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NAC81_ARATH
ID   NAC81_ARATH             Reviewed;         283 AA.
AC   Q9C598; Q38968; Q8GWD8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Protein ATAF2;
DE   AltName: Full=NAC domain-containing protein 81;
DE            Short=ANAC081;
GN   Name=NAC081; Synonyms=ATAF2; OrderedLocusNames=At5g08790;
GN   ORFNames=T2K12.140;
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 [MRNA] (ISOFORM 1).
RA   Rueth J., Schweyen R., Hirt H.;
RL   Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=16115070; DOI=10.1111/j.1365-313x.2005.02488.x;
RA   Delessert C., Kazan K., Wilson I.W., Van Der Straeten D., Manners J.,
RA   Dennis E.S., Dolferus R.;
RT   "The transcription factor ATAF2 represses the expression of pathogenesis-
RT   related genes in Arabidopsis.";
RL   Plant J. 43:745-757(2005).
RN   [9]
RP   INDUCTION BY CHITIN ELICITOR.
RX   PubMed=17722694; DOI=10.1094/mpmi-20-8-0900;
RA   Libault M., Wan J., Czechowski T., Udvardi M., Stacey G.;
RT   "Identification of 118 Arabidopsis transcription factor and 30 ubiquitin-
RT   ligase genes responding to chitin, a plant-defense elicitor.";
RL   Mol. Plant Microbe Interact. 20:900-911(2007).
RN   [10]
RP   INTERACTION WITH AHK2.
RX   PubMed=18642946; DOI=10.1021/pr0703831;
RA   Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT   "Toward an interaction map of the two-component signaling pathway of
RT   Arabidopsis thaliana.";
RL   J. Proteome Res. 7:3649-3660(2008).
RN   [11]
RP   FUNCTION.
RX   PubMed=18849494; DOI=10.1105/tpc.108.060160;
RA   Kunieda T., Mitsuda N., Ohme-Takagi M., Takeda S., Aida M., Tasaka M.,
RA   Kondo M., Nishimura M., Hara-Nishimura I.;
RT   "NAC family proteins NARS1/NAC2 and NARS2/NAM in the outer integument
RT   regulate embryogenesis in Arabidopsis.";
RL   Plant Cell 20:2631-2642(2008).
RN   [12]
RP   FUNCTION, INTERACTION WITH TOBAMOVIRUS REPLICASE, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=19625399; DOI=10.1128/jvi.00941-09;
RA   Wang X., Goregaoker S.P., Culver J.N.;
RT   "Interaction of the tobacco mosaic virus replicase protein with a NAC
RT   domain transcription factor is associated with the suppression of systemic
RT   host defenses.";
RL   J. Virol. 83:9720-9730(2009).
RN   [13]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=22937923; DOI=10.1186/1471-2229-12-157;
RA   Wang X., Culver J.N.;
RT   "DNA binding specificity of ATAF2, a NAC domain transcription factor
RT   targeted for degradation by tobacco mosaic virus.";
RL   BMC Plant Biol. 12:157-157(2012).
RN   [14]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22965747; DOI=10.1007/s10059-012-0122-2;
RA   Huh S.U., Lee S.B., Kim H.H., Paek K.H.;
RT   "ATAF2, a NAC transcription factor, binds to the promoter and regulates
RT   NIT2 gene expression involved in auxin biosynthesis.";
RL   Mol. Cells 34:305-313(2012).
RN   [15]
RP   INTERACTION WITH AHL12 AND AHL27.
RX   PubMed=24218605; DOI=10.1073/pnas.1219277110;
RA   Zhao J., Favero D.S., Peng H., Neff M.M.;
RT   "Arabidopsis thaliana AHL family modulates hypocotyl growth redundantly by
RT   interacting with each other via the PPC/DUF296 domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:E4688-E4697(2013).
RN   [16]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=26493403; DOI=10.1242/dev.124347;
RA   Peng H., Zhao J., Neff M.M.;
RT   "ATAF2 integrates Arabidopsis brassinosteroid inactivation and seedling
RT   photomorphogenesis.";
RL   Development 142:4129-4138(2015).
RN   [17]
RP   FUNCTION.
