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NAC domain-containing protein 91 (ANAC091) (TCV-interacting protein)

 NAC91_ARATH             Reviewed;         451 AA.
Q9LKG8;
11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 111.
RecName: Full=NAC domain-containing protein 91 {ECO:0000303|PubMed:15029955};
Short=ANAC091 {ECO:0000303|PubMed:15029955};
AltName: Full=TCV-interacting protein {ECO:0000303|PubMed:11041886};
Name=NAC091 {ECO:0000303|PubMed:15029955};
Synonyms=TIP {ECO:0000303|PubMed:11041886};
OrderedLocusNames=At5g24590 {ECO:0000312|EMBL:AAN72023.1};
ORFNames=K18P6.12 {ECO:0000312|EMBL:BAB11211.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|EMBL:AAF87300.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION (MICROBIAL INFECTION),
INTERACTION WITH THE CAPSID PROTEIN OF TURNIP CRINKLE VIRUS, AND
SUBUNIT (MICROBIAL INFECTION).
STRAIN=cv. Columbia, cv. Di-0, and cv. Di-17;
PubMed=11041886; DOI=10.1105/tpc.12.10.1917;
Ren T., Qu F., Morris T.J.;
"HRT gene function requires interaction between a NAC protein and
viral capsid protein to confer resistance to turnip crinkle virus.";
Plant Cell 12:1917-1926(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15029955; DOI=10.1093/dnares/10.6.239;
Ooka H., Satoh K., Doi K., Nagata T., Otomo Y., Murakami K.,
Matsubara K., Osato N., Kawai J., Carninci P., Hayashizaki Y.,
Suzuki K., Kojima K., Takahara Y., Yamamoto K., Kikuchi S.;
"Comprehensive analysis of NAC family genes in Oryza sativa and
Arabidopsis thaliana.";
DNA Res. 10:239-247(2003).
[6]
FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION (MICROBIAL
INFECTION), INTERACTION WITH THE CAPSID PROTEIN OF TURNIP CRINKLE
VIRUS, AND SUBUNIT (MICROBIAL INFECTION).
PubMed=15629774; DOI=10.1016/j.virol.2004.10.039;
Ren T., Qu F., Morris T.J.;
"The nuclear localization of the Arabidopsis transcription factor TIP
is blocked by its interaction with the coat protein of Turnip crinkle
virus.";
Virology 331:316-324(2005).
[7]
INDUCTION BY TTE (MICROBIAL INFECTION).
PubMed=16553893; DOI=10.1111/j.1365-313X.2006.02672.x;
Truman W., de Zabala M.T., Grant M.;
"Type III effectors orchestrate a complex interplay between
transcriptional networks to modify basal defence responses during
pathogenesis and resistance.";
Plant J. 46:14-33(2006).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia, and cv. Di-17;
PubMed=18785827; DOI=10.1094/MPMI-21-10-1316;
Jeong R.-D., Chandra-Shekara A.C., Kachroo A., Klessig D.F.,
Kachroo P.;
"HRT-mediated hypersensitive response and resistance to Turnip crinkle
virus in Arabidopsis does not require the function of TIP, the
presumed guardee protein.";
Mol. Plant Microbe Interact. 21:1316-1324(2008).
[9]
FUNCTION, INDUCTION BY TCV (MICROBIAL INFECTION), AND SUBUNIT
(MICROBIAL INFECTION).
STRAIN=cv. Columbia;
PubMed=24418554; DOI=10.1016/j.virol.2013.11.018;
Donze T., Qu F., Twigg P., Morris T.J.;
"Turnip crinkle virus coat protein inhibits the basal immune response
to virus invasion in Arabidopsis by binding to the NAC transcription
factor TIP.";
Virology 449:207-214(2014).
-!- FUNCTION: Transcription activator essential for the anti-viral
defense called virus basal resistance response pathway
(PubMed:11041886, PubMed:15629774, PubMed:18785827,
PubMed:24418554). Not involved in HRT-mediated hypersensitive
response (HR) and resistance to TCV (PubMed:18785827). Binds DNA
non specifically (PubMed:15629774). Activated by proteolytic
cleavage through regulated intramembrane proteolysis (RIP) (By
similarity). {ECO:0000250|UniProtKB:Q9SCK6,
ECO:0000269|PubMed:11041886, ECO:0000269|PubMed:15629774,
ECO:0000269|PubMed:18785827, ECO:0000269|PubMed:24418554}.
-!- FUNCTION: (Microbial infection) Compromised function in defense
response pathway when interacting with the invading viral capsid
protein (CP) of turnip crinkle virus (TCV) due to abnormal
subcellular localization. {ECO:0000269|PubMed:11041886,
ECO:0000269|PubMed:15629774}.
