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NAC53_ARATH
ID   NAC53_ARATH             Reviewed;         549 AA.
AC   Q949N0; Q8LAH6; Q9SQY1;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=NAC domain-containing protein 53 {ECO:0000303|PubMed:15029955};
DE            Short=ANAC053 {ECO:0000303|PubMed:15029955};
DE   AltName: Full=Protein ANTHER INDEHISCENCE FACTOR {ECO:0000303|PubMed:24323506};
DE   AltName: Full=Protein NTM1-like 4 {ECO:0000303|PubMed:17158162};
GN   Name=NAC053 {ECO:0000312|EMBL:AEE74917.1};
GN   Synonyms=AIF {ECO:0000303|PubMed:24323506},
GN   NTL4 {ECO:0000303|PubMed:17158162};
GN   OrderedLocusNames=At3g10500 {ECO:0000312|Araport:AT3G10500};
GN   ORFNames=F13M14.22 {ECO:0000312|EMBL:AAG51388.1},
GN   F18K10.7 {ECO:0000312|EMBL:AAF76351.1};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) 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   SUBCELLULAR LOCATION.
RA   Kim S.G., Lee S., Ryu J., Park C.M.;
RT   "Probing protein structural requirements for activation of membrane-bound
RT   NAC transcription factors in Arabidopsis and rice.";
RL   Plant Sci. 178:239-244(2010).
RN   [7]
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   [8]
RP   FUNCTION, INDUCTION BY ABSCISIC ACID, AND DISRUPTION PHENOTYPE.
RX   PubMed=22313226; DOI=10.1111/j.1365-313x.2012.04932.x;
RA   Lee S., Seo P.J., Lee H.J., Park C.M.;
RT   "A NAC transcription factor NTL4 promotes reactive oxygen species
RT   production during drought-induced leaf senescence in Arabidopsis.";
RL   Plant J. 70:831-844(2012).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=24323506; DOI=10.1093/jxb/ert412;
RA   Shih C.F., Hsu W.H., Peng Y.J., Yang C.H.;
RT   "The NAC-like gene ANTHER INDEHISCENCE FACTOR acts as a repressor that
RT   controls anther dehiscence by regulating genes in the jasmonate
RT   biosynthesis pathway in Arabidopsis.";
RL   J. Exp. Bot. 65:621-639(2014).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25219309; DOI=10.1016/j.plantsci.2014.07.003;
RA   Lee S., Lee H.J., Huh S.U., Paek K.H., Ha J.H., Park C.M.;
RT   "The Arabidopsis NAC transcription factor NTL4 participates in a positive
RT   feedback loop that induces programmed cell death under heat stress
RT   conditions.";
RL   Plant Sci. 227:76-83(2014).
CC   -!- FUNCTION: Transcriptional activator activated by proteolytic cleavage
CC       through regulated intramembrane proteolysis (RIP) (Ref.6,
CC       PubMed:24323506, PubMed:25219309). Promotes reactive oxygen species
CC       (ROS) production during drought-induced leaf senescence. In response to
CC       abscisic acid (ABA)-mediated drought stress signals, binds directly to
CC       the promoters of RBOHC and RBOHE genes, encoding ROS biosynthetic
CC       enzymes, resulting in ROS accumulation and triggering leaf senescence
CC       via programmed cell death (PCD). ROS-induced leaf senescence sustains
CC       plant survival under drought conditions (PubMed:22313226). Involved in
CC       heat stress response. Modulates PCD through a ROS-mediated positive
CC       feedback control under heat stress conditions. This may provide an
CC       adaptation strategy for plant survival under extreme heat stress
CC       conditions (PubMed:25219309). Acts as repressor in preventing anther
CC       dehiscence during stamen development by suppressing genes that
CC       participate in jasmonic acid (JA) biosynthesis, such as DAD1, AOS,
CC       AOC3, OPR3 and 4CLL5/OPCL1 (PubMed:24323506).
CC       {ECO:0000269|PubMed:22313226, ECO:0000269|PubMed:24323506,
CC       ECO:0000269|PubMed:25219309, ECO:0000269|Ref.6}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:24323506}; Single-pass membrane protein
CC       {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353,
CC       ECO:0000269|PubMed:24323506, ECO:0000269|PubMed:25219309,
CC       ECO:0000269|Ref.6}. Note=Localized primarily in plasma membrane or
CC       endoplasmic reticulum membrane as dormant form and, upon abiotic
CC       stress, is processed into a transcriptionally active and nuclear form
CC       after a proteolytic cleavage through regulated intramembrane
CC       proteolysis (RIP). {ECO:0000269|PubMed:24323506,
CC       ECO:0000269|PubMed:25219309, ECO:0000269|Ref.6}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves,
CC       shoot apex and stems. {ECO:0000269|PubMed:17158162}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the anthers and the upper parts of
CC       the stamen filaments after stage 7 to 9 of flower budding. In stage 10
CC       flower buds, expressed in the anthers and pollen grains. Weakly
CC       expressed in mature flowers at stage 12. {ECO:0000269|PubMed:24323506}.
