NTL9_ARATH
ID NTL9_ARATH Reviewed; 512 AA.
AC F4JN35; O81790; Q93ZN0;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Protein NTM1-like 9 {ECO:0000303|PubMed:17158162};
DE AltName: Full=Calmodulin-binding NAC protein {ECO:0000303|PubMed:17947243};
GN Name=NTL9 {ECO:0000303|PubMed:17158162};
GN Synonyms=CBNAC {ECO:0000303|PubMed:17947243};
GN OrderedLocusNames=At4g35580 {ECO:0000312|Araport:AT4G35580};
GN ORFNames=F8D20.90 {ECO:0000312|EMBL:CAA20028.1};
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 313-512.
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 [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15029955; DOI=10.1093/dnares/10.6.239;
RA Ooka H., Satoh K., Doi K., Nagata T., Otomo Y., Murakami K., Matsubara K.,
RA Osato N., Kawai J., Carninci P., Hayashizaki Y., Suzuki K., Kojima K.,
RA Takahara Y., Yamamoto K., Kikuchi S.;
RT "Comprehensive analysis of NAC family genes in Oryza sativa and Arabidopsis
RT thaliana.";
RL DNA Res. 10:239-247(2003).
RN [5]
RP FUNCTION, INTERACTION WITH CALMODULIN, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF TRP-487; ALA-491 AND ALA-496.
RX PubMed=17947243; DOI=10.1074/jbc.m705217200;
RA Kim H.S., Park B.O., Yoo J.H., Jung M.S., Lee S.M., Han H.J., Kim K.E.,
RA Kim S.H., Lim C.O., Yun D.J., Lee S.Y., Chung W.S.;
RT "Identification of a calmodulin-binding NAC protein as a transcriptional
RT repressor in Arabidopsis.";
RL J. Biol. Chem. 282:36292-36302(2007).
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=17158162; DOI=10.1093/nar/gkl1068;
RA Kim S.Y., Kim S.G., Kim Y.S., Seo P.J., Bae M., Yoon H.K., Park C.M.;
RT "Exploring membrane-associated NAC transcription factors in Arabidopsis:
RT implications for membrane biology in genome regulation.";
RL Nucleic Acids Res. 35:203-213(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=18443413;
RA Yoon H.K., Kim S.G., Kim S.Y., Park C.M.;
RT "Regulation of leaf senescence by NTL9-mediated osmotic stress signaling in
RT Arabidopsis.";
RL Mol. Cells 25:438-445(2008).
RN [8]
RP FUNCTION, INTERACTION WITH SNI1, AND DISRUPTION PHENOTYPE.
RX PubMed=22826500; DOI=10.1093/nar/gks683;
RA Kim H.S., Park H.C., Kim K.E., Jung M.S., Han H.J., Kim S.H., Kwon Y.S.,
RA Bahk S., An J., Bae D.W., Yun D.-J., Kwak S.-S., Chung W.S.;
RT "A NAC transcription factor and SNI1 cooperatively suppress basal pathogen
RT resistance in Arabidopsis thaliana.";
RL Nucleic Acids Res. 40:9182-9192(2012).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24329768; DOI=10.1111/nph.12626;
RA Block A., Toruno T.Y., Elowsky C.G., Zhang C., Steinbrenner J., Beynon J.,
RA Alfano J.R.;
RT "The Pseudomonas syringae type III effector HopD1 suppresses effector-
RT triggered immunity, localizes to the endoplasmic reticulum, and targets the
RT Arabidopsis transcription factor NTL9.";
RL New Phytol. 201:1358-1370(2014).
CC -!- FUNCTION: Transcriptional activator activated by proteolytic cleavage
CC through regulated intramembrane proteolysis (RIP) (PubMed:18443413,
CC PubMed:24329768). Calmodulin-regulated transcriptional repressor. Binds
CC several synthetic promoters with randomly selected binding sites
CC (PubMed:17947243). Functions synergistically with SNI1 as negative
CC regulator of pathogen-induced PR1 expression and basal resistance to a
CC virulent strain of P.syringae. Binds directly to the promoter of the
CC PR1 gene (PubMed:22826500). Acts as positive regulator of innate
CC immunity. Involved in the effector-triggered immunity (ETI) induction
CC of immunity-related gene expression (PubMed:24329768). Mediates osmotic
CC stress signaling in leaf senescence by up-regulating senescence-
CC associated genes (PubMed:18443413). {ECO:0000269|PubMed:17947243,
CC ECO:0000269|PubMed:18443413, ECO:0000269|PubMed:22826500,
CC ECO:0000269|PubMed:24329768}.
CC -!- SUBUNIT: Interacts with calmodulin (CaM) (PubMed:17947243). Interacts
CC with SNI1 (PubMed:22826500). {ECO:0000269|PubMed:17947243,
CC ECO:0000269|PubMed:22826500}.
CC -!- INTERACTION:
CC F4JN35; Q9FI23: PDF1.2A; NbExp=3; IntAct=EBI-4426607, EBI-25516740;
CC F4JN35; O80995: PDF1.3; NbExp=3; IntAct=EBI-4426607, EBI-25522494;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18443413};
CC Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:24329768}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353,
CC ECO:0000269|PubMed:17947243, ECO:0000269|PubMed:18443413}.
