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NAC76_ARATH
ID   NAC76_ARATH             Reviewed;         377 AA.
AC   O65508;
DT   27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=NAC domain-containing protein 76 {ECO:0000303|PubMed:15029955};
DE            Short=ANAC076 {ECO:0000303|PubMed:15029955};
DE   AltName: Full=Protein VASCULAR RELATED NAC-DOMAIN 2 {ECO:0000303|PubMed:16103214};
GN   Name=NAC076 {ECO:0000303|PubMed:15029955};
GN   Synonyms=VND2 {ECO:0000303|PubMed:16103214};
GN   OrderedLocusNames=At4g36160 {ECO:0000312|Araport:AT4G36160};
GN   ORFNames=F23E13.50 {ECO:0000312|EMBL:CAA18122.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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   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   [4]
RP   DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16103214; DOI=10.1101/gad.1331305;
RA   Kubo M., Udagawa M., Nishikubo N., Horiguchi G., Yamaguchi M., Ito J.,
RA   Mimura T., Fukuda H., Demura T.;
RT   "Transcription switches for protoxylem and metaxylem vessel formation.";
RL   Genes Dev. 19:1855-1860(2005).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16581911; DOI=10.1073/pnas.0510607103;
RA   Lee J.-Y., Colinas J., Wang J.Y., Mace D., Ohler U., Benfey P.N.;
RT   "Transcriptional and posttranscriptional regulation of transcription factor
RT   expression in Arabidopsis roots.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6055-6060(2006).
RN   [6]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH NAC030/VND7.
RC   STRAIN=cv. Columbia;
RX   PubMed=18445131; DOI=10.1111/j.1365-313x.2008.03533.x;
RA   Yamaguchi M., Kubo M., Fukuda H., Demura T.;
RT   "Vascular-related NAC-DOMAIN7 is involved in the differentiation of all
RT   types of xylem vessels in Arabidopsis roots and shoots.";
RL   Plant J. 55:652-664(2008).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=25148240; DOI=10.1371/journal.pone.0105726;
RA   Zhou J., Zhong R., Ye Z.-H.;
RT   "Arabidopsis NAC domain proteins, VND1 to VND5, are transcriptional
RT   regulators of secondary wall biosynthesis in vessels.";
RL   PLoS ONE 9:E105726-E105726(2014).
CC   -!- FUNCTION: Transcription activator that binds to the secondary wall NAC
CC       binding element (SNBE), 5'-
CC       (T/A)NN(C/T)(T/C/G)TNNNNNNNA(A/C)GN(A/C/T)(A/T)-3', in the promoter of
CC       target genes (By similarity). Involved in xylem formation by promoting
CC       the expression of secondary wall-associated transcription factors and
CC       of genes involved in secondary wall biosynthesis and programmed cell
CC       death, genes driven by the secondary wall NAC binding element (SNBE).
CC       Triggers thickening of secondary walls (PubMed:25148240).
CC       {ECO:0000250|UniProtKB:Q9LVA1, ECO:0000269|PubMed:25148240}.
CC   -!- SUBUNIT: Interacts with NAC030/VND7. {ECO:0000269|PubMed:18445131}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C8W9,
CC       ECO:0000255|PROSITE-ProRule:PRU00353}.
CC   -!- TISSUE SPECIFICITY: Detected in root protoxylem and metaxylem poles and
CC       in vessels of protoxylems, outermost metaxylems, inner metaxylems,
CC       shoots and hypocotyls (PubMed:18445131). Expressed in roots,
CC       hypocotyls, cotyledons and leaves. Present in developing xylems
CC       (PubMed:16103214, PubMed:16581911). Specifically expressed in vessels
CC       but not in interfascicular fibers in stems (PubMed:25148240).
CC       {ECO:0000269|PubMed:16103214, ECO:0000269|PubMed:16581911,
CC       ECO:0000269|PubMed:18445131, ECO:0000269|PubMed:25148240}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during xylem vessel element
CC       formation. Expressed preferentially in procambial cells adjacent to
CC       root meristem. {ECO:0000269|PubMed:16103214,
CC       ECO:0000269|PubMed:25148240}.
CC   -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC       domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC   -!- SIMILARITY: Belongs to the plant vascular related NAC-domain protein
CC       family. {ECO:0000305}.
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DR   EMBL; AL022141; CAA18122.1; -; Genomic_DNA.
DR   EMBL; AL161588; CAB81525.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86626.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67680.1; -; Genomic_DNA.
DR   PIR; T04585; T04585.
DR   RefSeq; NP_001329496.1; NM_001342407.1.
DR   RefSeq; NP_195339.1; NM_119783.3.
DR   AlphaFoldDB; O65508; -.
DR   SMR; O65508; -.
DR   IntAct; O65508; 1.
DR   STRING; 3702.AT4G36160.1; -.
DR   PaxDb; O65508; -.
DR   PRIDE; O65508; -.
DR   EnsemblPlants; AT4G36160.1; AT4G36160.1; AT4G36160.
DR   EnsemblPlants; AT4G36160.3; AT4G36160.3; AT4G36160.
DR   GeneID; 829773; -.
DR   Gramene; AT4G36160.1; AT4G36160.1; AT4G36160.
DR   Gramene; AT4G36160.3; AT4G36160.3; AT4G36160.
DR   KEGG; ath:AT4G36160; -.
DR   Araport; AT4G36160; -.
DR   TAIR; locus:2122219; AT4G36160.
DR   eggNOG; ENOG502QQGU; Eukaryota.
DR   HOGENOM; CLU_035664_1_2_1; -.
DR   InParanoid; O65508; -.
DR   PhylomeDB; O65508; -.
DR   PRO; PR:O65508; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O65508; baseline and differential.
DR   Genevisible; O65508; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:1901348; P:positive regulation of secondary cell wall biogenesis; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR   GO; GO:0048759; P:xylem vessel member cell differentiation; 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 wall biogenesis/degradation; Developmental protein;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..377
FT                   /note="NAC domain-containing protein 76"
FT                   /id="PRO_0000433122"
FT   DOMAIN          10..159
FT                   /note="NAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   DNA_BIND        110..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   REGION          312..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   377 AA;  43517 MW;  E391DF7A568CE4E7 CRC64;
     MESVDQSCSV PPGFRFHPTD EELVGYYLRK KVASQKIDLD VIRDIDLYRI EPWDLQESCR
     IGYEERNEWY FFSHKDKKYP TGTRTNRATM AGFWKATGRD KAVYDKSKLI GMRKTLVFYK
     GRAPNGQKTD WIMHEYRLES DENAPPQEEG WVVCRAFKKK PMTGQAKNTE TWSSSYFYDE
     LPSGVRSVTE PLNYVSKQKQ NVFAQDLMFK QELEGSDIGL NFIHCDQFIQ LPQLESPSLP
     LTKRPVSLTS ITSLEKNKNI YKRHLIEEDV SFNALISSGN KDKKKKKTSV MTTDWRALDK
     FVASQLMSQE DGVSGFGGHH EEDNNKIGHY NNEESNNKGS VETASSTLLS DREEENRFIS
     GLLCSNLDYD LYRDLHV
 
 
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