ID PQT3_ARATH Reviewed; 826 AA. AC F4JP52; F4JP50; O23583; O23584; Q0WV36; DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 31-JAN-2018, entry version 55. DE RecName: Full=E3 ubiquitin ligase PARAQUAT TOLERANCE 3 {ECO:0000303|PubMed:27676073}; DE EC=2.3.2.27 {ECO:0000269|PubMed:27676073}; GN Name=PQT3 {ECO:0000303|PubMed:27676073}; GN OrderedLocusNames=At4g17410 {ECO:0000312|Araport:AT4G17410}; GN ORFNames=dl4740w {ECO:0000312|EMBL:CAB10521.1}, GN FCAALL.426 {ECO:0000312|EMBL:CAB78743.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9461215; DOI=10.1038/35140; RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., RA Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., RA Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., RA Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., RA Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., RA Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., RA Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., RA Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., RA Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., RA Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., RA Klosterman S., Schueller C., Chalwatzis N.; RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of RT Arabidopsis thaliana."; RL Nature 391:485-488(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=cv. Columbia; RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004; RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., RA Andreasson E., Rathjen J.P., Peck S.C.; RT "Phosphoproteomic analysis of nuclei-enriched fractions from RT Arabidopsis thaliana."; RL J. Proteomics 72:439-451(2009). RN [6] RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PRMT13/PRMT4B, RP REPRESSION BY OXIDATIVE STRESS, CATALYTIC ACTIVITY, TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RC STRAIN=cv. Columbia; RX PubMed=27676073; DOI=10.1371/journal.pgen.1006332; RA Luo C., Cai X.-T., Du J., Zhao T.-L., Wang P.-F., Zhao P.-X., Liu R., RA Xie Q., Cao X.-F., Xiang C.-B.; RT "PARAQUAT TOLERANCE3 is an E3 ligase that switches off activated RT oxidative response by targeting histone-modifying PROTEIN RT METHYLTRANSFERASE4b."; RL PLoS Genet. 12:E1006332-E1006332(2016). CC -!- FUNCTION: E3 ubiquitin ligase acting as a negative regulator of CC oxidative stress tolerance, probably by mediating 26S proteasome- CC mediated degradation of PRMT13/PRMT4B, thus preventing APX1 and CC GPX1 accumulation via the reduction of histone H3 methylation CC (H3R17me2a). Confers sensitivity to cadmium CdCl(2) and salt NaCl CC stresses. {ECO:0000269|PubMed:27676073}. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor CC protein]-L-lysine. {ECO:0000269|PubMed:27676073}. CC -!- SUBUNIT: Interacts with PRMT13/PRMT4B in the nucleus. CC {ECO:0000269|PubMed:27676073}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE- CC ProRule:PRU00768, ECO:0000269|PubMed:27676073}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=F4JP52-1; Sequence=Displayed; CC Name=2; CC IsoId=F4JP52-2; Sequence=VSP_058683; CC Note=Derived from EST data. No experimental confirmation CC available. {ECO:0000312|EMBL:AEE83885.1, CC ECO:0000312|EMBL:AEE83886.1}; CC -!- TISSUE SPECIFICITY: Expressed constitutively in both shoot and CC root tissues. {ECO:0000269|PubMed:27676073}. CC -!- INDUCTION: Repressed rapidly by oxidative stress such as paraquat, CC hydrogen peroxide H(2)O(2), mannitol, drought and cadmium ion CC CdCl(2). {ECO:0000269|PubMed:27676073}. CC -!- DISRUPTION PHENOTYPE: Increased tolerance to paraquat-triggered CC oxidative stress associated with PRMT13/PRMT4B, APX1 and GPX1 CC accumulation due to increased histone H3 methylation (H3R17me2a). CC {ECO:0000269|PubMed:27676073}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB10521.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB10522.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB78743.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB78744.1; Type=Erroneous gene model prediction; 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; Z97343; CAB10521.1; ALT_SEQ; Genomic_DNA. DR EMBL; Z97343; CAB10522.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161546; CAB78743.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161546; CAB78744.