RX   PubMed=26518251; DOI=10.1111/tpj.13067;
RA   Takasaki H., Maruyama K., Takahashi F., Fujita M., Yoshida T.,
RA   Nakashima K., Myouga F., Toyooka K., Yamaguchi-Shinozaki K., Shinozaki K.;
RT   "SNAC-As, stress-responsive NAC transcription factors, mediate ABA-
RT   inducible leaf senescence.";
RL   Plant J. 84:1114-1123(2015).
CC   -!- FUNCTION: Involved in disease resistance response (PubMed:16115070,
CC       PubMed:19625399). May function as repressor of pathogenesis-related
CC       proteins (PubMed:16115070). May function in the regulation of host
CC       basal defense responses against viral infection (PubMed:19625399).
CC       Transcriptional activator involved in responses to wounding and
CC       infection with tobamovirus (TMV) (PubMed:22937923). Binds to the DNA
CC       sequences 5'-AAAATATCT-3' and 5'AGATTTTT-3' of CYP734A1/BAS1 and
CC       CYP72C1/SOB7 promoters, respectively. Acts as suppressor of the
CC       brassinosteroid (BR)-inactivating enzymes CYP734A1/BAS1 and
CC       CYP72C1/SOB7, and prevents their expression in almost all tissues.
CC       Plays a central role in integrating BR homeostasis and seedling
CC       development. Regulates the spatial regulation of BR homeostasis and
CC       participates in the regulation of hypocotyl elongation and root growth
CC       by suppressing BR catabolism. Mediates connection between BR catabolism
CC       and photomorphogenesis (PubMed:26493403). Binds to, and transactivates
CC       the promoter of the auxin biosynthetic gene NIT2 (PubMed:22965747).
CC       Stress-responsive NAC transcription factor involved in ABA-inducible
CC       leaf senescence signaling (PubMed:26518251). Required for normal seed
CC       development and morphology (PubMed:18849494).
CC       {ECO:0000269|PubMed:16115070, ECO:0000269|PubMed:18849494,
CC       ECO:0000269|PubMed:19625399, ECO:0000269|PubMed:22937923,
CC       ECO:0000269|PubMed:22965747, ECO:0000269|PubMed:26493403,
CC       ECO:0000269|PubMed:26518251}.
CC   -!- SUBUNIT: Homodimer (PubMed:22937923). Interacts with AHK2
CC       (PubMed:18642946). Interacts with AHL12 and AHL27 (PubMed:24218605).
CC       Interacts with the helicase domain of the tobamovirus (TMV) replicase
CC       (PubMed:19625399). {ECO:0000269|PubMed:18642946,
CC       ECO:0000269|PubMed:19625399, ECO:0000269|PubMed:22937923,
CC       ECO:0000269|PubMed:24218605}.
CC   -!- INTERACTION:
CC       Q9C598; Q8S3D1: BHLH68; NbExp=3; IntAct=EBI-1998565, EBI-15192111;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353,
CC       ECO:0000269|PubMed:19625399}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9C598-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9C598-2; Sequence=VSP_039771, VSP_039772;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, rosette leaves,
CC       cauline leaves and mature flowers. Expressed at low levels in stems and
CC       flower buds. {ECO:0000269|PubMed:16115070}.
CC   -!- INDUCTION: Induced by wounding, salicylic acid (SA), methyl jasmonate,
CC       drought stress, dark and sucrose starvation (PubMed:16115070). Induced
CC       by chitin elicitor (chitooctaose) (PubMed:17722694). Induced by
CC       salicylic acid and infection with tobamovirus (TMV) (PubMed:19625399).
CC       By indole-3-acetonitrile, salicylic acid (SA), sodium nitroprusside
CC       (SNP), salt stress and drought stress (PubMed:22965747). Down-regulated
CC       by brassinosteroid (BR) and transition from dark to white light
CC       (PubMed:26493403). {ECO:0000269|PubMed:16115070,
CC       ECO:0000269|PubMed:17722694, ECO:0000269|PubMed:19625399,
CC       ECO:0000269|PubMed:22965747, ECO:0000269|PubMed:26493403}.
