NAC62_ARATH
ID NAC62_ARATH Reviewed; 469 AA.
AC Q9SCK6;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=NAC domain-containing protein 62 {ECO:0000303|PubMed:15029955};
DE Short=ANAC062 {ECO:0000303|PubMed:15029955};
DE AltName: Full=Protein NTM1-like 6 {ECO:0000303|PubMed:17158162};
GN Name=NAC062 {ECO:0000312|EMBL:AEE78553.1};
GN Synonyms=NTL6 {ECO:0000303|PubMed:17158162};
GN OrderedLocusNames=At3g49530 {ECO:0000312|Araport:AT3G49530};
GN ORFNames=T9C5.120 {ECO:0000312|EMBL:CAB62457.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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].
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 GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=20156199; DOI=10.1042/bj20091762;
RA Seo P.J., Kim M.J., Song J.S., Kim Y.S., Kim H.J., Park C.M.;
RT "Proteolytic processing of an Arabidopsis membrane-bound NAC transcription
RT factor is triggered by cold-induced changes in membrane fluidity.";
RL Biochem. J. 427:359-367(2010).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19947982; DOI=10.1111/j.1365-313x.2009.04091.x;
RA Seo P.J., Kim M.J., Park J.Y., Kim S.Y., Jeon J., Lee Y.H., Kim J.,
RA Park C.M.;
RT "Cold activation of a plasma membrane-tethered NAC transcription factor
RT induces a pathogen resistance response in Arabidopsis.";
RL Plant J. 61:661-671(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-142.
RX PubMed=22967043; DOI=10.1042/bj20120244;
RA Kim M.J., Park M.J., Seo P.J., Song J.S., Kim H.J., Park C.M.;
RT "Controlled nuclear import of the transcription factor NTL6 reveals a
RT cytoplasmic role of SnRK2.8 in the drought-stress response.";
RL Biochem. J. 448:353-363(2012).
CC -!- FUNCTION: Transcriptional activator activated by proteolytic cleavage
CC through regulated intramembrane proteolysis (RIP) (PubMed:20156199,
CC PubMed:19947982). Transcriptional activator involved in response to
CC cold stress. Mediates induction of pathogenesis-related (PR) genes
CC independently of salicylic signaling in response to cold. Binds
CC directly to the PR gene promoters and enhances plant resistance to
CC pathogen infection, incorporating cold signals into pathogen resistance
CC responses (PubMed:19947982). Plays a regulatory role in abscisic acid
CC (ABA)-mediated drought-resistance response (PubMed:22967043).
CC {ECO:0000269|PubMed:19947982, ECO:0000269|PubMed:20156199,
CC ECO:0000269|PubMed:22967043}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19947982};
CC Single-pass membrane protein {ECO:0000255}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:19947982,
CC ECO:0000269|PubMed:20156199, ECO:0000269|PubMed:22967043}.
CC Note=Localized primarily in plasma membrane as dormant form and, upon
CC cold or stress, is processed into a transcriptionally active and
CC nuclear form after a proteolytic cleavage through regulated
CC intramembrane proteolysis (RIP). {ECO:0000269|PubMed:19947982,
CC ECO:0000269|PubMed:20156199}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves
CC and stems. {ECO:0000269|PubMed:17158162}.
CC -!- INDUCTION: By salt, drought stress, abscisic acid (ABA), salicylic acid
CC (SA) and methyl methanesulfonate (MMS) treatment.
CC {ECO:0000269|PubMed:17158162}.
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 by SRK2C/SNRK2.8. Phosphorylation at
CC Thr-142 is required for nuclear import. {ECO:0000269|PubMed:22967043}.
CC -!- MISCELLANEOUS: Plants over-expressing NTL6 show enhanced drought
CC resistance. {ECO:0000269|PubMed:22967043}.
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DR EMBL; AL132964; CAB62457.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78553.1; -; Genomic_DNA.
DR EMBL; AY059734; AAL24091.1; -; mRNA.
DR EMBL; BT000978; AAN41378.1; -; mRNA.
DR PIR; T46230; T46230.
DR RefSeq; NP_190522.1; NM_114813.4.
DR AlphaFoldDB; Q9SCK6; -.
DR SMR; Q9SCK6; -.
DR IntAct; Q9SCK6; 10.
DR STRING; 3702.AT3G49530.1; -.
DR iPTMnet; Q9SCK6; -.
DR PaxDb; Q9SCK6; -.
DR PRIDE; Q9SCK6; -.
DR ProteomicsDB; 251196; -.
DR EnsemblPlants; AT3G49530.1; AT3G49530.1; AT3G49530.
DR GeneID; 824115; -.
DR Gramene; AT3G49530.1; AT3G49530.1; AT3G49530.
DR KEGG; ath:AT3G49530; -.
DR Araport; AT3G49530; -.
DR TAIR; locus:2114678; AT3G49530.
DR eggNOG; ENOG502QS98; Eukaryota.
DR HOGENOM; CLU_016524_1_0_1; -.
DR InParanoid; Q9SCK6; -.
DR OrthoDB; 689986at2759; -.
DR PhylomeDB; Q9SCK6; -.
DR PRO; PR:Q9SCK6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCK6; baseline and differential.
DR Genevisible; Q9SCK6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0070417; P:cellular response to cold; IMP:TAIR.
DR GO; GO:0098542; P:defense response to other organism; IMP:TAIR.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IMP: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; Cell membrane; DNA-binding; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..469
FT /note="NAC domain-containing protein 62"
FT /id="PRO_0000432446"
FT TRANSMEM 441..461
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 172..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22967043"
SQ SEQUENCE 469 AA; 52494 MW; 732BF81A4A7517D2 CRC64;
MNQNLHVLSM DSLPVGLRFR PTDEELIRYY LRRKINGHDD DVKAIREIDI CKWEPWDLPD
FSVIKTKDSE WLYFCPLDRK YPSGSRQNRA TVAGYWKATG KDRKIKSGKT NIIGVKRTLV
FHAGRAPRGT RTNWIIHEYR ATEDDLSGTN PGQSPFVICK LFKKEELVLG EEDSKSDEVE
EPAVSSPTVE VTKSEVSEVI KTEDVKRHDI AESSLVISGD SHSDACDEAT TAELVDFKWY
PELESLDFTL FSPLHSQVQS ELGSSYNTFQ PGSSNFSGNN NNSFQIQTQY GTNEVDTYIS
DFLDSILKSP DEDPEKHKYV LQSGFDVVAP DQIAQVCQQG SAVDMSNDVS VTGIQIKSRQ
AQPSGYTNDY IAQGNGPRRL RLQSNFNGIN TKNPELQAIK REAEDTVGES IKKRCGKLMR
SKNVTGFVFK KITSVKCSYG GLFRAAVVAV VFLMSVCSLT VDFRASAVS
