SNC1_ARATH
ID SNC1_ARATH Reviewed; 1437 AA.
AC O23530;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 5.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1 {ECO:0000303|PubMed:14576290};
DE Short=AtSNC1 {ECO:0000303|PubMed:14576290};
DE AltName: Full=Disease resistance RPP5-like protein;
DE AltName: Full=Probable NAD(+) hydrolase SNC1;
DE EC=3.2.2.6 {ECO:0000305|PubMed:31439792};
GN Name=SNC1 {ECO:0000303|PubMed:14576290};
GN Synonyms=BAL {ECO:0000303|PubMed:17890374};
GN OrderedLocusNames=At4g16890 {ECO:0000312|Araport:AT4G16890};
GN ORFNames=dl4475c {ECO:0000312|EMBL:CAB46044.1},
GN FCAALL.51 {ECO:0000312|EMBL:CAB80960.1};
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH SRFR1.
RX PubMed=21079790; DOI=10.1371/journal.ppat.1001172;
RA Kim S.H., Gao F., Bhattacharjee S., Adiasor J.A., Nam J.C., Gassmann W.;
RT "The Arabidopsis resistance-like gene SNC1 is activated by mutations in
RT SRFR1 and contributes to resistance to the bacterial effector AvrRps4.";
RL PLoS Pathog. 6:E1001172-E1001172(2010).
RN [2]
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 [3]
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 [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 FUNCTION, AND MUTAGENESIS OF GLU-561.
RX PubMed=14576290; DOI=10.1105/tpc.015842;
RA Zhang Y., Goritschnig S., Dong X., Li X.;
RT "A gain-of-function mutation in a plant disease resistance gene leads to
RT constitutive activation of downstream signal transduction pathways in
RT suppressor of npr1-1, constitutive 1.";
RL Plant Cell 15:2636-2646(2003).
RN [6]
RP IDENTIFICATION, REGULATION, AND INDUCTION BY SALICYLIC ACID AND HEAT.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, cv. No-0, and cv. Wassilewskija;
RX PubMed=15031411; DOI=10.1105/tpc.020479;
RA Yang S., Hua J.;
RT "A haplotype-specific Resistance gene regulated by BONZAI1 mediates
RT temperature-dependent growth control in Arabidopsis.";
RL Plant Cell 16:1060-1071(2004).
RN [7]
RP REGULATION.
RX PubMed=17977156; DOI=10.1094/mpmi-20-11-1449;
RA Li Y., Yang S., Yang H., Hua J.;
RT "The TIR-NB-LRR gene SNC1 is regulated at the transcript level by multiple
RT factors.";
RL Mol. Plant Microbe Interact. 20:1449-1456(2007).
RN [8]
RP REGULATION BY SILENCING.
RX PubMed=17890374; DOI=10.1105/tpc.107.051821;
RA Yi H., Richards E.J.;
RT "A cluster of disease resistance genes in Arabidopsis is coordinately
RT regulated by transcriptional activation and RNA silencing.";
RL Plant Cell 19:2929-2939(2007).
RN [9]
RP REGULATION.
RX PubMed=19797048; DOI=10.1534/genetics.109.105569;
RA Yi H., Richards E.J.;
RT "Gene duplication and hypermutation of the pathogen Resistance gene SNC1 in
RT the Arabidopsis bal variant.";
RL Genetics 183:1227-1234(2009).
RN [10]
RP INTERACTION WITH MORC1/CRT1.
RX PubMed=20332379; DOI=10.1105/tpc.109.071662;
RA Kang H.-G., Oh C.-S., Sato M., Katagiri F., Glazebrook J., Takahashi H.,
RA Kachroo P., Martin G.B., Klessig D.F.;
RT "Endosome-associated CRT1 functions early in resistance gene-mediated
RT defense signaling in Arabidopsis and tobacco.";
RL Plant Cell 22:918-936(2010).
RN [11]
RP FUNCTION, AND INTERACTION WITH TPR1.
RX PubMed=20647385; DOI=10.1073/pnas.1002828107;
RA Zhu Z., Xu F., Zhang Y., Cheng Y.T., Wiermer M., Li X., Zhang Y.;
RT "Arabidopsis resistance protein SNC1 activates immune responses through
RT association with a transcriptional corepressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13960-13965(2010).
RN [12]
RP REGULATION.
