ABEC3_MOUSE
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 03-AUG-2022, entry version 149.
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-ILE-ASP-49; 123-VAL-LEU-124; 145-ILE-ARG-146; ASN-150; LYS-192;
RP 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., 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-ILE-ASP-49; 123-VAL-LEU-124; 145-ILE-ARG-146; ASN-150; LYS-192;
RP 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 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};
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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 AlphaFoldDB; Q99J72; -.
DR SMR; Q99J72; -.
DR STRING; 10090.ENSMUSP00000135027; -.
DR iPTMnet; Q99J72; -.
DR PhosphoSitePlus; Q99J72; -.
DR EPD; Q99J72; -.
DR jPOST; Q99J72; -.
DR MaxQB; Q99J72; -.
DR PaxDb; Q99J72; -.
DR PRIDE; Q99J72; -.
DR ProteomicsDB; 286048; -. [Q99J72-1]
DR ProteomicsDB; 286049; -. [Q99J72-2]
DR ProteomicsDB; 286050; -. [Q99J72-3]
DR ProteomicsDB; 286051; -. [Q99J72-4]
DR Antibodypedia; 26556; 47 antibodies from 19 providers.
DR DNASU; 80287; -.
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 VEuPathDB; HostDB:ENSMUSG00000009585; -.
DR eggNOG; KOG4075; Eukaryota.
DR GeneTree; ENSGT00940000162772; -.
DR InParanoid; Q99J72; -.
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 181 other tissues.
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; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0004126; F:cytidine deaminase activity; ISO:MGI.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
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: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; 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
