NPR4_ARATH
ID NPR4_ARATH Reviewed; 574 AA.
AC Q5ICL9; O81848;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Regulatory protein NPR4;
DE AltName: Full=BTB/POZ domain-containing protein NPR4;
GN Name=NPR4; OrderedLocusNames=At4g19660; ORFNames=T16H5.20;
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 [MRNA], GENE FAMILY, NOMENCLATURE, FUNCTION, DISRUPTION
RP PHENOTYPE, INDUCTION, SUBCELLULAR LOCATION, INTERACTION WITH TGA FACTORS,
RP AND MUTAGENESIS OF HIS-321.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15634206; DOI=10.1111/j.1365-313x.2004.02296.x;
RA Liu G., Holub E.B., Alonso J.M., Ecker J.R., Fobert P.R.;
RT "An Arabidopsis NPR1-like gene, NPR4, is required for disease resistance.";
RL Plant J. 41:304-318(2005).
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 DOMAIN BTB.
RX PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA Vierstra R.D.;
RT "Cullins 3a and 3b assemble with members of the broad
RT complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL J. Biol. Chem. 280:18810-18821(2005).
RN [5]
RP FUNCTION, INDUCTION, AND INTERACTION WITH TGA FACTORS.
RX PubMed=17076807; DOI=10.1111/j.1365-313x.2006.02903.x;
RA Zhang Y., Cheng Y.T., Qu N., Zhao Q., Bi D., Li X.;
RT "Negative regulation of defense responses in Arabidopsis by two NPR1
RT paralogs.";
RL Plant J. 48:647-656(2006).
CC -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). Involved in the regulation of basal defense
CC responses against pathogens, and may be implicated in the cross-talk
CC between the SA- and JA-dependent signaling pathways. {ECO:0000250,
CC ECO:0000269|PubMed:15634206, ECO:0000269|PubMed:17076807}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with TGA2, TGA3, TGA5, TGA6 and TGA7.
CC {ECO:0000269|PubMed:15634206, ECO:0000269|PubMed:17076807}.
CC -!- INTERACTION:
CC Q5ICL9; Q8VZE5: At1g05410; NbExp=3; IntAct=EBI-1392093, EBI-4425726;
CC Q5ICL9; F4IDX2: At1g12810; NbExp=3; IntAct=EBI-1392093, EBI-25529516;
CC Q5ICL9; Q0WLB5: CHC2; NbExp=3; IntAct=EBI-1392093, EBI-4412194;
CC Q5ICL9; F4JRR1: COG2; NbExp=3; IntAct=EBI-1392093, EBI-4429018;
CC Q5ICL9; Q9SCK1: LSU1; NbExp=3; IntAct=EBI-1392093, EBI-4424157;
CC Q5ICL9; Q9FIR9: LSU2; NbExp=3; IntAct=EBI-1392093, EBI-4424076;
CC Q5ICL9; O64471: MTX1; NbExp=3; IntAct=EBI-1392093, EBI-2123898;
CC Q5ICL9; Q9FNH6: NHL3; NbExp=3; IntAct=EBI-1392093, EBI-4461284;
CC Q5ICL9; P93002: NPR1; NbExp=3; IntAct=EBI-1392093, EBI-1392127;
CC Q5ICL9; Q8L746: NPR3; NbExp=5; IntAct=EBI-1392093, EBI-4441365;
CC Q5ICL9; Q5ICL9: NPR4; NbExp=2; IntAct=EBI-1392093, EBI-1392093;
CC Q5ICL9; Q9FMS4: SIED1; NbExp=3; IntAct=EBI-1392093, EBI-25529548;
CC Q5ICL9; P25269: TSB2; NbExp=3; IntAct=EBI-1392093, EBI-25529585;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15634206}.
CC -!- INDUCTION: Up-regulated following pathogen challenge or salicylic acid
CC (SA) treatment, and down-regulated by methyl jasmonic acid (MeJA)
CC treatment. {ECO:0000269|PubMed:15634206, ECO:0000269|PubMed:17076807}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- DISRUPTION PHENOTYPE: Enhanced susceptibility to the virulent bacterial
CC pathogen Pseudomonas syringe and to the fungal pathogen Erysiphe
CC cichoracearum (powdery mildew). {ECO:0000269|PubMed:15634206}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA19683.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78968.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY785951; AAW31628.1; -; mRNA.
