NPR1_ARATH
ID NPR1_ARATH Reviewed; 593 AA.
AC P93002; O04742;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Regulatory protein NPR1;
DE AltName: Full=BTB/POZ domain-containing protein NPR1;
DE AltName: Full=Non-inducible immunity protein 1;
DE Short=Nim1;
DE AltName: Full=Nonexpresser of PR genes 1;
DE AltName: Full=Salicylic acid insensitive 1;
DE Short=Sai1;
GN Name=NPR1; Synonyms=NIM1, SAI1; OrderedLocusNames=At1g64280;
GN ORFNames=F15H21.6;
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], FUNCTION, AND MUTANTS NPR1-1 AND NPR1-2.
RC STRAIN=cv. Columbia;
RX PubMed=9019406; DOI=10.1016/s0092-8674(00)81858-9;
RA Cao H., Glazebrook J., Clarke J.D., Volko S., Dong X.;
RT "The Arabidopsis NPR1 gene that controls systemic acquired resistance
RT encodes a novel protein containing ankyrin repeats.";
RL Cell 88:57-63(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-93; THR-96; ALA-108 DEL;
RP TRP-268 AND PRO-406, AND MUTANTS NIM1-2; NIM1-4 AND NIM1-5.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=9090885; DOI=10.2307/3870492;
RA Ryals J., Weymann K., Lawton K., Friedrich L., Ellis D., Steiner H.-Y.,
RA Johnson J., Delaney T.P., Jesse T., Vos P., Uknes S.;
RT "The Arabidopsis NIM1 protein shows homology to the mammalian transcription
RT factor inhibitor I kappa B.";
RL Plant Cell 9:425-439(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION.
RX PubMed=11607555; DOI=10.1073/pnas.92.14.6602;
RA Delaney T.P., Friedrich L., Ryals J.A.;
RT "Arabidopsis signal transduction mutant defective in chemically and
RT biologically induced disease resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6602-6606(1995).
RN [7]
RP FUNCTION.
RX PubMed=9002272; DOI=10.1094/mpmi.1997.10.1.69;
RA Shah J., Tsui F., Klessig D.F.;
RT "Characterization of a salicylic acid-insensitive mutant (sai1) of
RT Arabidopsis thaliana, identified in a selective screen utilizing the SA-
RT inducible expression of the tms2 gene.";
RL Mol. Plant Microbe Interact. 10:69-78(1997).
RN [8]
RP INTERACTION WITH TGA FACTORS.
RX PubMed=10659709; DOI=10.1094/mpmi.2000.13.2.191;
RA Zhou J.-M., Trifa Y., Silva H., Pontier D., Lam E., Shah J., Klessig D.F.;
RT "NPR1 differentially interacts with members of the TGA/OBF family of
RT transcription factors that bind an element of the PR-1 gene required for
RT induction by salicylic acid.";
RL Mol. Plant Microbe Interact. 13:191-202(2000).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TGA FACTORS.
RX PubMed=10662863; DOI=10.2307/3870928;
RA Despres C., DeLong C., Glaze S., Liu E., Fobert P.R.;
RT "The Arabidopsis NPR1/NIM1 protein enhances the DNA binding activity of a
RT subgroup of the TGA family of bZIP transcription factors.";
RL Plant Cell 12:279-290(2000).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=11148282; DOI=10.2307/3871233;
RA Kinkema M., Fan W., Dong X.;
RT "Nuclear localization of NPR1 is required for activation of PR gene
RT expression.";
RL Plant Cell 12:2339-2350(2000).
RN [11]
RP INTERACTION WITH NIMIN-1; NIMIN-2 AND NIMIN-3.
RX PubMed=11442055; DOI=10.1023/a:1010652620115;
RA Weigel R.R., Baeuscher C., Pfitzner A.J.P., Pfitzner U.M.;
RT "NIMIN-1, NIMIN-2 and NIMIN-3, members of a novel family of proteins from
RT Arabidopsis that interact with NPR1/NIM1, a key regulator of systemic
RT acquired resistance in plants.";
RL Plant Mol. Biol. 46:143-160(2001).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-82 AND CYS-216.
RX PubMed=12837250; DOI=10.1016/s0092-8674(03)00429-x;
RA Mou Z., Fan W., Dong X.;
RT "Inducers of plant systemic acquired resistance regulate NPR1 function
RT through redox changes.";
RL Cell 113:935-944(2003).
RN [13]
RP FUNCTION.