CC   -!- DOMAIN: The NAC domain includes a DNA-binding domain and a dimerization
CC       domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC   -!- DISRUPTION PHENOTYPE: Reduced sensitivity to indole-3-acetonitrile.
CC       {ECO:0000269|PubMed:22965747}.
CC   -!- MISCELLANEOUS: Plants over-expressing NAC081 show enhanced
CC       susceptibility to the necrotrophic fungal pathogen Fusarium oxysporum
CC       (PubMed:16115070). Plants over-expressing NAC081 exhibit abnormal
CC       developmental phenotypes such as dwarfism and leaf-yellowing
CC       (PubMed:22965747). Plants silencing NAC081 produce abnormally shaped
CC       seeds (PubMed:18849494). {ECO:0000269|PubMed:16115070,
CC       ECO:0000269|PubMed:18849494, ECO:0000269|PubMed:22965747}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA52772.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA52772.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X74756; CAA52772.1; ALT_SEQ; mRNA.
DR   EMBL; AL590346; CAC35884.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91350.1; -; Genomic_DNA.
DR   EMBL; AK118910; BAC43493.1; -; mRNA.
DR   EMBL; AY080862; AAL87335.1; -; mRNA.
DR   EMBL; AY133762; AAM91696.1; -; mRNA.
DR   EMBL; AK228803; BAF00699.1; -; mRNA.
DR   PIR; S37100; S37100.
DR   RefSeq; NP_680161.1; NM_147856.4. [Q9C598-1]
DR   AlphaFoldDB; Q9C598; -.
DR   SMR; Q9C598; -.
DR   BioGRID; 16057; 25.
DR   IntAct; Q9C598; 19.
DR   STRING; 3702.AT5G08790.1; -.
DR   PaxDb; Q9C598; -.
DR   PRIDE; Q9C598; -.
DR   ProteomicsDB; 251269; -. [Q9C598-1]
DR   EnsemblPlants; AT5G08790.1; AT5G08790.1; AT5G08790. [Q9C598-1]
DR   GeneID; 830779; -.
DR   Gramene; AT5G08790.1; AT5G08790.1; AT5G08790. [Q9C598-1]
DR   KEGG; ath:AT5G08790; -.
DR   Araport; AT5G08790; -.
DR   TAIR; locus:504956335; AT5G08790.
DR   eggNOG; ENOG502QVRF; Eukaryota.
DR   HOGENOM; CLU_035664_3_1_1; -.
DR   InParanoid; Q9C598; -.
DR   OMA; RSPWMES; -.
DR   PhylomeDB; Q9C598; -.
DR   PRO; PR:Q9C598; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9C598; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR   GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IPI:TAIR.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR   GO; GO:0010150; P:leaf senescence; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
DR   GO; GO:0010099; P:regulation of photomorphogenesis; IMP:UniProtKB.
DR   GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR   GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR   GO; GO:0009744; P:response to sucrose; IEP:TAIR.
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   Activator; Alternative splicing; DNA-binding; Host-virus interaction;
KW   Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..283
FT                   /note="Protein ATAF2"
FT                   /id="PRO_0000398601"
FT   DOMAIN          7..159
FT                   /note="NAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   DNA_BIND        103..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   REGION          171..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         148..153
FT                   /note="LDDWVL -> VSSVSY (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11910074"
FT                   /id="VSP_039771"
FT   VAR_SEQ         154..283
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11910074"
FT                   /id="VSP_039772"
SQ   SEQUENCE   283 AA;  32225 MW;  0EA26ADF23B94A7C CRC64;
     MKSELNLPAG FRFHPTDEEL VKFYLCRKCA SEQISAPVIA EIDLYKFNPW ELPEMSLYGE
     KEWYFFSPRD RKYPNGSRPN RAAGTGYWKA TGADKPIGKP KTLGIKKALV FYAGKAPKGI
     KTNWIMHEYR LANVDRSASV NKKNNLRLDD WVLCRIYNKK GTMEKYFPAD EKPRTTTMAE
     QSSSPFDTSD STYPTLQEDD SSSSGGHGHV VSPDVLEVQS EPKWGELEDA LEAFDTSMFG
     SSMELLQPDA FVPQFLYQSD YFTSFQDPPE QKPFLNWSFA PQG
 
 
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