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NAC96_ARATH
ID   NAC96_ARATH             Reviewed;         292 AA.
AC   Q9LS24;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=NAC domain-containing protein 96 {ECO:0000303|PubMed:15029955};
DE            Short=ANAC096 {ECO:0000303|PubMed:15029955};
GN   Name=NAC096 {ECO:0000305};
GN   OrderedLocusNames=At5g46590 {ECO:0000312|Araport:AT5G46590};
GN   ORFNames=F10E10.6 {ECO:0000312|EMBL:BAA97530.1};
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA   Takagi M.;
RT   "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL   Submitted (MAR-2009) 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   FUNCTION, INTERACTION WITH ABF2 AND ABF4, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24285786; DOI=10.1105/tpc.113.119099;
RA   Xu Z.Y., Kim S.Y., Hyeon D.Y., Kim D.H., Dong T., Park Y., Jin J.B.,
RA   Joo S.H., Kim S.K., Hong J.C., Hwang D., Hwang I.;
RT   "The Arabidopsis NAC transcription factor ANAC096 cooperates with bZIP-type
RT   transcription factors in dehydration and osmotic stress responses.";
RL   Plant Cell 25:4708-4724(2013).
RN   [7]
RP   FUNCTION.
RX   PubMed=25182467; DOI=10.1111/tpj.12654;
RA   Pitaksaringkarn W., Matsuoka K., Asahina M., Miura K., Sage-Ono K., Ono M.,
RA   Yokoyama R., Nishitani K., Ishii T., Iwai H., Satoh S.;
RT   "XTH20 and XTH19 regulated by ANAC071 under auxin flow are involved in cell
RT   proliferation in incised Arabidopsis inflorescence stems.";
RL   Plant J. 80:604-614(2014).
CC   -!- FUNCTION: Transcriptional activator involved in the positive regulation
CC       of abscisic acid (ABA) responsive genes. Acts as a positive factor of
CC       ABA-mediated responses. Involved in the transcriptional activation of
CC       ABA-inducible genes in response to dehydration and osmotic stresses.
CC       Plays a positive role in both stomatal closure and water loss under
CC       dehydration stress conditions. Acts synergistically with ABF2 to
CC       activate the dehydration stress-response factor RD29A transcription.
CC       Binds to the consensus core cis-acting elements 5'-CGTA-3' and 5'-CACG-
CC       3' at the RD29A promoter (PubMed:24285786). Involved in hypocotyl graft
CC       union formation. Required for the auxin-mediated promotion of vascular
CC       tissue proliferation during hypocotyl graft attachment
CC       (PubMed:25182467). {ECO:0000269|PubMed:24285786,
CC       ECO:0000269|PubMed:25182467}.
CC   -!- SUBUNIT: Interacts with ABF2 and ABF4. {ECO:0000269|PubMed:24285786}.
CC   -!- INTERACTION:
CC       Q9LS24; Q9FJ49: PYL12; NbExp=3; IntAct=EBI-1238916, EBI-2363244;
CC       Q9LS24; Q8S8E3: PYL6; NbExp=3; IntAct=EBI-1238916, EBI-2363192;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353,
CC       ECO:0000269|PubMed:24285786}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, rosettes leaves, cauline leaves
CC       and stems. {ECO:0000269|PubMed:24285786}.
CC   -!- INDUCTION: Induced by abscisic acid (ABA), dehydration and osmotic
CC       stress. {ECO:0000269|PubMed:24285786}.
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, but mutant seedlings are hyposensitive to growth inhibition
CC       mediated by abscisic acid (ABA), and show decreased resistance to
CC       dehydration stress. {ECO:0000269|PubMed:24285786}.
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DR   EMBL; AB028605; BAA97530.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95401.1; -; Genomic_DNA.
DR   EMBL; BT020305; AAV85660.1; -; mRNA.
DR   EMBL; BT020555; AAW70401.1; -; mRNA.
DR   EMBL; AB493778; BAH30616.1; -; mRNA.
DR   RefSeq; NP_199471.1; NM_124029.3.
DR   AlphaFoldDB; Q9LS24; -.
DR   SMR; Q9LS24; -.
DR   IntAct; Q9LS24; 3.
DR   STRING; 3702.AT5G46590.1; -.
DR   PaxDb; Q9LS24; -.
DR   PRIDE; Q9LS24; -.
DR   EnsemblPlants; AT5G46590.1; AT5G46590.1; AT5G46590.
DR   GeneID; 834702; -.
DR   Gramene; AT5G46590.1; AT5G46590.1; AT5G46590.
DR   KEGG; ath:AT5G46590; -.
DR   Araport; AT5G46590; -.
DR   TAIR; locus:2142285; AT5G46590.
DR   eggNOG; ENOG502QPKD; Eukaryota.
DR   HOGENOM; CLU_035664_9_1_1; -.
DR   InParanoid; Q9LS24; -.
DR   OMA; VSPDMIL; -.
DR   OrthoDB; 1174567at2759; -.
DR   PhylomeDB; Q9LS24; -.
DR   PRO; PR:Q9LS24; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LS24; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IEP: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   DNA-binding; Nucleus; Reference proteome; Stress response; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..292
FT                   /note="NAC domain-containing protein 96"
FT                   /id="PRO_0000439705"
FT   DOMAIN          6..158
FT                   /note="NAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   DNA_BIND        106..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   REGION          171..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   292 AA;  33580 MW;  B751FDCEC6F5C3E5 CRC64;
     MGSSCLPPGF RFHPTDEELI EYYLKRKVEG LEIELEVIPV IDLYSFDPWE LPDKSFLPNR
     DMEWYFFCSR DKKYPNGFRT NRGTKAGYWK ATGKDRKITS RSSSIIGYRK TLVFYKGRAP
     LGDRSNWIMH EYRLCDDDTS QGSQNLKGAF VLCRVAMKNE IKTNTKIRKI PSEQTIGSGE
     SSGLSSRVTS PSRDETMPFH SFANPVSTET DSSNIWISPE FILDSSKDYP QIQDVASQCF
     QQDFDFPIIG NQNMEFPAST SLDQNMDEFM QNGYWTNYGY DQTGLFGYSD FS
 
 
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