RX PubMed=12615947; DOI=10.1105/tpc.009159;
RA Spoel S.H., Koornneef A., Claessens S.M., Korzelius J.P., Van Pelt J.A.,
RA Mueller M.J., Buchala A.J., Metraux J.P., Brown R., Kazan K.,
RA Van Loon L.C., Dong X., Pieterse C.M.;
RT "NPR1 modulates cross-talk between salicylate- and jasmonate-dependent
RT defense pathways through a novel function in the cytosol.";
RL Plant Cell 15:760-770(2003).
RN [14]
RP FUNCTION.
RX PubMed=12897257; DOI=10.1105/tpc.012211;
RA Johnson C., Boden E., Arias J.;
RT "Salicylic acid and NPR1 induce the recruitment of trans-activating TGA
RT factors to a defense gene promoter in Arabidopsis.";
RL Plant Cell 15:1846-1858(2003).
RN [15]
RP FUNCTION, AND INTERACTION WITH TGA1 AND TGA4.
RX PubMed=12953119; DOI=10.1105/tpc.012849;
RA Despres C., Chubak C., Rochon A., Clark R., Bethune T., Desveaux D.,
RA Fobert P.R.;
RT "The Arabidopsis NPR1 disease resistance protein is a novel cofactor that
RT confers redox regulation of DNA binding activity to the basic
RT domain/leucine zipper transcription factor TGA1.";
RL Plant Cell 15:2181-2191(2003).
RN [16]
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 [17]
RP S-NITROSYLATION AT CYS-156.
RX PubMed=18635760; DOI=10.1126/science.1156970;
RA Tada Y., Spoel S.H., Pajerowska-Mukhtar K., Mou Z., Song J., Wang C.,
RA Zuo J., Dong X.;
RT "Plant immunity requires conformational changes of NPR1 via S-nitrosylation
RT and thioredoxins.";
RL Science 321:952-956(2008).
RN [18]
RP PHOSPHORYLATION AT SER-11 AND SER-15, MUTAGENESIS OF SER-11 AND SER-15,
RP UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
RX PubMed=19490895; DOI=10.1016/j.cell.2009.03.038;
RA Spoel S.H., Mou Z., Tada Y., Spivey N.W., Genschik P., Dong X.;
RT "Proteasome-mediated turnover of the transcription coactivator NPR1 plays
RT dual roles in regulating plant immunity.";
RL Cell 137:860-872(2009).
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). Key positive regulator of the SA-dependent
CC signaling pathway that negatively regulates JA-dependent signaling
CC pathway. Mediates the binding of TGA factors to the as-1 motif found in
CC the pathogenesis-related PR-1 gene, leading to the transcriptional
CC regulation of the gene defense. Controls the onset of systemic acquired
CC resistance (SAR). Upon SAR induction, a biphasic change in cellular
CC reduction potential occurs, resulting in reduction of the cytoplasmic
CC oligomeric form to a monomeric form that accumulates in the nucleus and
CC activates gene expression. Phosphorylated form is target of proteasome
CC degradation. {ECO:0000250, ECO:0000269|PubMed:11607555,
CC ECO:0000269|PubMed:12615947, ECO:0000269|PubMed:12837250,
CC ECO:0000269|PubMed:12897257, ECO:0000269|PubMed:12953119,
CC ECO:0000269|PubMed:9002272, ECO:0000269|PubMed:9019406}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Oligomer in an uninduced state; disulfide-linked. Forms
CC activated monomer upon SAR induction. Interacts with TGA1, TGA3, TGA4,
CC TGA5, TGA6, TGA7 and with reduced forms of TGA1 and TGA4. Interacts
CC with NIMIN-1, NIMIN-2 and NIMIN-3. {ECO:0000269|PubMed:10659709,
CC ECO:0000269|PubMed:10662863, ECO:0000269|PubMed:11442055,
CC ECO:0000269|PubMed:12953119}.