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002687; AEE83884.1; -; Genomic_DNA. DR EMBL; CP002687; AEE83885.1; -; Genomic_DNA. DR EMBL; CP002687; AEE83886.1; -; Genomic_DNA. DR EMBL; CP002687; ANM66691.1; -; Genomic_DNA. DR EMBL; AK226942; BAE99012.1; -; mRNA. DR PIR; D71443; D71443. DR PIR; E71443; E71443. DR RefSeq; NP_001190750.1; NM_001203821.2. [F4JP52-2] DR RefSeq; NP_001190751.1; NM_001203822.1. [F4JP52-2] DR RefSeq; NP_001328573.1; NM_001341221.1. [F4JP52-1] DR RefSeq; NP_193471.2; NM_117844.5. [F4JP52-1] DR UniGene; At.4477; -. DR ProteinModelPortal; F4JP52; -. DR SMR; F4JP52; -. DR STRING; 3702.AT4G17410.2; -. DR iPTMnet; F4JP52; -. DR EnsemblPlants; AT4G17410.1; AT4G17410.1; AT4G17410. [F4JP52-1] DR EnsemblPlants; AT4G17410.2; AT4G17410.2; AT4G17410. [F4JP52-2] DR EnsemblPlants; AT4G17410.3; AT4G17410.3; AT4G17410. [F4JP52-2] DR EnsemblPlants; AT4G17410.5; AT4G17410.5; AT4G17410. [F4JP52-1] DR GeneID; 827452; -. DR Gramene; AT4G17410.1; AT4G17410.1; AT4G17410. [F4JP52-1] DR Gramene; AT4G17410.2; AT4G17410.2; AT4G17410. [F4JP52-2] DR Gramene; AT4G17410.3; AT4G17410.3; AT4G17410. [F4JP52-2] DR Gramene; AT4G17410.5; AT4G17410.5; AT4G17410. [F4JP52-1] DR KEGG; ath:AT4G17410; -. DR Araport; AT4G17410; -. DR TAIR; locus:2130933; AT4G17410. DR eggNOG; KOG0314; Eukaryota. DR eggNOG; COG5222; LUCA. DR HOGENOM; HOG000015179; -. DR KO; K10624; -. DR OMA; CKEVMRD; -. DR OrthoDB; EOG093603LD; -. DR Reactome; R-ATH-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR PRO; PR:F4JP52; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; F4JP52; baseline and differential. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB. DR GO; GO:0061659; F:ubiquitin-like protein ligase activity; IDA:TAIR. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0072756; P:cellular response to paraquat; IMP:UniProtKB. DR GO; GO:0034971; P:histone H3-R17 methylation; IMP:UniProtKB. DR GO; GO:1902883; P:negative regulation of response to oxidative stress; IMP:UniProtKB. DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:TAIR. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0046686; P:response to cadmium ion; IEP:UniProtKB. DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB. DR GO; GO:0010555; P:response to mannitol; IEP:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB. DR GO; GO:1901562; P:response to paraquat; IEP:UniProtKB. DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB. DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR014891; DWNN_domain. DR InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF08783; DWNN; 1. DR Pfam; PF13696; zf-CCHC_2; 1. DR SMART; SM01180; DWNN; 1. DR PROSITE; PS51282; DWNN; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Stress response; Transferase; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1 826 E3 ubiquitin ligase PARAQUAT TOLERANCE 3. FT /FTId=PRO_0000438583. FT DOMAIN 3 76 DWNN. {ECO:0000255|PROSITE- FT ProRule:PRU00612}. FT ZN_FING 203 216 CCHC-type. {ECO:0000255|PROSITE- FT ProRule:PRU00047}. FT ZN_FING 288 326 RING-type; degenerate. FT {ECO:0000255|PROSITE-ProRule:PRU00175}. FT MOTIF 668 675 Nuclear localization signal 1. FT {ECO:0000255|PROSITE-ProRule:PRU00768}. FT MOTIF 695 702 Nuclear localization signal 2. FT {ECO:0000255|PROSITE-ProRule:PRU00768}. FT COMPBIAS 493 550 Gly-rich. {ECO:0000255|PROSITE- FT ProRule:PRU00008}. FT COMPBIAS 654 711 Arg-rich. {ECO:0000255|PROSITE- FT ProRule:PRU00002}. FT MOD_RES 278 278 Phosphoserine. FT {ECO:0000250|UniProtKB:B9DFV2}. FT MOD_RES 397 397 Phosphoserine. FT {ECO:0000250|UniProtKB:B9DFV2}. FT MOD_RES 800 800 Phosphoserine. FT {ECO:0000250|UniProtKB:B9DFV2}. FT VAR_SEQ 468 468 Q -> QA (in isoform 2). FT /FTId=VSP_058683. FT CONFLICT 776 776 E -> G (in Ref. 4; BAE99012). FT {ECO:0000305}. SQ SEQUENCE 826 AA; 91306 MW; 8561CAD8B8AD0C14 CRC64; MAIYYKFKSA RDYDTISMDG PFITVGLLKE KIYETKHLGS GKDLDIVISN AQTNEEYLDE AMLIPKNTSV LIRRVPGRPR IRIITREEPR VEDKVENVQA DMNNVITADA SPVEDEFDEF GNDLYSIPDA PAVHSNNLCH DSAPADDEET KLKALIDTPA LDWHQQGADS FGPGRGYGRG MAGRMGGRGF GMERTTPPPG YVCHRCNVSG HFIQHCSTNG NPNFDVKRVK PPTGIPKSML MATPNGSYSL PSGAVAVLKP NEDAFEKEME GLTSTTRSVG EFPPELKCPL CKEVMRDAAL ASKCCLKSYC DKCIRDHIIA KSMCVCGATH VLADDLLPNK TLRDTINRIL ESGNSSAENA GSMCQVQDME SVRCPPPKAL SPTTSAASGG EKKPAPSNNN ETSTLKPSIE IAEITSAWAS AEIVKVEKPV DASANIQGSS NGKEAAVSQL NTQPPKEEMP QQVASGEQGK RKKKKPRMSG TDLAGPDYMM PMGPGPGNQY FNGFQPGFNG VQHGFNGVQP GFNGFHHGFN GFPGPFPGAM PPFVGYGFGG VIHPDPFAAQ GFGFPNIPPP YRDLAEMGNR MNLQHPIMGR EEFEAKKTEM KRKRENEIRR SEGGNVVRDS EKSRIMNNSA VTSSPVKPKS RQGPPPPISS DYDRRRRSDR SSPERQSSRR FTSPPRSSSR KSERDRHHDL DSEHDRRRDR PRETDRKHRK RSEKSSSDPT VEIDDNNKSN VFTRISFPEE SSGKQRKTSK SSPAPPESSV APVSSGRRHH SRREREMVEY DSSDDEDRHF KRKPSRYKRS PSVAPSDAGD EHFRHSKRSK GERARA //