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 02-OCT-2024, entry version 161. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS RP ARG-45; 48-LYS-GLY-49 DELINS ILE-ASP; 123-ILE-VAL-124 DELINS VAL-LEU; RP 145-VAL-GLN-146 DELINS ILE-ARG; ASN-150; LYS-192; 244-MET--PRO-246 DELINS RP VAL-HIS-LEU; 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., 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., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-45; RP 48-LYS-GLY-49 DELINS ILE-ASP; 123-ILE-VAL-124 DELINS VAL-LEU; RP 145-VAL-GLN-146 DELINS ILE-ARG; ASN-150; LYS-192; 244-MET--PRO-246 DELINS RP VAL-HIS-LEU; 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 project: RT 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., 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 [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., 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 [7] RP DOMAIN CMP/DCMP DEAMINASE, SUBUNIT, AND MUTAGENESIS OF GLU-84 AND 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., Neuberger M.S., RA Rada C., Miyazawa M.; RT "Mouse APOBEC3 restricts friend leukemia virus infection and pathogenesis RT in vivo."; RL J. Virol. 82:10998-11008(2008). 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. Selectively targets single- CC stranded DNA and does not deaminate double-stranded DNA or single- or CC double-stranded RNA. Exhibits antiviral activity against HIV-1, simian CC immunodeficiency viruses (SIVs), mouse mammary tumor virus (MMTV) and CC friend murine leukemia virus (FrMLV) and may inhibit the mobility of CC LTR retrotransposons. {ECO:0000269|PubMed:16378963, CC ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:17259974, CC ECO:0000269|PubMed:18786991}. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer. Interacts with mouse mammary tumor virus (MMTV) CC 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 -!- TISSUE SPECIFICITY: Expressed in spleen, node and lung. CC {ECO:0000269|PubMed:12859895}. CC -!- DOMAIN: The CMP/dCMP deaminase domain 1 confers deoxycytidine deaminase CC activity, whereas the CMP/dCMP deaminase domain 2 mediates RNA- CC dependent oligomerization and virion incorporation. CC {ECO:0000269|PubMed:17020885}. CC -!- MISCELLANEOUS: Probable human APOBEC3G ortholog. CC -!- MISCELLANEOUS: [Isoform 4]: Lacks exon V. Found in cell line MDTF. CC {ECO:0000305}. 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}; 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; 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 AlphaFoldDB; Q99J72; -. DR SMR; Q99J72; -. DR STRING; 10090.ENSMUSP00000105249; -. DR GlyGen; Q99J72; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99J72; -. DR PhosphoSitePlus; Q99J72; -. DR jPOST; Q99J72; -. DR PaxDb; 10090-ENSMUSP00000135027; -. DR ProteomicsDB; 286048; -. [Q99J72-1] DR ProteomicsDB; 286049; -. [Q99J72-2] DR ProteomicsDB; 286050; -. [Q99J72-3] DR ProteomicsDB; 286051; -. [Q99J72-4] DR Pumba; Q99J72; -. DR Antibodypedia; 26556; 60 antibodies from 19 providers. DR DNASU; 80287; -. DR Ensembl; ENSMUST00000175714.8; ENSMUSP00000135027.2; ENSMUSG00000009585.19. [Q99J72-1] DR Ensembl; ENSMUST00000175752.8; ENSMUSP00000135358.2; ENSMUSG00000009585.19. [Q99J72-4] DR Ensembl; ENSMUST00000176325.8; ENSMUSP00000134838.2; ENSMUSG00000009585.19. [Q99J72-2] DR Ensembl; ENSMUST00000177098.8; ENSMUSP00000135079.2; ENSMUSG00000009585.19. [Q99J72-3] DR GeneID; 80287; -. DR AGR; MGI:1933111; -. DR CTD; 80287; -. DR MGI; MGI:1933111; Apobec3. DR VEuPathDB; HostDB:ENSMUSG00000009585; -. DR eggNOG; KOG4075; Eukaryota. DR GeneTree; ENSGT00940000162772; -. DR InParanoid; Q99J72; -. DR OMA; FLCNQAP; -. DR OrthoDB; 5355962at2759; -. 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 RNAct; Q99J72; protein. DR Bgee; ENSMUSG00000009585; Expressed in mesenteric lymph node and 184 other cell types or tissues. DR ExpressionAtlas; Q99J72; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000932; C:P-body; IBA:GO_Central. DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0070383; P:DNA cytosine deamination; 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: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 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; IPR050610; APOBEC_Cyt_Deaminase. DR InterPro; IPR002125; CMP_dCMP_dom. DR InterPro; IPR016193; Cytidine_deaminase-like. DR PANTHER; PTHR13857:SF43; DNA DC-DU-EDITING ENZYME APOBEC-3H; 1. DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1. DR Pfam; PF18772; APOBEC2; 1. DR Pfam; PF18782; NAD2; 1. DR SUPFAM; SSF53927; Cytidine deaminase-like; 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; Cytoplasm; Hydrolase; Immunity; KW Innate