CC -!- INTERACTION:
CC P93002; Q9ZVH4: CUL3A; NbExp=3; IntAct=EBI-1392127, EBI-531362;
CC P93002; Q9FMI5: MHJ24.13; NbExp=3; IntAct=EBI-1392127, EBI-25518065;
CC P93002; Q9FNZ5: NIMIN-1; NbExp=4; IntAct=EBI-1392127, EBI-541099;
CC P93002; Q9LUA3: NIMIN-2; NbExp=5; IntAct=EBI-1392127, EBI-541107;
CC P93002; Q9FNZ4: NIMIN-3; NbExp=5; IntAct=EBI-1392127, EBI-541115;
CC P93002; Q9SZI3: NPR2; NbExp=2; IntAct=EBI-1392127, EBI-15987489;
CC P93002; Q8L746: NPR3; NbExp=2; IntAct=EBI-1392127, EBI-4441365;
CC P93002; Q5ICL9: NPR4; NbExp=3; IntAct=EBI-1392127, EBI-1392093;
CC P93002; Q93ZX1: RFC4; NbExp=3; IntAct=EBI-1392127, EBI-4470690;
CC P93002; Q39237: TGA1; NbExp=7; IntAct=EBI-1392127, EBI-541351;
CC P93002; P43273: TGA2; NbExp=12; IntAct=EBI-1392127, EBI-541307;
CC P93002; Q39234: TGA3; NbExp=9; IntAct=EBI-1392127, EBI-541366;
CC P93002; Q39163: TGA5; NbExp=8; IntAct=EBI-1392127, EBI-541381;
CC P93002; Q39140: TGA6; NbExp=5; IntAct=EBI-1392127, EBI-541321;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Accumulation in nucleus
CC after induction by salicylic acid (SA) treatment or after pathogen
CC infection.
CC -!- INDUCTION: By salicylic acid (SA), benzol(1,2,3)thiadiazole-7-
CC carbothioic acid S-methyl ester (BTH) and 2,6-dichloroisonicotinic acid
CC (INA).
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- PTM: Phosphorylated at Ser-11 and Ser-15 in the nucleus; facilitates
CC its recruitment to a cullin3-based ubiquitin ligase leading to
CC polyubiquitination and subsequent CUL3/CSN-mediated degradation.
CC {ECO:0000269|PubMed:19490895}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:19490895}.
CC -!- PTM: The Cys-82-SH group reacts with Cys-216-SH of the other subunit to
CC form an intermolecular disulfide. This disulfide might subsequently be
CC reduced upon SAR induction.
CC -!- PTM: S-nitrosylation at Cys-156 facilitates its oligomerization.
CC {ECO:0000269|PubMed:18635760}.
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DR EMBL; U76707; AAC49611.1; -; mRNA.
DR EMBL; U87794; AAB58262.1; -; Genomic_DNA.
DR EMBL; AC066689; AAG51705.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34220.1; -; Genomic_DNA.
DR EMBL; AY050455; AAK91469.1; -; mRNA.
DR EMBL; AY093992; AAM16253.1; -; mRNA.
DR PIR; F96666; F96666.
DR RefSeq; NP_176610.1; NM_105102.3.
DR PDB; 7MK2; EM; 3.80 A; A/B=1-593.
DR PDB; 7MK3; X-ray; 3.06 A; A/B=39-410.
DR PDB; 7TAC; EM; 3.60 A; A/B=1-593.
DR PDB; 7TAD; EM; 3.60 A; A/B=1-593.
DR PDBsum; 7MK2; -.
DR PDBsum; 7MK3; -.
DR PDBsum; 7TAC; -.
DR PDBsum; 7TAD; -.
DR AlphaFoldDB; P93002; -.
DR SMR; P93002; -.
DR BioGRID; 27954; 16.
DR ComplexPortal; CPX-3572; TGA2-NPR1 complex.
DR DIP; DIP-38585N; -.
DR IntAct; P93002; 21.
DR STRING; 3702.AT1G64280.1; -.
DR iPTMnet; P93002; -.
DR PaxDb; P93002; -.
DR PRIDE; P93002; -.
DR ProteomicsDB; 249048; -.
DR EnsemblPlants; AT1G64280.1; AT1G64280.1; AT1G64280.
DR GeneID; 842733; -.
DR Gramene; AT1G64280.1; AT1G64280.1; AT1G64280.
DR KEGG; ath:AT1G64280; -.
DR Araport; AT1G64280; -.
DR TAIR; locus:2014200; AT1G64280.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_034895_1_0_1; -.
DR InParanoid; P93002; -.
DR OMA; CADENCC; -.
DR OrthoDB; 342053at2759; -.
DR PhylomeDB; P93002; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P93002; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P93002; baseline and differential.
DR Genevisible; P93002; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0106167; P:extracellular ATP signaling; IMP:TAIR.
DR GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ComplexPortal.
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:0010112; P:regulation of systemic acquired resistance; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0080027; P:response to herbivore; IEA:EnsemblPlants.