RX PubMed=20439546; DOI=10.1104/pp.110.156240;
RA Li Y., Tessaro M.J., Li X., Zhang Y.;
RT "Regulation of the expression of plant Resistance gene SNC1 by a protein
RT with a conserved BAT2 domain.";
RL Plant Physiol. 153:1425-1434(2010).
RN [13]
RP INTERACTION WITH EDS1.
RX PubMed=22158819; DOI=10.1126/science.1211592;
RA Bhattacharjee S., Halane M.K., Kim S.H., Gassmann W.;
RT "Pathogen effectors target Arabidopsis EDS1 and alter its interactions with
RT immune regulators.";
RL Science 334:1405-1408(2011).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22454454; DOI=10.1105/tpc.112.096198;
RA Mang H.G., Qian W., Zhu Y., Qian J., Kang H.G., Klessig D.F., Hua J.;
RT "Abscisic acid deficiency antagonizes high-temperature inhibition of
RT disease resistance through enhancing nuclear accumulation of resistance
RT proteins SNC1 and RPS4 in Arabidopsis.";
RL Plant Cell 24:1271-1284(2012).
RN [15]
RP MISCELLANEOUS.
RX PubMed=22248079; DOI=10.1111/j.1365-313x.2012.04906.x;
RA Xu F., Xu S., Wiermer M., Zhang Y., Li X.;
RT "The cyclin L homolog MOS12 and the MOS4-associated complex are required
RT for the proper splicing of plant resistance genes.";
RL Plant J. 70:916-928(2012).
RN [16]
RP MISCELLANEOUS.
RX PubMed=23803746; DOI=10.4161/psb.25372;
RA Copeland C., Xu S., Qi Y., Li X.;
RT "MOS2 has redundant function with its homolog MOS2H and is required for
RT proper splicing of SNC1.";
RL Plant Signal. Behav. 8:E253720-E253720(2013).
RN [17]
RP INTERACTION WITH HSP90-3.
RX PubMed=24889324; DOI=10.1111/tpj.12573;
RA Huang S., Monaghan J., Zhong X., Lin L., Sun T., Dong O.X., Li X.;
RT "HSP90s are required for NLR immune receptor accumulation in Arabidopsis.";
RL Plant J. 79:427-439(2014).
RN [18]
RP PARTIAL PROTEIN SEQUENCE (ISOFORMS 1 AND 2), ALTERNATIVE INITIATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT MET-1, AND ACETYLATION
RP AT MET-1 (ISOFORM 2).
RX PubMed=25966763; DOI=10.1105/tpc.15.00173;
RA Xu F., Huang Y., Li L., Gannon P., Linster E., Huber M., Kapos P.,
RA Bienvenut W., Polevoda B., Meinnel T., Hell R., Giglione C., Zhang Y.,
RA Wirtz M., Chen S., Li X.;
RT "Two N-terminal acetyltransferases antagonistically regulate the stability
RT of a nod-like receptor in Arabidopsis.";
RL Plant Cell 27:1547-1562(2015).
RN [19]
RP INTERACTION WITH TRAF1B.
RX PubMed=26867179; DOI=10.1016/j.chom.2016.01.005;
RA Huang S., Chen X., Zhong X., Li M., Ao K., Huang J., Li X.;
RT "Plant TRAF proteins regulate NLR immune receptor turnover.";
RL Cell Host Microbe 19:204-215(2016).
RN [20]
RP DISRUPTION PHENOTYPE, AND REPRESSION BY ZED1.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=28499073; DOI=10.1111/nph.14585;
RA Wang Z., Cui D., Liu J., Zhao J., Liu C., Xin W., Li Y., Liu N., Ren D.,
RA Tang D., Hu Y.;
RT "Arabidopsis ZED1-related kinases mediate the temperature-sensitive
RT intersection of immune response and growth homeostasis.";
RL New Phytol. 215:711-724(2017).
RN [21]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31439792; DOI=10.1126/science.aax1911;
RA Horsefield S., Burdett H., Zhang X., Manik M.K., Shi Y., Chen J., Qi T.,
RA Gilley J., Lai J.S., Rank M.X., Casey L.W., Gu W., Ericsson D.J., Foley G.,
RA Hughes R.O., Bosanac T., von Itzstein M., Rathjen J.P., Nanson J.D.,
RA Boden M., Dry I.B., Williams S.J., Staskawicz B.J., Coleman M.P., Ve T.,
RA Dodds P.N., Kobe B.;
RT "NAD+ cleavage activity by animal and plant TIR domains in cell death
RT pathways.";
RL Science 365:793-799(2019).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 17-190, AND SUBUNIT.