CC   -!- INDUCTION: By abscisic acid (ABA) (PubMed:22313226, PubMed:25219309).
CC       Induced by heat shock (PubMed:25219309). Induced by cold, drought
CC       stress and methyl methanesulfonate (MMS) treatment (PubMed:17158162).
CC       {ECO:0000269|PubMed:17158162, ECO:0000269|PubMed:22313226,
CC       ECO:0000269|PubMed:25219309}.
CC   -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC       domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC   -!- DISRUPTION PHENOTYPE: Delayed leaf senescence and enhanced drought
CC       resistance (PubMed:22313226). Enhanced heat resistance
CC       (PubMed:25219309). {ECO:0000269|PubMed:22313226,
CC       ECO:0000269|PubMed:25219309}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF76351.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG51388.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC011560; AAG51388.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC013428; AAF76351.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE74917.1; -; Genomic_DNA.
DR   EMBL; AY051003; AAK93680.1; -; mRNA.
DR   EMBL; AY079345; AAL85076.1; -; mRNA.
DR   EMBL; AY087802; AAM65338.1; -; mRNA.
DR   RefSeq; NP_566376.1; NM_111885.4.
DR   AlphaFoldDB; Q949N0; -.
DR   SMR; Q949N0; -.
DR   STRING; 3702.AT3G10500.1; -.
DR   PaxDb; Q949N0; -.
DR   PRIDE; Q949N0; -.
DR   ProteomicsDB; 251225; -.
DR   DNASU; 820214; -.
DR   EnsemblPlants; AT3G10500.1; AT3G10500.1; AT3G10500.
DR   GeneID; 820214; -.
DR   Gramene; AT3G10500.1; AT3G10500.1; AT3G10500.
DR   KEGG; ath:AT3G10500; -.
DR   Araport; AT3G10500; -.
DR   TAIR; locus:2075815; AT3G10500.
DR   eggNOG; ENOG502QTKI; Eukaryota.
DR   HOGENOM; CLU_032008_1_0_1; -.
DR   InParanoid; Q949N0; -.
DR   OrthoDB; 416063at2759; -.
DR   PhylomeDB; Q949N0; -.
DR   PRO; PR:Q949N0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q949N0; baseline and differential.
DR   Genevisible; Q949N0; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; 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:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0009819; P:drought recovery; IMP:TAIR.
DR   GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR   GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; 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   2: Evidence at transcript level;
KW   Activator; DNA-binding; Endoplasmic reticulum; Membrane; Nucleus;
KW   Reference proteome; Repressor; Stress response; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..549
FT                   /note="NAC domain-containing protein 53"
FT                   /id="PRO_0000432444"
FT   TRANSMEM        526..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          9..159
FT                   /note="NAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   DNA_BIND        108..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   REGION          395..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        74
FT                   /note="D -> N (in Ref. 4; AAM65338)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276
FT                   /note="D -> H (in Ref. 4; AAM65338)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="T -> I (in Ref. 4; AAM65338)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   549 AA;  62356 MW;  89903EF6B7AFB5F5 CRC64;
     MGRGSVTSLA PGFRFHPTDE ELVRYYLKRK ICNKPFKFDA ISVTDVYKSE PWDLPDKSRL
     KSRDLEWYFF SMLDKKYRNG SKTNRATEMG YWKTTGKDRE ILNGSKVVGM KKTLVYHKGR
     APRGERTNWV MHEYRLVDQD LDKTGVHQDA FVLCRIFQKS GSGPKNGEQY GAPFVEEEWE
     EEDDMTFVPD QEDLGSEDHV YVHMDDIDQK SENFVVYDAI PIPLNFIHGE SSNNVETNYS
     DSINYIQQTG NYMDSGGYFE QPAESYEKDQ KPIIRDRDGS LQNEGIGCGV QDKHSETLQS
     SDNIFGTDTS CYNDFPVESN YLIGEAFLDP NSNLLENDGL YLETNDLSST QQDGFDFEDY
     LTFFDETFDP SQLMGNEDVF FDQEELFQEV ETKELEKEET SRSKHVVEEK EKDEASCSKQ
     VDADATEFEP DYKYPLLKKA SHMLGAIPAP LANASEFPTK DAAIRLHAAQ SSGSVHVTAG
     MITISDSNMG WSYGKNENLD LILSLGLVQG NTAPEKSGNS SAWAMLIFMC FWVLLLSVSF
     KVSILVSSR
 
 
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