DR GO; GO:0001666; P:response to hypoxia; IMP:TAIR.
DR GO; GO:0009625; P:response to insect; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IMP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IDA:ComplexPortal.
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; Cytoplasm; Disulfide bond;
KW Hypersensitive response; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Repeat; S-nitrosylation; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..593
FT /note="Regulatory protein NPR1"
FT /id="PRO_0000067063"
FT DOMAIN 65..144
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 265..295
FT /note="ANK 1"
FT REPEAT 297..324
FT /note="ANK 2"
FT REPEAT 328..357
FT /note="ANK 3"
FT REGION 563..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 537..554
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 563..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19490895"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19490895"
FT MOD_RES 156
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:18635760"
FT DISULFID 82
FT /note="Interchain (with C-216); in linked form"
FT DISULFID 216
FT /note="Interchain (with C-82); in linked form"
FT VARIANT 93
FT /note="S -> N (in strain: cv. Wassilewskija)"
FT /evidence="ECO:0000269|PubMed:9090885"
FT VARIANT 96
FT /note="A -> T (in strain: cv. Wassilewskija)"
FT /evidence="ECO:0000269|PubMed:9090885"
FT VARIANT 108
FT /note="Missing (in strain: cv. Wassilewskija)"
FT /evidence="ECO:0000269|PubMed:9090885"
FT VARIANT 268
FT /note="S -> W (in strain: cv. Wassilewskija)"
FT /evidence="ECO:0000269|PubMed:9090885"
FT VARIANT 406
FT /note="Q -> P (in strain: cv. Wassilewskija)"
FT /evidence="ECO:0000269|PubMed:9090885"
FT MUTAGEN 11
FT /note="S->A: Loss of ubiquitination and degradation; when
FT associated with A-15."
FT /evidence="ECO:0000269|PubMed:19490895"
FT MUTAGEN 15
FT /note="S->A: Loss of ubiquitination and degradation; when
FT associated with A-11."
FT /evidence="ECO:0000269|PubMed:19490895"
FT MUTAGEN 82
FT /note="C->A: Prevents oligomerization and leads to the
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:12837250"
FT MUTAGEN 150
FT /note="C->Y: In npr1-2; loss of SAR induction, loss of
FT expression of PR genes and increased susceptibility to
FT infections."
FT MUTAGEN 156
FT /note="C->A: Abolishes S-nitrosylation and
FT oligomerization."
FT MUTAGEN 216
FT /note="C->A: Prevents oligomerization and leads to the
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:12837250"
FT MUTAGEN 300
FT /note="H->Y: In nim1-2; no induction of SAR genes
FT expression or disease resistance."
FT MUTAGEN 334
FT /note="H->Y: In npr1-1; loss of SAR induction, loss of
FT expression of PR genes and increased susceptibility to
FT infections."
FT MUTAGEN 432
FT /note="R->K: In nim1-4 and nim1-5; no induction of SAR
FT genes expression or disease resistance."
SQ SEQUENCE 593 AA; 66032 MW; DDD618146254CD68 CRC64;
MDTTIDGFAD SYEISSTSFV ATDNTDSSIV YLAAEQVLTG PDVSALQLLS NSFESVFDSP
DDFYSDAKLV LSDGREVSFH RCVLSARSSF FKSALAAAKK EKDSNNTAAV KLELKEIAKD
YEVGFDSVVT VLAYVYSSRV RPPPKGVSEC ADENCCHVAC RPAVDFMLEV LYLAFIFKIP
ELITLYQRHL LDVVDKVVIE DTLVILKLAN ICGKACMKLL DRCKEIIVKS NVDMVSLEKS
LPEELVKEII DRRKELGLEV PKVKKHVSNV HKALDSDDIE LVKLLLKEDH TNLDDACALH
FAVAYCNVKT ATDLLKLDLA DVNHRNPRGY TVLHVAAMRK EPQLILSLLE KGASASEATL
EGRTALMIAK QATMAVECNN IPEQCKHSLK GRLCVEILEQ EDKREQIPRD VPPSFAVAAD
ELKMTLLDLE NRVALAQRLF PTEAQAAMEI AEMKGTCEFI VTSLEPDRLT GTKRTSPGVK
IAPFRILEEH QSRLKALSKT VELGKRFFPR CSAVLDQIMN CEDLTQLACG EDDTAEKRLQ
KKQRYMEIQE TLKKAFSEDN LELGNSSLTD STSSTSKSTG GKRSNRKLSH RRR
