NAC91_ARATH
ID NAC91_ARATH Reviewed; 451 AA.
AC Q9LKG8;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=NAC domain-containing protein 91 {ECO:0000303|PubMed:15029955};
DE Short=ANAC091 {ECO:0000303|PubMed:15029955};
DE AltName: Full=TCV-interacting protein {ECO:0000303|PubMed:11041886};
GN Name=NAC091 {ECO:0000303|PubMed:15029955};
GN Synonyms=TIP {ECO:0000303|PubMed:11041886};
GN OrderedLocusNames=At5g24590 {ECO:0000312|EMBL:AAN72023.1};
GN ORFNames=K18P6.12 {ECO:0000312|EMBL:BAB11211.1};
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 {ECO:0000312|EMBL:AAF87300.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION (MICROBIAL INFECTION), INTERACTION
RP WITH THE CAPSID PROTEIN OF TURNIP CRINKLE VIRUS, AND SUBUNIT (MICROBIAL
RP INFECTION).
RC STRAIN=cv. Columbia, cv. Di-0, and cv. Di-17;
RX PubMed=11041886; DOI=10.2307/3871202;
RA Ren T., Qu F., Morris T.J.;
RT "HRT gene function requires interaction between a NAC protein and viral
RT capsid protein to confer resistance to turnip crinkle virus.";
RL Plant Cell 12:1917-1926(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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].
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 [5]
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 [6]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION (MICROBIAL INFECTION),
RP INTERACTION WITH THE CAPSID PROTEIN OF TURNIP CRINKLE VIRUS, AND SUBUNIT
RP (MICROBIAL INFECTION).
RX PubMed=15629774; DOI=10.1016/j.virol.2004.10.039;
RA Ren T., Qu F., Morris T.J.;
RT "The nuclear localization of the Arabidopsis transcription factor TIP is
RT blocked by its interaction with the coat protein of Turnip crinkle virus.";
RL Virology 331:316-324(2005).
RN [7]
RP INDUCTION BY TTE (MICROBIAL INFECTION).
RX PubMed=16553893; DOI=10.1111/j.1365-313x.2006.02672.x;
RA Truman W., de Zabala M.T., Grant M.;
RT "Type III effectors orchestrate a complex interplay between transcriptional
RT networks to modify basal defence responses during pathogenesis and
RT resistance.";
RL Plant J. 46:14-33(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Di-17;
RX PubMed=18785827; DOI=10.1094/mpmi-21-10-1316;
RA Jeong R.-D., Chandra-Shekara A.C., Kachroo A., Klessig D.F., Kachroo P.;
RT "HRT-mediated hypersensitive response and resistance to Turnip crinkle
RT virus in Arabidopsis does not require the function of TIP, the presumed
RT guardee protein.";
RL Mol. Plant Microbe Interact. 21:1316-1324(2008).
RN [9]
RP FUNCTION, INDUCTION BY TCV (MICROBIAL INFECTION), AND SUBUNIT (MICROBIAL
RP INFECTION).
RC STRAIN=cv. Columbia;
RX PubMed=24418554; DOI=10.1016/j.virol.2013.11.018;
RA Donze T., Qu F., Twigg P., Morris T.J.;
RT "Turnip crinkle virus coat protein inhibits the basal immune response to
RT virus invasion in Arabidopsis by binding to the NAC transcription factor
RT TIP.";
RL Virology 449:207-214(2014).
CC -!- FUNCTION: Transcription activator essential for the anti-viral defense
CC called virus basal resistance response pathway (PubMed:11041886,
CC PubMed:15629774, PubMed:18785827, PubMed:24418554). Not involved in
CC HRT-mediated hypersensitive response (HR) and resistance to TCV
CC (PubMed:18785827). Binds DNA non specifically (PubMed:15629774).
CC Activated by proteolytic cleavage through regulated intramembrane
CC proteolysis (RIP) (By similarity). {ECO:0000250|UniProtKB:Q9SCK6,
CC ECO:0000269|PubMed:11041886, ECO:0000269|PubMed:15629774,
CC ECO:0000269|PubMed:18785827, ECO:0000269|PubMed:24418554}.
CC -!- FUNCTION: (Microbial infection) Compromised function in defense
CC response pathway when interacting with the invading viral capsid
CC protein (CP) of turnip crinkle virus (TCV) due to abnormal subcellular
CC localization. {ECO:0000269|PubMed:11041886,
CC ECO:0000269|PubMed:15629774}.
CC -!- SUBUNIT: (Microbial infection) Interacts via its C-terminal region with
CC the N-terminal region of the turnip crinkle virus (TCV) capsid protein
CC (CP); this interaction prevents its nuclear localization and inhibits
CC its function in basal resistance response pathway.