immunity; Metal-binding; Reference proteome; Repeat; Zinc. FT CHAIN 1..440 FT /note="DNA dC->dU-editing enzyme APOBEC-3" FT /id="PRO_0000171772" FT DOMAIN 49..165 FT /note="CMP/dCMP-type deaminase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT DOMAIN 249..368 FT /note="CMP/dCMP-type deaminase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT ACT_SITE 84 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 82 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 116 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 299 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 327 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 330 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT VAR_SEQ 209..241 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_009831" FT VAR_SEQ 420..440 FT /note="SWGLQDLVNDFGNLQLGPPMS -> VRTTLLQGPAS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_009832" FT VAR_SEQ 420..440 FT /note="SWGLQDLVNDFGNLQLGPPMS -> SRSHAS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_009833" FT VARIANT 31 FT /note="L -> V (in cell line MDTF)" FT VARIANT 42 FT /note="K -> E (in cell line MDTF)" FT VARIANT 45..46 FT /note="GY -> PF (in cell line MDTF)" FT VARIANT 45 FT /note="G -> R (in cell lines L1.2 and 3T3)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT VARIANT 48..49 FT /note="KG -> ID (in cell lines L1.2 and 3T3)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT VARIANT 49 FT /note="G -> K (in cell line MDTF; requires 2 nucleotide FT substitutions)" FT VARIANT 122 FT /note="Q -> R (in cell line L1.2)" FT VARIANT 123..124 FT /note="IV -> VL (in cell lines L1.2 and 3T3)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT VARIANT 123 FT /note="I -> V (in cell line MDTF)" FT VARIANT 139 FT /note="S -> F (in cell line MDTF)" FT VARIANT 145..150 FT /note="VQDPET -> IRNPEN (in cell line MDTF)" FT VARIANT 145..146 FT /note="VQ -> IR (in cell lines L1.2 and 3T3)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT VARIANT 150..151 FT /note="TQ -> NQL (in cell line 3T3)" FT VARIANT 150 FT /note="T -> N (in cell line L1.2)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT VARIANT 159 FT /note="Q -> L (in cell line MDTF)" FT VARIANT 173..174 FT /note="KK -> EE (in cell line MDTF)" FT VARIANT 192 FT /note="R -> K (in cell lines L1.2 and 3T3)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT VARIANT 241..246 FT /note="GRRMDP -> RRRVHL (in cell line 3T3)" FT VARIANT 244..246 FT /note="MDP -> VHL" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT VARIANT 245..246 FT /note="DP -> SL (in cell line MDTF)" FT VARIANT 259 FT /note="Q -> L (in cell line MDTF)" FT VARIANT 269..270 FT /note="RM -> GV (in cell line 3T3)" FT VARIANT 269 FT /note="R -> G (in cell line L1.2)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT VARIANT 275 FT /note="C -> F (in cell line MDTF)" FT VARIANT 280 FT /note="Q -> W (in cell line MDTF; requires 2 nucleotide FT substitutions)" FT VARIANT 285 FT /note="A -> E (in cell line MDTF)" FT VARIANT 295..307 FT /note="Missing (in cell line MDTF)" FT VARIANT 317 FT /note="T -> I (in cell lines L1.2 and 3T3)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT VARIANT 325 FT /note="S -> G (in cell line EL4)" FT VARIANT 339 FT /note="R -> K (in cell line MDTF)" FT VARIANT 392 FT /note="N -> S (in cell line MDTF)" FT VARIANT 398 FT /note="W -> R (in splenocytes)" FT VARIANT 405..406 FT /note="II -> KT (in cell line MDTF)" FT VARIANT 410 FT /note="T -> A (in cell line L1.2)" FT VARIANT 415 FT /note="R -> C (in cell lines MDTF and 3T3)" FT VARIANT 415 FT /note="R -> H (in cell line L1.2)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT MUTAGEN 84 FT /note="E->A: Decrease in cytidine deaminase and antiviral FT activity." FT /evidence="ECO:0000269|PubMed:17020885" FT MUTAGEN 84 FT /note="E->A: Decrease in cytidine deaminase and antiviral FT activity; when associated with A-301." FT /evidence="ECO:0000269|PubMed:17020885" FT MUTAGEN 301 FT /note="E->A: Decrease in cytidine deaminase and antiviral FT activity; when associated with A-84." FT /evidence="ECO:0000269|PubMed:17020885" FT MUTAGEN 301 FT /note="E->A: No effect on cytidine deaminase and antiviral FT activity." FT /evidence="ECO:0000269|PubMed:17020885" FT CONFLICT 6 FT /note="L -> M (in Ref. 1; BAC31901 and 4; AAH03314)" FT /evidence="ECO:0000305" FT CONFLICT 214 FT /note="S -> P (in Ref. 1; BAC31901 and 4; AAH03314)" FT /evidence="ECO:0000305" FT CONFLICT 238 FT /note="W -> C (in Ref. 1; BAC31901 and 4; AAH03314)" FT /evidence="ECO:0000305" FT CONFLICT 241 FT /note="G -> R (in Ref. 2; no nucleotide entry)" FT /evidence="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 //