ID   ABEC3_MOUSE             Reviewed;         440 AA.
AC   Q99J72; H3BJL0; Q8C7L0; Q8C8V7;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 3.
DT   13-NOV-2019, entry version 138.
DE   RecName: Full=DNA dC->dU-editing enzyme APOBEC-3;
DE            EC=3.5.4.38;
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; Myomorpha;
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-45; 48-ILE-ASP-49; 123-VAL-LEU-124; 145-ILE-ARG-146;
RP   ASN-150; LYS-192; 244-VAL-HIS-LEU-246; GLY-269; ILE-317 AND HIS-415.
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP   ARG-45; 48-ILE-ASP-49; 123-VAL-LEU-124; 145-ILE-ARG-146; ASN-150;
RP   LYS-192; 244-VAL-HIS-LEU-246; GLY-269; ILE-317 AND HIS-415.
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-84 AND
RP   GLU-301.
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:
CC       Reaction=a 2'-deoxycytidine in a single-stranded DNA + H(+) + H2O
CC         = a 2'-deoxyuridine in a single-stranded DNA + NH4(+);
CC         Xref=Rhea:RHEA:50948, Rhea:RHEA-COMP:12846, Rhea:RHEA-
CC         COMP:12847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:85452, ChEBI:CHEBI:133902;
CC         EC=3.5.4.38;
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAH03314.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC31901.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC34023.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK044394; BAC31901.1; ALT_INIT; mRNA.
DR   EMBL; AK049998; BAC34023.1; ALT_INIT; mRNA.
DR   EMBL; AC113595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003314; AAH03314.1; ALT_INIT; mRNA.
DR   RefSeq; XP_017172295.1; XM_017316806.1. [Q99J72-3]
DR   SMR; Q99J72; -.
DR   STRING; 10090.ENSMUSP00000135027; -.
DR   iPTMnet; Q99J72; -.
DR   PhosphoSitePlus; Q99J72; -.
DR   MaxQB; Q99J72; -.
DR   PaxDb; Q99J72; -.
DR   PRIDE; Q99J72; -.
DR   Ensembl; ENSMUST00000175714; ENSMUSP00000135027; ENSMUSG00000009585. [Q99J72-1]
DR   Ensembl; ENSMUST00000175752; ENSMUSP00000135358; ENSMUSG00000009585. [Q99J72-4]
DR   Ensembl; ENSMUST00000176325; ENSMUSP00000134838; ENSMUSG00000009585. [Q99J72-2]
DR   Ensembl; ENSMUST00000177098; ENSMUSP00000135079; ENSMUSG00000009585. [Q99J72-3]
DR   GeneID; 80287; -.
DR   CTD; 80287; -.
DR   MGI; MGI:1933111; Apobec3.
DR   eggNOG; ENOG410JBA1; Eukaryota.
DR   eggNOG; ENOG41119MS; LUCA.
DR   GeneTree; ENSGT00940000162772; -.
DR   HOGENOM; HOG000033755; -.
DR   InParanoid; Q99J72; -.
DR   OrthoDB; 586309at2759; -.
DR   PhylomeDB; Q99J72; -.
DR   TreeFam; TF331356; -.
DR   BRENDA; 3.5.4.1; 3474.
DR   Reactome; R-MMU-72200; mRNA Editing: C to U Conversion.
DR   Reactome; R-MMU-75094; Formation of the Editosome.
DR   ChiTaRS; Apobec3; mouse.
DR   PRO; PR:Q99J72; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000009585; Expressed in 195 organ(s), highest expression level in bone marrow.
DR   ExpressionAtlas; Q99J72; baseline and differential.
DR   Genevisible; Q99J72; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
DR   GO; GO:0047844; F:deoxycytidine deaminase activity; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016554; P:cytidine to uridine editing; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR   GO; GO:0070383; P:DNA cytosine deamination; IBA:GO_Central.
DR   GO; GO:0080111; P:DNA demethylation; IBA:GO_Central.
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:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IBA:GO_Central.
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:0050688; P:regulation of defense response to virus; IMP:MGI.
DR   GO; GO:1903900; P:regulation of viral life cycle; IMP:MGI.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
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    440       DNA dC->dU-editing enzyme APOBEC-3.
FT                                /FTId=PRO_0000171772.
FT   DOMAIN       49    165       CMP/dCMP-type deaminase 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01083}.
FT   DOMAIN      249    368       CMP/dCMP-type deaminase 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01083}.
FT   ACT_SITE     84     84       Proton donor. {ECO:0000250}.
FT   METAL        82     82       Zinc. {ECO:0000250}.
FT   METAL       116    116       Zinc. {ECO:0000250}.
FT   METAL       119    119       Zinc. {ECO:0000250}.
FT   METAL       299    299       Zinc. {ECO:0000250}.
FT   METAL       327    327       Zinc. {ECO:0000250}.
FT   METAL       330    330       Zinc. {ECO:0000250}.
FT   VAR_SEQ     209    241       Missing (in isoform 3 and isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_009831.
FT   VAR_SEQ     420    440       SWGLQDLVNDFGNLQLGPPMS -> VRTTLLQGPAS (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_009832.
FT   VAR_SEQ     420    440       SWGLQDLVNDFGNLQLGPPMS -> SRSHAS (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_009833.