RX PubMed=27818198; DOI=10.1016/j.bbrc.2016.11.004;
RA Hyun K.G., Lee Y., Yoon J., Yi H., Song J.J.;
RT "Crystal structure of Arabidopsis thaliana SNC1 TIR domain.";
RL Biochem. Biophys. Res. Commun. 481:146-152(2016).
CC -!- FUNCTION: Disease resistance protein of the TIR-NB-LRR-type
CC (PubMed:14576290). Part of the RPP5 locus that contains a cluster of
CC several paralogous disease resistance (R) genes (PubMed:14576290).
CC Resistance proteins guard the plant against pathogens that contain an
CC appropriate avirulence protein via an indirect interaction with this
CC avirulence protein (PubMed:14576290). That triggers a defense system
CC including the hypersensitive response, which restricts the pathogen
CC growth (PubMed:14576290). Probably acts as a NAD(+) hydrolase (NADase):
CC in response to activation, catalyzes cleavage of NAD(+) into ADP-D-
CC ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense
CC system that promotes cell death (PubMed:31439792). Expression regulated
CC by MOS1 at chromatin level (PubMed:20647385). Nuclear localization of
CC SNC1 is essential for its activity (PubMed:22454454). ABA deficiency
CC can rescue high-temperature inhibition of SNC1-mediated defense
CC responses (PubMed:22454454). {ECO:0000269|PubMed:14576290,
CC ECO:0000269|PubMed:20647385, ECO:0000269|PubMed:22454454,
CC ECO:0000269|PubMed:31439792}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000305|PubMed:31439792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000305|PubMed:31439792};
CC -!- SUBUNIT: Homodimer (PubMed:27818198). Interacts (via TIR domain) with
CC TPR1 (PubMed:20647385). Interacts with EDS1 (PubMed:22158819).
CC Interacts with SRFR1 (PubMed:21079790). Interacts with HSP90-3
CC (PubMed:24889324). Binds to MORC1/CRT1 (PubMed:20332379). Interacts
CC with TRAF1B (PubMed:26867179). {ECO:0000269|PubMed:20332379,
CC ECO:0000269|PubMed:20647385, ECO:0000269|PubMed:21079790,
CC ECO:0000269|PubMed:22158819, ECO:0000269|PubMed:24889324,
CC ECO:0000269|PubMed:26867179, ECO:0000269|PubMed:27818198}.
CC -!- INTERACTION:
CC O23530; Q9SU30: CPR1; NbExp=2; IntAct=EBI-15866586, EBI-15941797;
CC O23530; Q0WV90: TPR1; NbExp=2; IntAct=EBI-15866586, EBI-15866619;
CC O23530; P59263: UBQ16; NbExp=2; IntAct=EBI-15866586, EBI-1541543;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21079790}.
CC Microsome {ECO:0000269|PubMed:21079790}. Nucleus
CC {ECO:0000269|PubMed:21079790, ECO:0000269|PubMed:22454454}.
CC Note=Restricted to microsomes when interacting with SRFR1. Accumulates
CC in nucleus at 22 degrees Celsius, but not at 28 degrees Celsius.
CC Nuclear accumulation is enhanced by abscisic acid deficiency.
CC {ECO:0000269|PubMed:21079790, ECO:0000269|PubMed:22454454}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=2;
CC IsoId=O23530-2; Sequence=Displayed;
CC Name=1;
CC IsoId=O23530-1; Sequence=VSP_057982;
CC -!- TISSUE SPECIFICITY: Expressed in guard cells and epidermal cells, but
CC not detected in mesophyll cells. {ECO:0000269|PubMed:22454454}.
CC -!- INDUCTION: Up-regulated by salicylic acid and in mutants defective in
CC RNA silencing. Down-regulated by high temperature. Repressed by ZED1 in
CC the absence of pathogens in an ambient temperature-sensitive manner
CC (PubMed:28499073). {ECO:0000269|PubMed:15031411,
CC ECO:0000269|PubMed:28499073}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- PTM: [Isoform 2]: Met-1 is specifically acetylated by N-terminal
CC acetyltransferase complex A (NatA). The NatA-mediated acetylation
CC serves as a degradation signal. {ECO:0000269|PubMed:25966763}.
