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 28-FEB-2018, entry version 127. 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; 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: 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 -!- SEQUENCE CAUTION: CC Sequence=AAH03314.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=BAC31901.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=BAC34023.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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 UniGene; Mm.284059; -. DR UniGene; Mm.432615; -. DR ProteinModelPortal; Q99J72; -. DR SMR; Q99J72; -. DR STRING; 10090.ENSMUSP00000105249; -. 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 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 OMA; ITCYLTW; -. DR OrthoDB; EOG091G0J2L; -. 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 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: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 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; IPR013158; APOBEC_N. DR InterPro; IPR002125; CMP_dCMP_dom. 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 1 440 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 //