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 10-FEB-2021, entry version 71. 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., Ridley P., RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E., RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.; RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis RT 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., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., 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., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). 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., Hayashizaki Y., RA 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., Andreasson E., RA Rathjen J.P., Peck S.C.; RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis RT thaliana."; RL J. Proteomics 72:439-451(2009). RN [6] RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PRMT13/PRMT4B, REPRESSION RP BY OXIDATIVE STRESS, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND RP 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 oxidative RT response by targeting histone-modifying PROTEIN 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 GPX1 CC accumulation via the reduction of histone H3 methylation (H3R17me2a). CC Confers sensitivity to cadmium CdCl(2) and salt NaCl stresses. CC {ECO:0000269|PubMed:27676073}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={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-ProRule:PRU00768, CC 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 -!- TISSUE SPECIFICITY: Expressed constitutively in both shoot and root CC 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 CdCl(2). CC {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 SMR; F4JP52; -. DR STRING; 3702.AT4G17410.3; -. DR iPTMnet; F4JP52; -. DR PRIDE; F4JP52; -. DR ProteomicsDB; 234840; -. 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 OMA; TPCCEKT; -. DR OrthoDB; 872739at2759; -. 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:0006397; P:mRNA processing; IEA:InterPro. 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; IPR033489; RBBP6. DR InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR15439; PTHR15439; 2. 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; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Stress response; Transferase; Ubl conjugation pathway; KW Zinc; Zinc-finger. FT CHAIN 1..826 FT /note="E3 ubiquitin ligase PARAQUAT TOLERANCE 3" FT /id="PRO_0000438583" FT DOMAIN 3..76 FT /note="DWNN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00612" FT ZN_FING 203..216 FT /note="CCHC-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047" FT ZN_FING 288..326 FT /note="RING-type; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT MOTIF 668..675 FT /note="Nuclear localization signal 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768" FT MOTIF 695..702 FT /note="Nuclear localization signal 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768" FT COMPBIAS 493..550 FT /note="Gly-rich" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00008" FT COMPBIAS 654..711 FT /note="Arg-rich" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00002" FT MOD_RES 278 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:B9DFV2" FT MOD_RES 397 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:B9DFV2" FT MOD_RES 800 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:B9DFV2" FT VAR_SEQ 468 FT /note="Q -> QA (in isoform 2)" FT /id="VSP_058683" FT CONFLICT 776 FT /note="E -> G (in Ref. 4; BAE99012)" FT /evidence="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 //