CC -!- PTM: [Isoform 1]: Met-1 is specifically acetylated by N-terminal
CC acetyltransferase complex B (NatB). The NatB-mediated acetylation
CC stabilizes SNC1. {ECO:0000269|PubMed:25966763}.
CC -!- DISRUPTION PHENOTYPE: Impaired disease resistance responses.
CC {ECO:0000269|PubMed:28499073}.
CC -!- MISCELLANEOUS: A gain-of-function mutant in SNC1 resulting from a point
CC mutation leads to a dwarf and curled-leaf phenotype and a constitutive
CC disease resistance in the absence of cell death.
CC -!- MISCELLANEOUS: The phenotypically unstable bal phenotype is caused by a
CC duplication of the locus carrying SNC1 followed by a hypermutation of
CC the gene.
CC -!- MISCELLANEOUS: SNC1 is not found in cv. Landsberg erecta, cv. No-0, and
CC cv. Wassilewskija and is probably unique to cv. Columbia
CC (PubMed:15031411). Cv. RLD encodes a non-functional truncated SNC1
CC protein lacking most of the LRR domain (PubMed:21079790).
CC -!- MISCELLANEOUS: MOS2, MOS2H, MOS12 and the MOS4-associated complex (MAC)
CC are required for the proper splicing of R genes and contribute in the
CC alternative splicing of SNC1. {ECO:0000269|PubMed:22248079,
CC ECO:0000269|PubMed:23803746}.
CC -!- SIMILARITY: Belongs to the disease resistance TIR-NB-LRR family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB46044.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80960.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97342; CAB46044.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161545; CAB80960.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83820.2; -; Genomic_DNA.
DR PIR; D85188; D85188.
DR PIR; H71436; H71436.
DR RefSeq; NP_001319970.1; NM_001341145.1. [O23530-2]
DR PDB; 5H3C; X-ray; 2.60 A; A/B=17-190.
DR PDB; 5TEC; X-ray; 2.20 A; A/B=17-190.
DR PDBsum; 5H3C; -.
DR PDBsum; 5TEC; -.
DR AlphaFoldDB; O23530; -.
DR SMR; O23530; -.
DR BioGRID; 12690; 6.
DR DIP; DIP-59360N; -.
DR IntAct; O23530; 3.
DR STRING; 3702.AT4G16890.1; -.
DR iPTMnet; O23530; -.
DR PaxDb; O23530; -.
DR PRIDE; O23530; -.
DR ProteomicsDB; 232546; -. [O23530-2]
DR EnsemblPlants; AT4G16890.1; AT4G16890.1; AT4G16890. [O23530-2]
DR GeneID; 827397; -.
DR Gramene; AT4G16890.1; AT4G16890.1; AT4G16890. [O23530-2]
DR KEGG; ath:AT4G16890; -.
DR Araport; AT4G16890; -.
DR TAIR; locus:2129236; AT4G16890.
DR eggNOG; ENOG502QQJE; Eukaryota.
DR HOGENOM; CLU_001561_0_1_1; -.
DR InParanoid; O23530; -.
DR OrthoDB; 1282076at2759; -.
DR PRO; PR:O23530; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23530; baseline and differential.
DR Genevisible; O23530; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; ISS:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IGI:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:TAIR.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR045344; C-JID.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR011713; Leu-rich_rpt_3.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11017; PTHR11017; 6.
DR Pfam; PF20160; C-JID; 1.
DR Pfam; PF07725; LRR_3; 2.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Hydrolase;
KW Leucine-rich repeat; Microsome; NAD; Nucleotide-binding; Nucleus;
KW Plant defense; Reference proteome; Repeat.
FT CHAIN 1..1437
FT /note="Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1"
FT /id="PRO_0000399467"
FT DOMAIN 19..182
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REPEAT 554..576
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 577..598
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 600..621
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 622..645
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 647..668
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 670..691
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 692..715
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 781..805
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 807..828
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 829..851
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 852..875
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 877..895
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 897..918
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 919..939
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 940..962
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 964..985
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 1009..1029
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 1030..1052
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 1054..1075
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 1076..1096
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 1097..1121
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 1123..1143
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 1161..1185
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT ACT_SITE 93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 28..33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:25966763"
FT VAR_SEQ 1
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_057982"
FT MUTAGEN 561
FT /note="E->K: In snc1; constitutive disease resistance."