DR EMBL; AL024486; CAA19683.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161551; CAB78968.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84211.1; -; Genomic_DNA.
DR PIR; T04747; T04747.
DR RefSeq; NP_001328027.1; NM_001341366.1.
DR RefSeq; NP_193701.2; NM_118086.3.
DR PDB; 6WPG; X-ray; 2.28 A; A/B=373-516.
DR PDBsum; 6WPG; -.
DR AlphaFoldDB; Q5ICL9; -.
DR SMR; Q5ICL9; -.
DR BioGRID; 13003; 16.
DR DIP; DIP-40035N; -.
DR IntAct; Q5ICL9; 18.
DR STRING; 3702.AT4G19660.1; -.
DR PaxDb; Q5ICL9; -.
DR PRIDE; Q5ICL9; -.
DR ProteomicsDB; 251071; -.
DR EnsemblPlants; AT4G19660.1; AT4G19660.1; AT4G19660.
DR GeneID; 827710; -.
DR Gramene; AT4G19660.1; AT4G19660.1; AT4G19660.
DR KEGG; ath:AT4G19660; -.
DR Araport; AT4G19660; -.
DR TAIR; locus:2133925; AT4G19660.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_034895_1_0_1; -.
DR InParanoid; Q5ICL9; -.
DR OMA; MSHPEKG; -.
DR OrthoDB; 631377at2759; -.
DR PhylomeDB; Q5ICL9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5ICL9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5ICL9; baseline and differential.
DR Genevisible; Q5ICL9; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1901149; F:salicylic acid binding; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IGI:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR044292; NPR.
DR InterPro; IPR021094; NPR1/NIM1-like_C.
DR InterPro; IPR024228; NPR_central_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR46475; PTHR46475; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF11900; DUF3420; 1.
DR Pfam; PF12313; NPR1_like_C; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..574
FT /note="Regulatory protein NPR4"
FT /id="PRO_0000407993"
FT DOMAIN 54..130
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 252..280
FT /note="ANK 1"
FT REPEAT 281..311
FT /note="ANK 2"
FT REPEAT 315..344
FT /note="ANK 3"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P93002"
FT MUTAGEN 321
FT /note="H->Y: Abolishes interaction with TGA2 or with TGA7."
FT /evidence="ECO:0000269|PubMed:15634206"
FT HELIX 373..389
FT /evidence="ECO:0007829|PDB:6WPG"
FT HELIX 409..426
FT /evidence="ECO:0007829|PDB:6WPG"
FT HELIX 428..438
FT /evidence="ECO:0007829|PDB:6WPG"
FT HELIX 471..495
FT /evidence="ECO:0007829|PDB:6WPG"
FT HELIX 497..508
FT /evidence="ECO:0007829|PDB:6WPG"
SQ SEQUENCE 574 AA; 65115 MW; 11DCA45A220A7F46 CRC64;
MAATAIEPSS SISFTSSHLS NPSPVVTTYH SAANLEELSS NLEQLLTNPD CDYTDAEIII
EEEANPVSVH RCVLAARSKF FLDLFKKDKD SSEKKPKYQM KDLLPYGNVG REAFLHFLSY
IYTGRLKPFP IEVSTCVDSV CAHDSCKPAI DFAVELMYAS FVFQIPDLVS SFQRKLRNYV
EKSLVENVLP ILLVAFHCDL TQLLDQCIER VARSDLDRFC IEKELPLEVL EKIKQLRVKS
VNIPEVEDKS IERTGKVLKA LDSDDVELVK LLLTESDITL DQANGLHYAV AYSDPKVVTQ
VLDLDMADVN FRNSRGYTVL HIAAMRREPT IIIPLIQKGA NASDFTFDGR SAVNICRRLT
RPKDYHTKTS RKEPSKYRLC IDILEREIRR NPLVSGDTPT CSHSMPEDLQ MRLLYLEKRV
GLAQLFFPAE ANVAMDVANV EGTSECTGLL TPPPSNDTTE NLGKVDLNET PYVQTKRMLT
RMKALMKTVE TGRRYFPSCY EVLDKYMDQY MDEEIPDMSY PEKGTVKERR QKRMRYNELK
NDVKKAYSKD KVARSCLSSS SPASSLREAL ENPT
