537; ENSMUSP00000132391; ENSMUSG00000009585. [Q99J72-4]
DR   MGI; MGI:1933111; Apobec3.
DR   eggNOG; ENOG410JBA1; Eukaryota.
DR   eggNOG; ENOG41119MS; LUCA.
DR   GeneTree; ENSGT00530000062933; -.
DR   HOGENOM; HOG000033755; -.
DR   HOVERGEN; HBG050434; -.
DR   InParanoid; Q99J72; -.
DR   PhylomeDB; Q99J72; -.
DR   BRENDA; 3.5.4.1; 3474.
DR   PRO; PR:Q99J72; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000009585; -.
DR   CleanEx; MM_APOBEC3; -.
DR   ExpressionAtlas; Q99J72; baseline and differential.
DR   Genevisible; Q99J72; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0047844; F:deoxycytidine deaminase activity; ISO:MGI.
DR   GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR013158; APOBEC_N.
DR   InterPro; IPR002125; CMP_dCMP_Zn-bd.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   Pfam; PF08210; APOBEC_N; 2.
DR   SUPFAM; SSF53927; SSF53927; 2.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 2.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiviral defense; Complete proteome; Cytoplasm;
KW   Hydrolase; Immunity; Innate immunity; Metal-binding; Polymorphism;
KW   Reference proteome; Repeat; Zinc.
FT   CHAIN         1    429       DNA dC->dU-editing enzyme APOBEC-3.
FT                                /FTId=PRO_0000171772.
FT   DOMAIN       38    154       CMP/dCMP-type deaminase 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01083}.
FT   DOMAIN      238    357       CMP/dCMP-type deaminase 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01083}.
FT   ACT_SITE     73     73       Proton donor. {ECO:0000250}.
FT   METAL        71     71       Zinc. {ECO:0000250}.
FT   METAL       105    105       Zinc. {ECO:0000250}.
FT   METAL       108    108       Zinc. {ECO:0000250}.
FT   METAL       288    288       Zinc. {ECO:0000250}.
FT   METAL       316    316       Zinc. {ECO:0000250}.
FT   METAL       319    319       Zinc. {ECO:0000250}.
FT   VAR_SEQ     198    230       Missing (in isoform 3 and isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_009831.
FT   VAR_SEQ     409    429       SWGLQDLVNDFGNLQLGPPMS -> VRTTLLQGPAS (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_009832.
FT   VAR_SEQ     409    429       SWGLQDLVNDFGNLQLGPPMS -> SRSHAS (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_009833.
FT   VARIANT      20     20       L -> V (in cell line MDTF).
FT   VARIANT      31     31       K -> E (in cell line MDTF).
FT   VARIANT      34     35       GY -> PF (in cell line MDTF).
FT   VARIANT      34     34       G -> R (in cell lines L1.2 and 3T3).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT      37     38       KG -> ID (in cell lines L1.2 and 3T3).
FT   VARIANT      38     38       G -> K (in cell line MDTF; requires 2
FT                                nucleotide substitutions).
FT   VARIANT     111    111       Q -> R (in cell line L1.2).
FT   VARIANT     112    113       IV -> VL (in cell lines L1.2 and 3T3).
FT   VARIANT     112    112       I -> V (in cell line MDTF).
FT   VARIANT     128    128       S -> F (in cell line MDTF).
FT   VARIANT     134    139       VQDPET -> IRNPEN (in cell line MDTF).
FT   VARIANT     134    135       VQ -> IR (in cell lines L1.2 and 3T3).
FT   VARIANT     139    140       TQ -> NQL (in cell line 3T3).
FT   VARIANT     139    139       T -> N (in cell line L1.2).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     148    148       Q -> L (in cell line MDTF).
FT   VARIANT     162    163       KK -> EE (in cell line MDTF).
FT   VARIANT     181    181       R -> K (in cell lines L1.2 and 3T3).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     230    235       GRRMDP -> RRRVHL (in cell line 3T3).
FT   VARIANT     233    235       MDP -> VHL.
FT   VARIANT     234    235       DP -> SL (in cell line MDTF).
FT   VARIANT     248    248       Q -> L (in cell line MDTF).
FT   VARIANT     258    259       RM -> GV (in cell line 3T3).
FT   VARIANT     258    258       R -> G (in cell line L1.2).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     264    264       C -> F (in cell line MDTF).
FT   VARIANT     269    269       Q -> W (in cell line MDTF; requires 2
FT                                nucleotide substitutions).
FT   VARIANT     274    274       A -> E (in cell line MDTF).
FT   VARIANT     284    296       Missing (in cell line MDTF).
FT   VARIANT     306    306       T -> I (in cell lines L1.2 and 3T3).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     314    314       S -> G (in cell line EL4).
FT   VARIANT     328    328       R -> K (in cell line MDTF).
FT   VARIANT     381    381       N -> S (in cell line MDTF).
FT   VARIANT     387    387       W -> R (in splenocytes).
FT   VARIANT     394    395       II -> KT (in cell line MDTF).
FT   VARIANT     399    399       T -> A (in cell line L1.2).
FT   VARIANT     404    404       R -> C (in cell lines MDTF and 3T3).
FT   VARIANT     404    404       R -> H (in cell line L1.2).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   MUTAGEN      73     73       E->A: Decrease in cytidine deaminase and
FT                                antiviral activity.
FT                                {ECO:0000269|PubMed:17020885}.
FT   MUTAGEN      73     73       E->A: Decrease in cytidine deaminase and
FT                                antiviral activity; when associated with
FT                                A-290. {ECO:0000269|PubMed:17020885}.
FT   MUTAGEN     290    290       E->A: Decrease in cytidine deaminase and
FT                                antiviral activity; when associated with
FT                                A-73. {ECO:0000269|PubMed:17020885}.
FT   MUTAGEN     290    290       E->A: No effect on cytidine deaminase and
FT                                antiviral activity.
FT                                {ECO:0000269|PubMed:17020885}.
FT   CONFLICT    203    203       P -> S (in Ref. 3; AC113595).
FT                                {ECO:0000305}.
FT   CONFLICT    227    227       C -> W (in Ref. 3; AC113595).
FT                                {ECO:0000305}.
FT   CONFLICT    230    230       G -> R (in Ref. 2; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    410    414       WGLQD -> RSHAS (in Ref. 1; BAC34023).
FT                                {ECO:0000305}.
SQ   SEQUENCE   429 AA;  50948 MW;  2B4361CDD81C99E5 CRC64;
     MGPFCLGCSH RKCYSPIRNL ISQETFKFHF KNLGYAKGRK DTFLCYEVTR KDCDSPVSLH
     HGVFKNKDNI HAEICFLYWF HDKVLKVLSP REEFKITWYM SWSPCFECAE QIVRFLATHH
     NLSLDIFSSR LYNVQDPETQ QNLCRLVQEG AQVAAMDLYE FKKCWKKFVD NGGRRFRPWK
     RLLTNFRYQD SKLQEILRPC YIPVPSSSSS TLSNICLTKG LPETRFCVEG RRMDPLSEEE
     FYSQFYNQRV KHLCYYHRMK PYLCYQLEQF NGQAPLKGCL LSEKGKQHAE ILFLDKIRSM
     ELSQVTITCY LTWSPCPNCA WQLAAFKRDR PDLILHIYTS RLYFHWKRPF QKGLCSLWQS
     GILVDVMDLP QFTDCWTNFV NPKRPFWPWK GLEIISRRTQ RRLRRIKESW GLQDLVNDFG
     NLQLGPPMS
//