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NAC40_ARATH
ID   NAC40_ARATH             Reviewed;         335 AA.
AC   Q9XIN7;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=NAC domain-containing protein 40 {ECO:0000303|PubMed:15029955};
DE            Short=ANAC040 {ECO:0000303|PubMed:15029955};
DE   AltName: Full=Protein NTM1-like 8 {ECO:0000303|PubMed:17158162};
GN   Name=NTL8 {ECO:0000303|PubMed:17158162};
GN   OrderedLocusNames=At2g27300 {ECO:0000312|Araport:AT2G27300};
GN   ORFNames=F12K2.12 {ECO:0000312|EMBL:AAD41999.1};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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].
RC   STRAIN=cv. Columbia;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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   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   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALT AND IMBIBITION,
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PROTEOLYTIC CLEAVAGE.
RX   PubMed=19704545; DOI=10.4161/psb.2.6.4645;
RA   Kim S.-G., Park C.-M.;
RT   "Membrane-mediated salt stress signaling in flowering time control.";
RL   Plant Signal. Behav. 2:517-518(2007).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION BY SALT,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PROTEOLYTIC CLEAVAGE.
RC   STRAIN=cv. Columbia;
RX   PubMed=17410378; DOI=10.1007/s00425-007-0513-3;
RA   Kim S.-G., Kim S.-Y., Park C.-M.;
RT   "A membrane-associated NAC transcription factor regulates salt-responsive
RT   flowering via FLOWERING LOCUS T in Arabidopsis.";
RL   Planta 226:647-654(2007).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALT AND GIBBERELLIC ACID,
RP   SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX   PubMed=18363782; DOI=10.1111/j.1365-313x.2008.03493.x;
RA   Kim S.-G., Lee A.-K., Yoon H.-K., Park C.-M.;
RT   "A membrane-bound NAC transcription factor NTL8 regulates gibberellic acid-
RT   mediated salt signaling in Arabidopsis seed germination.";
RL   Plant J. 55:77-88(2008).
RN   [10]
RP   FUNCTION, AND INDUCTION BY SALT AND IMBIBITION.
RX   PubMed=19704528; DOI=10.4161/psb.3.10.6247;
RA   Kim S.-G., Park C.-M.;
RT   "Gibberellic acid-mediated salt signaling in seed germination.";
RL   Plant Signal. Behav. 3:877-879(2008).
CC   -!- FUNCTION: Transcriptional activator activated by proteolytic cleavage
CC       through regulated intramembrane proteolysis (RIP), probably via
CC       metalloprotease activity. Regulates gibberellic acid-mediated salt-
CC       responsive repression of seed germination and flowering via FT, thus
CC       delaying seed germination under high salinity conditions.
CC       {ECO:0000269|PubMed:17410378, ECO:0000269|PubMed:18363782,
CC       ECO:0000269|PubMed:19704528, ECO:0000269|PubMed:19704545}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17410378,
CC       ECO:0000269|PubMed:18363782, ECO:0000269|PubMed:19704545}; Single-pass
CC       membrane protein {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00353, ECO:0000269|PubMed:17410378,
CC       ECO:0000269|PubMed:18363782, ECO:0000269|PubMed:19704545}.
CC       Note=Localized primarily in plasma membrane as dormant form and, upon
CC       salt stress, is processed into a transcriptionally active and nuclear
CC       form after a proteolytic cleavage through regulated intramembrane
CC       proteolysis (RIP). {ECO:0000269|PubMed:17410378,
CC       ECO:0000269|PubMed:18363782, ECO:0000269|PubMed:19704545}.
CC   -!- TISSUE SPECIFICITY: Expressed in seeds, leaves, roots and inflorescence
CC       (PubMed:17410378). Expressed in roots, rosette leaves, cauline leaves,
CC       shoot apex, stems and flowers (PubMed:17158162).
CC       {ECO:0000269|PubMed:17158162, ECO:0000269|PubMed:17410378}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates in imbibed seeds (PubMed:19704545).
CC       Detected in early stages of seed development, especially in the basal
CC       tip of immature embryo. Particularly expressed in vascular tissues of
CC       inflorescence stems, roots, leaves and petioles (PubMed:17410378).
CC       {ECO:0000269|PubMed:17410378, ECO:0000269|PubMed:19704545}.
