PQT3_ARATH
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 25-MAY-2022, entry version 76.
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};
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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 AlphaFoldDB; F4JP52; -.
DR SMR; F4JP52; -.
DR STRING; 3702.AT4G17410.3; -.
DR iPTMnet; F4JP52; -.
DR PRIDE; F4JP52; -.
DR ProteomicsDB; 234840; -. [F4JP52-1]
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; RSKGERW; -.
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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 REGION 356..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 381..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