CC Note=Localized primarily in plasma membrane or endoplasmic reticulum
CC membrane as dormant form and, upon osmotic stress or pathogen attack,
CC is processed into a transcriptionally active and nuclear form after a
CC proteolytic cleavage through regulated intramembrane proteolysis (RIP).
CC {ECO:0000269|PubMed:18443413, ECO:0000269|PubMed:24329768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=F4JN35-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves,
CC shoot apex, stems and flowers (PubMed:17158162). Expressed in guard
CC cells (PubMed:18443413). {ECO:0000269|PubMed:17158162,
CC ECO:0000269|PubMed:18443413}.
CC -!- DEVELOPMENTAL STAGE: Induced during normal senescence.
CC {ECO:0000269|PubMed:18443413}.
CC -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:18443413, PubMed:22826500). Mutant plants display
CC enhanced resistance to the bacterial pathogen P.syringae pv. tomato
CC DC3000 (PubMed:22826500). {ECO:0000269|PubMed:18443413,
CC ECO:0000269|PubMed:22826500}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE86534.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA20028.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80274.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL031135; CAA20028.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161587; CAB80274.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86533.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86534.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY056443; AAL08299.1; -; mRNA.
DR EMBL; AY081716; AAL87369.1; -; mRNA.
DR PIR; T04663; T04663.
DR RefSeq; NP_001119122.1; NM_001125650.1.
DR RefSeq; NP_567986.3; NM_119723.5. [F4JN35-1]
DR AlphaFoldDB; F4JN35; -.
DR SMR; F4JN35; -.
DR IntAct; F4JN35; 168.
DR STRING; 3702.AT4G35580.2; -.
DR iPTMnet; F4JN35; -.
DR PaxDb; F4JN35; -.
DR PRIDE; F4JN35; -.
DR ProteomicsDB; 249181; -. [F4JN35-1]
DR EnsemblPlants; AT4G35580.1; AT4G35580.1; AT4G35580. [F4JN35-1]
DR GeneID; 829710; -.
DR Gramene; AT4G35580.1; AT4G35580.1; AT4G35580. [F4JN35-1]
DR KEGG; ath:AT4G35580; -.
DR Araport; AT4G35580; -.
DR TAIR; locus:2128013; AT4G35580.
DR eggNOG; ENOG502QQI4; Eukaryota.
DR HOGENOM; CLU_016524_1_0_1; -.
DR OrthoDB; 781000at2759; -.
DR PRO; PR:F4JN35; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JN35; baseline and differential.
DR Genevisible; F4JN35; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0071470; P:cellular response to osmotic stress; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR Gene3D; 2.170.150.80; -; 1.
DR InterPro; IPR003441; NAC-dom.
DR InterPro; IPR036093; NAC_dom_sf.
DR Pfam; PF02365; NAM; 1.
DR SUPFAM; SSF101941; SSF101941; 1.
DR PROSITE; PS51005; NAC; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Calmodulin-binding; Cell membrane;
KW DNA-binding; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Repressor; Stress response; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..512
FT /note="Protein NTM1-like 9"
FT /id="PRO_0000432447"
FT TRANSMEM 489..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 9..159
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 108..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT REGION 175..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 487
FT /note="W->R: Loss of binding to calmodulin."
FT /evidence="ECO:0000269|PubMed:17947243"
FT MUTAGEN 491
FT /note="A->R: No effect on binding to calmodulin."
FT /evidence="ECO:0000269|PubMed:17947243"
FT MUTAGEN 496
FT /note="A->R: No effect on binding to calmodulin."
FT /evidence="ECO:0000269|PubMed:17947243"
FT CONFLICT 457
FT /note="A -> V (in Ref. 3; AAL08299/AAL87369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 57250 MW; 8C89C450717C116F CRC64;
MGAVSMESLP LGFRFRPTDE ELVNHYLRLK INGRHSDVRV IPDIDVCKWE PWDLPALSVI
KTDDPEWFFF CPRDRKYPNG HRSNRATDSG YWKATGKDRS IKSKKTLIGM KKTLVFYRGR
APKGERTNWI MHEYRPTLKD LDGTSPGQSP YVLCRLFHKP DDRVNGVKSD EAAFTASNKY
SPDDTSSDLV QETPSSDAAV EKPSDYSGGC GYAHSNSTAD GTMIEAPEEN LWLSCDLEDQ
KAPLPCMDSI YAGDFSYDEI GFQFQDGTSE PDVSLTELLE EVFNNPDDFS CEESISRENP
AVSPNGIFSS AKMLQSAAPE DAFFNDFMAF TDTDAEMAQL QYGSEGGASG WPSDTNSYYS
DLVQQEQMIN HNTENNLTEG RGIKIRARQP QNRQSTGLIN QGIAPRRIRL QLQSNSEVKE
REEVNEGHTV IPEAKEAAAK YSEKSGSLVK PQIKLRARGT IGQVKGERFA DDEVQVQSRK
RRGGKRWKVV ATVMVAVMVG VGMGIWRTLV SS