FT /evidence="ECO:0000269|PubMed:14576290"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:5TEC"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:5TEC"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:5TEC"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:5TEC"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:5TEC"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:5TEC"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:5TEC"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5TEC"
FT HELIX 88..104
FT /evidence="ECO:0007829|PDB:5TEC"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:5TEC"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:5TEC"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:5TEC"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:5TEC"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:5TEC"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:5TEC"
FT MOD_RES O23530-1:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:25966763"
SQ SEQUENCE 1437 AA; 162713 MW; E1DFAC43DAD04058 CRC64;
MMDTSKDDDM EIASSSGSRR YDVFPSFRGE DVRDSFLSHL LKELRGKAIT FIDDEIERSR
SIGPELLSAI KESRIAIVIF SKNYASSTWC LNELVEIHKC YTNLNQMVIP IFFHVDASEV
KKQTGEFGKV FEETCKAKSE DEKQSWKQAL AAVAVMAGYD LRKWPSEAAM IEELAEDVLR
KTMTPSDDFG DLVGIENHIE AIKSVLCLES KEARIMVGIW GQSGIGKSTI GRALYSKLSI
QFHHRAFITY KSTSGSDVSG MKLRWEKELL SEILGQKDIK IEHFGVVEQR LKQQKVLILL
DDVDSLEFLK TLVGKAEWFG SGSRIIVITQ DRQLLKAHEI DLIYEVEFPS EHLALTMLCR
SAFGKDSPPD DFKELAFEVA KLAGNLPLGL SVLGSSLKGR TKEWWMEMMP RLRNGLNGDI
MKTLRVSYDR LHQKDQDMFL YIACLFNGFE VSYVKDLLKD NVGFTMLTEK SLIRITPDGY
IEMHNLLEKL GREIDRAKSK GNPGKRRFLT NFEDIHEVVT EKTGTETLLG IRLPFEEYFS
TRPLLIDKES FKGMRNLQYL EIGYYGDLPQ SLVYLPLKLR LLDWDDCPLK SLPSTFKAEY
LVNLIMKYSK LEKLWEGTLP LGSLKEMNLR YSNNLKEIPD LSLAINLEEL DLVGCKSLVT
LPSSIQNATK LIYLDMSDCK KLESFPTDLN LESLEYLNLT GCPNLRNFPA IKMGCSDVDF
PEGRNEIVVE DCFWNKNLPA GLDYLDCLTR CMPCEFRPEQ LAFLNVRGYK HEKLWEGIQS
LGSLEGMDLS ESENLTEIPD LSKATKLESL ILNNCKSLVT LPSTIGNLHR LVRLEMKECT
GLEVLPTDVN LSSLETLDLS GCSSLRSFPL ISTNIVWLYL ENTAIEEIPS TIGNLHRLVR
LEMKKCTGLE VLPTDVNLSS LETLDLSGCS SLRSFPLISE SIKWLYLENT AIEEIPDLSK
ATNLKNLKLN NCKSLVTLPT TIGNLQKLVS FEMKECTGLE VLPIDVNLSS LMILDLSGCS
SLRTFPLIST NIVWLYLENT AIEEIPSTIG NLHRLVKLEM KECTGLEVLP TDVNLSSLMI
LDLSGCSSLR TFPLISTRIE CLYLQNTAIE EVPCCIEDFT RLTVLMMYCC QRLKTISPNI
FRLTRLELAD FTDCRGVIKA LSDATVVATM EDHVSCVPLS ENIEYIWDKL YRVAYLQEHF
SFRNCFKLDR DARELILRSC FKPVALPGEE IPKYFTYRAY GDSLTVIVPQ SSLSQNFLRF
KACVVVEPLS KGKGFYPFLK VNVGFNGKQY QKSFSKDAEL ELCKTDHLFF CSFKFRSEDL
PSKLNFNDVE FKFCCSNRIK ECGVRLMYVS QEENNQQTTR SEKRMRMTSG TSEEDINLPY
GLIVADTGLA ALNMELSLGQ GEPSSSTSLE GEALCVDYMI TEEQDKGIPI LFPVSGN