CC {ECO:0000269|PubMed:11041886, ECO:0000269|PubMed:15629774,
CC ECO:0000269|PubMed:24418554}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353,
CC ECO:0000269|PubMed:15629774}. Endomembrane system
CC {ECO:0000269|PubMed:15629774}; Single-pass membrane protein
CC {ECO:0000255}. Note=(Microbial infection) Nuclear localization is
CC blocked by its interaction with the coat protein (CP) of turnip crinkle
CC virus (TCV), thus leading to its accumulation in inclusion-like
CC structures peripheral to the nuclei. {ECO:0000269|PubMed:15629774}.
CC -!- INDUCTION: Induced by bacterial pathogens type III effector proteins
CC (TTEs). {ECO:0000269|PubMed:16553893}.
CC -!- INDUCTION: (Microbial infection) Accumulates 2 days post infection with
CC turnip crinkle virus (TCV) (PubMed:24418554).
CC {ECO:0000269|PubMed:24418554}.
CC -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC -!- PTM: Phosphorylated at Thr-142. Phosphorylation at Thr-142 is required
CC for nuclear import. {ECO:0000250|UniProtKB:Q9SCK6, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Increased replication of turnip crinkle virus
CC (TCV) and cucumber mosaic virus (CMV) (PubMed:18785827,
CC PubMed:24418554). Normal HRT-mediated hypersensitive response (HR) and
CC resistance to TCV (PubMed:18785827). Delayed flower development in
CC antisense asTIP plants (PubMed:24418554). {ECO:0000269|PubMed:18785827,
CC ECO:0000269|PubMed:24418554}.
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DR EMBL; AF281062; AAF87300.1; -; mRNA.
DR EMBL; AB010068; BAB11211.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93330.1; -; Genomic_DNA.
DR EMBL; BT002012; AAN72023.1; -; mRNA.
DR EMBL; BT009683; AAP81801.1; -; mRNA.
DR RefSeq; NP_197847.3; NM_122367.4.
DR AlphaFoldDB; Q9LKG8; -.
DR SMR; Q9LKG8; -.
DR IntAct; Q9LKG8; 34.
DR STRING; 3702.AT5G24590.2; -.
DR PaxDb; Q9LKG8; -.
DR PRIDE; Q9LKG8; -.
DR ProteomicsDB; 251240; -.
DR EnsemblPlants; AT5G24590.2; AT5G24590.2; AT5G24590.
DR GeneID; 832530; -.
DR Gramene; AT5G24590.2; AT5G24590.2; AT5G24590.
DR KEGG; ath:AT5G24590; -.
DR Araport; AT5G24590; -.
DR TAIR; locus:2153899; AT5G24590.
DR eggNOG; ENOG502QS98; Eukaryota.
DR HOGENOM; CLU_016524_1_0_1; -.
DR InParanoid; Q9LKG8; -.
DR OMA; TQYGTND; -.
DR OrthoDB; 689986at2759; -.
DR PhylomeDB; Q9LKG8; -.
DR PRO; PR:Q9LKG8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LKG8; baseline and differential.
DR Genevisible; Q9LKG8; AT.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA 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; IPI:TAIR.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0051607; P:defense response to virus; IPI:TAIR.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0016032; P:viral process; IMP:UniProtKB.
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; Antiviral defense; DNA-binding; Host-virus interaction;
KW Membrane; Nucleus; Phosphoprotein; Plant defense; Reference proteome;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..451
FT /note="NAC domain-containing protein 91"
FT /id="PRO_0000434570"
FT TRANSMEM 431..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 13..164
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 113..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT REGION 1..268
FT /note="Involved in Transcription activation"
FT /evidence="ECO:0000269|PubMed:15629774"
FT REGION 351..451
FT /note="Turnip crinkle virus (TCV) capsid protein- (CP-)
FT binding"
FT /evidence="ECO:0000269|PubMed:15629774"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9SCK6, ECO:0000305"
SQ SEQUENCE 451 AA; 50891 MW; 29B014A988C6D866 CRC64;
MKEDMEVLSL ASLPVGFRFS PTDEELVRYY LRLKINGHDN DVRVIREIDI CKWEPWDLPD
FSVVKTTDSE WLFFCPLDRK YPSGSRMNRA TVAGYWKATG KDRKIKSGKT KIIGVKRTLV
FYTGRAPKGT RTCWIMHEYR ATEKDLDGTK SGQNPFVVCK LFKKQDIVNG AAEPEESKSC
EVEPAVSSPT VVDEVEMSEV SPVFPKTEET NPCDVAESSL VIPSECRSGY SVPEVTTTGL
DDIDWLSFME FDSPKLFSPL HSQVQSELGS SFNGLQSESS ELFKNHNEDY IQTQYGTNDA
DEYMSKFLDS FLDIPYEPEQ IPYEPQNLSS CNKINDESKR GIKIRARRAQ APGCAEQFVM
QGDASRRLRL QVNLNSHKSE TDSTQLQFIK KEVKDTTTET MTKGCGNFTR SKSRTSFIFK
KIAAMGCSYR GLFRVGVVAV VCVMSVCSLV A
