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NAC7_ARATH
ID   NAC7_ARATH              Reviewed;         395 AA.
AC   Q9FWX2; A1L4X4;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=NAC domain-containing protein 7 {ECO:0000303|PubMed:15029955};
DE            Short=ANAC007 {ECO:0000303|PubMed:15029955};
DE   AltName: Full=Protein EMBRYO DEFECTIVE 2749 {ECO:0000303|Ref.7};
DE   AltName: Full=Protein VASCULAR RELATED NAC-DOMAIN 4 {ECO:0000303|PubMed:16103214};
GN   Name=NAC007 {ECO:0000303|PubMed:15029955};
GN   Synonyms=EMB2749 {ECO:0000303|Ref.7}, VND4 {ECO:0000303|PubMed:16103214};
GN   OrderedLocusNames=At1g12260 {ECO:0000312|Araport:AT1G12260};
GN   ORFNames=T28K15.1 {ECO:0000312|EMBL:AAG12568.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY, AND
RP   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   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=17565617; DOI=10.1111/j.1365-313x.2007.03109.x;
RA   Ko J.-H., Yang S.H., Park A.H., Lerouxel O., Han K.-H.;
RT   "ANAC012, a member of the plant-specific NAC transcription factor family,
RT   negatively regulates xylary fiber development in Arabidopsis thaliana.";
RL   Plant J. 50:1035-1048(2007).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RA   Muralla R., Sweeney C., Lloyd J., Meinke D., Dickerman A.;
RT   "The Arabidopsis SeedGenes project: approaching saturation for essential
RT   genes.";
RL   (In) Abstracts of the 19th international conference on Arabidopsis
RL   research, pp.219-219, Montreal (2008).
RN   [8]
RP   TISSUE SPECIFICITY.
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   [9]
RP   INTERACTION WITH NAC083/VNI2.
RX   PubMed=20388856; DOI=10.1105/tpc.108.064048;
RA   Yamaguchi M., Ohtani M., Mitsuda N., Kubo M., Ohme-Takagi M., Fukuda H.,
RA   Demura T.;
RT   "VND-INTERACTING2, a NAC domain transcription factor, negatively regulates
RT   xylem vessel formation in Arabidopsis.";
RL   Plant Cell 22:1249-1263(2010).
RN   [10]
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:16103214,
CC       PubMed:25148240). {ECO:0000250|UniProtKB:Q9LVA1,
CC       ECO:0000269|PubMed:16103214, ECO:0000269|PubMed:25148240}.
CC   -!- SUBUNIT: Interacts with NAC083/VNI2. {ECO:0000269|PubMed:20388856}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C8W9,
CC       ECO:0000255|PROSITE-ProRule:PRU00353}.
CC   -!- TISSUE SPECIFICITY: Expressed in root, shoot and hypocotyl vascular
CC       elements, columella root caps, epidermal and cortex root cells and
CC       root-hypocotyl junctions. Observed predominantly in root imature xylem
CC       vessels (PubMed:18445131). Present in root developing xylems
CC       (PubMed:16103214, PubMed:17565617). Specifically expressed in vessels
CC       in the secondary xylem of the root-hypocotyl region, and in vessels but
CC       not in interfascicular fibers in stems (PubMed:25148240).
CC       {ECO:0000269|PubMed:16103214, ECO:0000269|PubMed:17565617,
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   -!- DISRUPTION PHENOTYPE: Embryo deffective. {ECO:0000269|Ref.7}.
CC   -!- SIMILARITY: Belongs to the plant vascular related NAC-domain protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG12568.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC022522; AAG12568.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28859.1; -; Genomic_DNA.
DR   EMBL; BT029761; ABM06031.1; -; mRNA.
DR   PIR; G86257; G86257.
DR   RefSeq; NP_172690.1; NM_101098.5.
DR   AlphaFoldDB; Q9FWX2; -.
DR   SMR; Q9FWX2; -.
DR   BioGRID; 23020; 1.
DR   IntAct; Q9FWX2; 1.
DR   STRING; 3702.AT1G12260.1; -.
DR   PaxDb; Q9FWX2; -.
DR   PRIDE; Q9FWX2; -.
DR   EnsemblPlants; AT1G12260.1; AT1G12260.1; AT1G12260.
DR   GeneID; 837780; -.
DR   Gramene; AT1G12260.1; AT1G12260.1; AT1G12260.
DR   KEGG; ath:AT1G12260; -.
DR   Araport; AT1G12260; -.
DR   TAIR; locus:2202028; AT1G12260.
DR   eggNOG; ENOG502QT6P; Eukaryota.
DR   HOGENOM; CLU_035664_1_2_1; -.
DR   InParanoid; Q9FWX2; -.
DR   OMA; PCKPELM; -.
DR   OrthoDB; 688436at2759; -.
DR   PhylomeDB; Q9FWX2; -.
DR   PRO; PR:Q9FWX2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FWX2; baseline and differential.
DR   Genevisible; Q9FWX2; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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..395
FT                   /note="NAC domain-containing protein 7"
FT                   /id="PRO_0000376615"
FT   DOMAIN          7..156
FT                   /note="NAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   DNA_BIND        107..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   REGION          344..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   395 AA;  45841 MW;  940618F84DD86A8A CRC64;
     MNSFSHVPPG FRFHPTDEEL VDYYLRKKVA SKRIEIDFIK DIDLYKIEPW DLQELCKIGH
     EEQSDWYFFS HKDKKYPTGT RTNRATKAGF WKATGRDKAI YLRHSLIGMR KTLVFYKGRA
     PNGQKSDWIM HEYRLETDEN GTPQEEGWVV CRVFKKRLAA VRRMGDYDSS PSHWYDDQLS
     FMASELETNG QRRILPNHHQ QQQHEHQQHM PYGLNASAYA LNNPNLQCKQ ELELHYNHLV
     QRNHLLDESH LSFLQLPQLE SPKIQQDNSN CNSLPYGTSN IDNNSSHNAN LQQSNIAHEE
     QLNQGNQNFS SLYMNSGNEQ VMDQVTDWRV LDKFVASQLS NEEAATASAS IQNNAKDTSN
     AEYQVDEEKD PKRASDMGEE YTASTSSSCQ IDLWK
 
 
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