CC   -!- INDUCTION: By high salt stress (PubMed:19704545, PubMed:17410378,
CC       PubMed:18363782, PubMed:19704528). Repressed by gibberellic acid (GA),
CC       but induced by the GA biosynthetic inhibitor paclabutrazol (PAC)
CC       (PubMed:18363782). Accumulates transiently in seeds upon imbibition
CC       (PubMed:19704545, PubMed:17410378, PubMed:18363782, PubMed:19704528).
CC       Induced by drought stress (PubMed:17158162).
CC       {ECO:0000269|PubMed:17158162, ECO:0000269|PubMed:17410378,
CC       ECO:0000269|PubMed:18363782, ECO:0000269|PubMed:19704528,
CC       ECO:0000269|PubMed:19704545}.
CC   -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC       domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC   -!- PTM: Proteolytically cleaved, probably by metalloprotease activity.
CC       This cleavage mediates a translocation from the plasma membrane to the
CC       nucleus. {ECO:0000269|PubMed:17410378, ECO:0000269|PubMed:18363782,
CC       ECO:0000269|PubMed:19704545}.
CC   -!- DISRUPTION PHENOTYPE: In ntl8-1, no discernible phenotypic changes
CC       except slight differences in lateral root growth and flowering time, as
CC       well as reduced lateral root growth rate. Insensitive to high salt.
CC       {ECO:0000269|PubMed:17410378, ECO:0000269|PubMed:18363782,
CC       ECO:0000269|PubMed:19704545}.
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DR   EMBL; AC006233; AAD41999.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07970.1; -; Genomic_DNA.
DR   EMBL; DQ056544; AAY78696.1; -; mRNA.
DR   EMBL; BT028934; ABI49481.1; -; mRNA.
DR   PIR; C84671; C84671.
DR   RefSeq; NP_180298.1; NM_128289.2.
DR   AlphaFoldDB; Q9XIN7; -.
DR   SMR; Q9XIN7; -.
DR   IntAct; Q9XIN7; 5.
DR   STRING; 3702.AT2G27300.1; -.
DR   PaxDb; Q9XIN7; -.
DR   PRIDE; Q9XIN7; -.
DR   ProteomicsDB; 248924; -.
DR   EnsemblPlants; AT2G27300.1; AT2G27300.1; AT2G27300.
DR   GeneID; 817273; -.
DR   Gramene; AT2G27300.1; AT2G27300.1; AT2G27300.
DR   KEGG; ath:AT2G27300; -.
DR   Araport; AT2G27300; -.
DR   TAIR; locus:2039600; AT2G27300.
DR   eggNOG; ENOG502QRAU; Eukaryota.
DR   HOGENOM; CLU_035664_18_0_1; -.
DR   InParanoid; Q9XIN7; -.
DR   OMA; DDDCYAE; -.
DR   OrthoDB; 936963at2759; -.
DR   PhylomeDB; Q9XIN7; -.
DR   PRO; PR:Q9XIN7; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9XIN7; baseline and differential.
DR   Genevisible; Q9XIN7; AT.
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:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0071472; P:cellular response to salt stress; IMP:UniProtKB.
DR   GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR   GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
DR   GO; GO:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0048573; P:photoperiodism, flowering; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR   GO; GO:2000039; P:regulation of trichome morphogenesis; IMP:TAIR.
DR   GO; GO:0009739; P:response to gibberellin; IDA:UniProtKB.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   GO; GO:0009845; P:seed germination; IDA: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; Cell membrane; DNA-binding; Flowering;
KW   Gibberellin signaling pathway; Membrane; Nucleus; Reference proteome;
KW   Stress response; Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..335
FT                   /note="NAC domain-containing protein 40"
FT                   /id="PRO_0000431527"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          14..156
FT                   /note="NAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   DNA_BIND        112..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   REGION          245..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  38184 MW;  B0B34D87FB18134C CRC64;
     MSKEAEMSIA VSALFPGFRF SPTDVELISY YLRRKIDGDE NSVAVIAEVE IYKFEPWDLP
     EESKLKSENE WFYFCARGRK YPHGSQSRRA TQLGYWKATG KERSVKSGNQ VVGTKRTLVF
     HIGRAPRGER TEWIMHEYCI HGAPQDALVV CRLRKNADFR ASSTQKMEDG VVQDDGYVGQ
     RGGLEKEDKS YYESEHQIPN GDIAESSNVV EDQADTDDDC YAEILNDDII KLDEEALKAS
     QAFRPTNPTH QETISSESSS KRSKCGIKKE STETMNCYAL FRIKNVAGTD SSWRFPNPFK
     IKKDDSQRLM KNVLATTVFL AILFSFFWTV LIARN
 
 
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