FT   VARIANT      31     31       L -> V (in cell line MDTF).
FT   VARIANT      42     42       K -> E (in cell line MDTF).
FT   VARIANT      45     46       GY -> PF (in cell line MDTF).
FT   VARIANT      45     45       G -> R (in cell lines L1.2 and 3T3).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT      48     49       KG -> ID (in cell lines L1.2 and 3T3).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT      49     49       G -> K (in cell line MDTF; requires 2
FT                                nucleotide substitutions).
FT   VARIANT     122    122       Q -> R (in cell line L1.2).
FT   VARIANT     123    124       IV -> VL (in cell lines L1.2 and 3T3).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     123    123       I -> V (in cell line MDTF).
FT   VARIANT     139    139       S -> F (in cell line MDTF).
FT   VARIANT     145    150       VQDPET -> IRNPEN (in cell line MDTF).
FT   VARIANT     145    146       VQ -> IR (in cell lines L1.2 and 3T3).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     150    151       TQ -> NQL (in cell line 3T3).
FT   VARIANT     150    150       T -> N (in cell line L1.2).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     159    159       Q -> L (in cell line MDTF).
FT   VARIANT     173    174       KK -> EE (in cell line MDTF).
FT   VARIANT     192    192       R -> K (in cell lines L1.2 and 3T3).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     241    246       GRRMDP -> RRRVHL (in cell line 3T3).
FT   VARIANT     244    246       MDP -> VHL. {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     245    246       DP -> SL (in cell line MDTF).
FT   VARIANT     259    259       Q -> L (in cell line MDTF).
FT   VARIANT     269    270       RM -> GV (in cell line 3T3).
FT   VARIANT     269    269       R -> G (in cell line L1.2).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     275    275       C -> F (in cell line MDTF).
FT   VARIANT     280    280       Q -> W (in cell line MDTF; requires 2
FT                                nucleotide substitutions).
FT   VARIANT     285    285       A -> E (in cell line MDTF).
FT   VARIANT     295    307       Missing (in cell line MDTF).
FT   VARIANT     317    317       T -> I (in cell lines L1.2 and 3T3).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     325    325       S -> G (in cell line EL4).
FT   VARIANT     339    339       R -> K (in cell line MDTF).
FT   VARIANT     392    392       N -> S (in cell line MDTF).
FT   VARIANT     398    398       W -> R (in splenocytes).
FT   VARIANT     405    406       II -> KT (in cell line MDTF).
FT   VARIANT     410    410       T -> A (in cell line L1.2).
FT   VARIANT     415    415       R -> C (in cell lines MDTF and 3T3).
FT   VARIANT     415    415       R -> H (in cell line L1.2).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:16141072}.
FT   MUTAGEN      84     84       E->A: Decrease in cytidine deaminase and
FT                                antiviral activity.
FT                                {ECO:0000269|PubMed:17020885}.
FT   MUTAGEN      84     84       E->A: Decrease in cytidine deaminase and
FT                                antiviral activity; when associated with
FT                                A-301. {ECO:0000269|PubMed:17020885}.
FT   MUTAGEN     301    301       E->A: Decrease in cytidine deaminase and
FT                                antiviral activity; when associated with
FT                                A-84. {ECO:0000269|PubMed:17020885}.
FT   MUTAGEN     301    301       E->A: No effect on cytidine deaminase and
FT                                antiviral activity.
FT                                {ECO:0000269|PubMed:17020885}.
FT   CONFLICT      6      6       L -> M (in Ref. 1; BAC31901 and 4;
FT                                AAH03314). {ECO:0000305}.
FT   CONFLICT    214    214       S -> P (in Ref. 1; BAC31901 and 4;
FT                                AAH03314). {ECO:0000305}.
FT   CONFLICT    238    238       W -> C (in Ref. 1; BAC31901 and 4;
FT                                AAH03314). {ECO:0000305}.
FT   CONFLICT    241    241       G -> R (in Ref. 2; no nucleotide entry).
FT                                {ECO:0000305}.
SQ   SEQUENCE   440 AA;  52213 MW;  AA0DA7AC616252E9 CRC64;
     MQPQRLGPRA GMGPFCLGCS HRKCYSPIRN LISQETFKFH FKNLGYAKGR KDTFLCYEVT
     RKDCDSPVSL HHGVFKNKDN IHAEICFLYW FHDKVLKVLS PREEFKITWY MSWSPCFECA
     EQIVRFLATH HNLSLDIFSS RLYNVQDPET QQNLCRLVQE GAQVAAMDLY EFKKCWKKFV
     DNGGRRFRPW KRLLTNFRYQ DSKLQEILRP CYISVPSSSS STLSNICLTK GLPETRFWVE
     GRRMDPLSEE EFYSQFYNQR VKHLCYYHRM KPYLCYQLEQ FNGQAPLKGC LLSEKGKQHA
     EILFLDKIRS MELSQVTITC YLTWSPCPNC AWQLAAFKRD RPDLILHIYT SRLYFHWKRP
     FQKGLCSLWQ SGILVDVMDL PQFTDCWTNF VNPKRPFWPW KGLEIISRRT QRRLRRIKES
     WGLQDLVNDF GNLQLGPPMS
//