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NAC68_ARATH
ID   NAC68_ARATH             Reviewed;         473 AA.
AC   A8MQY1; C0SVG8; O82591;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=NAC domain-containing protein 68 {ECO:0000303|PubMed:15029955};
DE            Short=ANAC068 {ECO:0000303|PubMed:15029955};
DE   AltName: Full=Protein NAC WITH TRANSMEMBRANE MOTIF 1;
DE   AltName: Full=Protein NTM1-like 12 {ECO:0000303|PubMed:17158162};
GN   Name=NAC68; Synonyms=NTL12 {ECO:0000303|PubMed:17158162}, NTM1;
GN   OrderedLocusNames=At4g01540; ORFNames=F11O4.4;
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=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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   DOI=10.1002/cfg.146;
RA   Paz-Ares J., Valencia A., Costantino P., Vittorioso P., Davies B.,
RA   Gilmartin P., Giraudat J., Parcy F., Reindl A., Sablowski R., Coupland G.,
RA   Martin C., Angenent G.C., Baeumlein H., Mock H.-P., Carbonero P.,
RA   Colombo L., Tonelli C., Engstroem P., Droege-Laser W., Gatz C.,
RA   Kavanagh T., Kushnir S., Zabeau M., Laux T., Hordsworth M., Ruberti I.,
RA   Ratcliff F., Smeekens S., Somssich I., Weisshaar B., Traas J.;
RT   "REGIA, an EU project on functional genomics of transcription factors from
RT   Arabidopsis thaliana.";
RL   Comp. Funct. Genomics 3:102-108(2002).
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, INDUCTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND GENE
RP   FAMILY.
RX   PubMed=17098812; DOI=10.1105/tpc.106.043018;
RA   Kim Y.-S., Kim S.-G., Park J.-E., Park H.-Y., Lim M.-H., Chua N.-H.,
RA   Park C.-M.;
RT   "A membrane-bound NAC transcription factor regulates cell division in
RT   Arabidopsis.";
RL   Plant Cell 18:3132-3144(2006).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
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).
CC   -!- FUNCTION: Transcription activator activated by proteolytic cleavage
CC       through regulated intramembrane proteolysis (RIP) mediated by calpain
CC       or its functional homolog. Regulates cytokinin signaling during cell
CC       division. {ECO:0000269|PubMed:17098812}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17098812}; Single-
CC       pass membrane protein {ECO:0000269|PubMed:17098812}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:17098812}.
CC       Note=Localized primarily in plasma membrane or endoplasmic reticulum
CC       membrane as dormant form and, upon specific stress or signal, is
CC       processed into a transcriptionally active and nuclear form after a
CC       proteolytic cleavage through regulated intramembrane proteolysis (RIP).
CC       {ECO:0000269|PubMed:17098812}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=A8MQY1-1; Sequence=Displayed;
CC   -!- INDUCTION: Stabilized by cytokinins. {ECO:0000269|PubMed:17098812}.
CC   -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC       domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC62780.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB77724.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF096370; AAC62780.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161492; CAB77724.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82038.1; -; Genomic_DNA.
DR   EMBL; DR751097; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; DR751098; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AB493671; BAH30509.1; -; mRNA.
DR   PIR; T01940; T01940.
DR   RefSeq; NP_001078343.1; NM_001084874.1.
DR   RefSeq; NP_192063.2; NM_116384.3. [A8MQY1-1]
DR   AlphaFoldDB; A8MQY1; -.
DR   SMR; A8MQY1; -.
DR   BioGRID; 13438; 2.
DR   IntAct; A8MQY1; 2.
DR   STRING; 3702.AT4G01540.1; -.
DR   PaxDb; A8MQY1; -.
DR   PRIDE; A8MQY1; -.
DR   EnsemblPlants; AT4G01540.1; AT4G01540.1; AT4G01540. [A8MQY1-1]
DR   GeneID; 828149; -.
DR   Gramene; AT4G01540.1; AT4G01540.1; AT4G01540. [A8MQY1-1]
DR   KEGG; ath:AT4G01540; -.
DR   Araport; AT4G01540; -.
DR   TAIR; locus:2116972; AT4G01540.
DR   InParanoid; A8MQY1; -.
DR   OrthoDB; 893230at2759; -.
DR   PhylomeDB; A8MQY1; -.
DR   PRO; PR:A8MQY1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; A8MQY1; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0009736; P:cytokinin-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR   GO; GO:0051302; P:regulation of cell division; 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; Alternative splicing; DNA-binding; Membrane; Nucleus;
KW   Reference proteome; Stress response; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..473
FT                   /note="NAC domain-containing protein 68"
FT                   /id="PRO_0000323714"
FT   TRANSMEM        446..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          4..154
FT                   /note="NAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   DNA_BIND        108..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT   REGION          326..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        187
FT                   /note="Q -> R (in Ref. 3; DR751097)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281..282
FT                   /note="DN -> RH (in Ref. 3; DR751097)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   473 AA;  53599 MW;  A30308E26C68ACB3 CRC64;
     MMKGLIGYRF SPTGEEVINH YLKNKLLGKY WLVDEAISEI NILSHKPSKD LPKLARIQSE
     DLEWYFFSPI EYTNPNKMKM KRTTGSGFWK PTGVDREIRD KRGNGVVIGI KKTLVYHEGK
     SPHGVRTPWV MHEYHITCLP HHKRKYVVCQ VKYKGEAAEI SYEPSPSLVS DSHTVIAITG
     EPEPELQVEQ PGKENLLGMS VDDLIEPMNQ QEEPQGPHLA PNDDEFIRGL RHVDRGTVEY
     LFANEENMDG LSMNDLRIPM IVQQEDLSEW EGFNADTFFS DNNNNYNLNV HHQLTPYGDG
     YLNAFSGYNE GNPPDHELVM QENRNDHMPR KPVTGTIDYS SDSGSDAGSI STTSYQGTSS
     PNISVGSSSR HLSSCSSTDS CKDLQTCTDP SIISREIREL TQEVKQEIPR AVDAPMNNES
     SLVKTEKKGL FIVEDAMERN RKKPRFIYLM KMIIGNIISV LLPVKRLIPV KKL
 
 
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