-!- SUBUNIT: (Microbial infection) Interacts via its C-terminal region
with the N-terminal region of the turnip crinkle virus (TCV)
capsid protein (CP); this interaction prevents its nuclear
localization and inhibits its function in basal resistance
response pathway. {ECO:0000269|PubMed:11041886,
ECO:0000269|PubMed:15629774, ECO:0000269|PubMed:24418554}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00353, ECO:0000269|PubMed:15629774}. Endomembrane
system {ECO:0000269|PubMed:15629774}; Single-pass membrane protein
{ECO:0000255}. Note=(Microbial infection) Nuclear localization is
blocked by its interaction with the coat protein (CP) of turnip
crinkle virus (TCV), thus leading to its accumulation in
inclusion-like structures peripheral to the nuclei.
{ECO:0000269|PubMed:15629774}.
-!- INDUCTION: Induced by bacterial pathogens type III effector
proteins (TTEs). {ECO:0000269|PubMed:16553893}.
-!- INDUCTION: (Microbial infection) Accumulates 2 days post infection
with turnip crinkle virus (TCV) (PubMed:24418554).
{ECO:0000269|PubMed:24418554}.
-!- DOMAIN: The NAC domain includes a DNA binding domain and a
dimerization domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
-!- PTM: Phosphorylated at Thr-142. Phosphorylation at Thr-142 is
required for nuclear import. {ECO:0000250|UniProtKB:Q9SCK6,
ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Increased replication of turnip crinkle
virus (TCV) and cucumber mosaic virus (CMV) (PubMed:18785827,
PubMed:24418554). Normal HRT-mediated hypersensitive response (HR)
and resistance to TCV (PubMed:18785827). Delayed flower
development in antisense asTIP plants (PubMed:24418554).
{ECO:0000269|PubMed:18785827, ECO:0000269|PubMed:24418554}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF281062; AAF87300.1; -; mRNA.
EMBL; AB010068; BAB11211.1; -; Genomic_DNA.
EMBL; CP002688; AED93330.1; -; Genomic_DNA.
EMBL; BT002012; AAN72023.1; -; mRNA.
EMBL; BT009683; AAP81801.1; -; mRNA.
RefSeq; NP_197847.3; NM_122367.4.
UniGene; At.65025; -.
ProteinModelPortal; Q9LKG8; -.
SMR; Q9LKG8; -.
IntAct; Q9LKG8; 34.
STRING; 3702.AT5G24590.2; -.
PaxDb; Q9LKG8; -.
EnsemblPlants; AT5G24590.2; AT5G24590.2; AT5G24590.
GeneID; 832530; -.
Gramene; AT5G24590.2; AT5G24590.2; AT5G24590.
KEGG; ath:AT5G24590; -.
Araport; AT5G24590; -.
TAIR; locus:2153899; AT5G24590.
eggNOG; ENOG410IGNU; Eukaryota.
eggNOG; ENOG410ZJIT; LUCA.
HOGENOM; HOG000074733; -.
OMA; TQYGTND; -.
OrthoDB; EOG09360IHI; -.
PhylomeDB; Q9LKG8; -.
PRO; PR:Q9LKG8; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9LKG8; baseline and differential.
Genevisible; Q9LKG8; AT.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:TAIR.
GO; GO:0003713; F:transcription coactivator activity; IDA:TAIR.
GO; GO:0044212; F:transcription regulatory region DNA binding; IPI:TAIR.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB.
GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IMP:UniProtKB.
Gene3D; 3.30.310.150; -; 1.
InterPro; IPR003441; NAC-dom.
InterPro; IPR036093; NAC_dom_sf.
Pfam; PF02365; NAM; 1.
SUPFAM; SSF101941; SSF101941; 1.
PROSITE; PS51005; NAC; 1.
1: Evidence at protein level;
Activator; Antiviral defense; Complete proteome; DNA-binding;
Host-virus interaction; Membrane; Nucleus; Phosphoprotein;
Plant defense; Reference proteome; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix.
CHAIN 1 451 NAC domain-containing protein 91.
/FTId=PRO_0000434570.
TRANSMEM 431 450 Helical. {ECO:0000255}.
DOMAIN 13 164 NAC. {ECO:0000255|PROSITE-
ProRule:PRU00353}.
DNA_BIND 113 170 {ECO:0000255|PROSITE-ProRule:PRU00353}.
REGION 1 268 Involved in Transcription activation.
{ECO:0000269|PubMed:15629774}.
REGION 351 451 Turnip crinkle virus (TCV) capsid
protein- (CP-) binding.
{ECO:0000269|PubMed:15629774}.
MOD_RES 142 142 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9SCK6,
ECO:0000305}.
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


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