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NPR6_ARATH
ID   NPR6_ARATH              Reviewed;         467 AA.
AC   Q9M1I7;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Regulatory protein NPR6;
DE   AltName: Full=BTB/POZ domain-containing protein NPR6;
DE   AltName: Full=Protein BLADE-ON-PETIOLE 1;
GN   Name=NPR6; Synonyms=BOP1; OrderedLocusNames=At3g57130; ORFNames=F24I3.210;
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;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   FUNCTION.
RX   PubMed=12441300; DOI=10.1242/dev.00196;
RA   Ha C.M., Kim G.T., Kim B.C., Jun J.H., Soh M.S., Ueno Y., Machida Y.,
RA   Tsukaya H., Nam H.G.;
RT   "The BLADE-ON-PETIOLE 1 gene controls leaf pattern formation through the
RT   modulation of meristematic activity in Arabidopsis.";
RL   Development 130:161-172(2003).
RN   [7]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=15564519; DOI=10.1093/pcp/pch201;
RA   Ha C.M., Jun J.H., Nam H.G., Fletcher J.C.;
RT   "BLADE-ON-PETIOLE1 encodes a BTB/POZ domain protein required for leaf
RT   morphogenesis in Arabidopsis thaliana.";
RL   Plant Cell Physiol. 45:1361-1370(2004).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15800002; DOI=10.1242/dev.01815;
RA   Norberg M., Holmlund M., Nilsson O.;
RT   "The BLADE ON PETIOLE genes act redundantly to control the growth and
RT   development of lateral organs.";
RL   Development 132:2203-2213(2005).
RN   [9]
RP   DOMAIN BTB.
RX   PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA   Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA   Vierstra R.D.;
RT   "Cullins 3a and 3b assemble with members of the broad
RT   complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT   ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL   J. Biol. Chem. 280:18810-18821(2005).
RN   [10]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH PAN.
RX   PubMed=15805484; DOI=10.1105/tpc.104.030536;
RA   Hepworth S.R., Zhang Y., McKim S., Li X., Haughn G.W.;
RT   "BLADE-ON-PETIOLE-dependent signaling controls leaf and floral patterning
RT   in Arabidopsis.";
RL   Plant Cell 17:1434-1448(2005).
RN   [11]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15634206; DOI=10.1111/j.1365-313x.2004.02296.x;
RA   Liu G., Holub E.B., Alonso J.M., Ecker J.R., Fobert P.R.;
RT   "An Arabidopsis NPR1-like gene, NPR4, is required for disease resistance.";
RL   Plant J. 41:304-318(2005).
RN   [12]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17601823; DOI=10.1105/tpc.107.051938;
RA   Ha C.M., Jun J.H., Nam H.G., Fletcher J.C.;
RT   "BLADE-ON-PETIOLE 1 and 2 control Arabidopsis lateral organ fate through
RT   regulation of LOB domain and adaxial-abaxial polarity genes.";
RL   Plant Cell 19:1809-1825(2007).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18339677; DOI=10.1242/dev.012807;
RA   McKim S.M., Stenvik G.E., Butenko M.A., Kristiansen W., Cho S.K.,
RA   Hepworth S.R., Aalen R.B., Haughn G.W.;
RT   "The BLADE-ON-PETIOLE genes are essential for abscission zone formation in
RT   Arabidopsis.";
RL   Development 135:1537-1546(2008).
RN   [14]
RP   FUNCTION.
RX   PubMed=20610407; DOI=10.1534/genetics.110.118703;
RA   Ha C.M., Jun J.H., Fletcher J.C.;
RT   "Control of Arabidopsis leaf morphogenesis through regulation of the YABBY
RT   and KNOX families of transcription factors.";
RL   Genetics 186:197-206(2010).
RN   [15]
RP   FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=20118228; DOI=10.1105/tpc.109.070763;
RA   Jun J.H., Ha C.M., Fletcher J.C.;
RT   "BLADE-ON-PETIOLE1 coordinates organ determinacy and axial polarity in
RT   arabidopsis by directly activating ASYMMETRIC LEAVES2.";
RL   Plant Cell 22:62-76(2010).
RN   [16]
RP   FUNCTION.
RX   PubMed=20626659; DOI=10.1111/j.1365-313x.2010.04299.x;
RA   Xu M., Hu T., McKim S.M., Murmu J., Haughn G.W., Hepworth S.R.;
RT   "Arabidopsis BLADE-ON-PETIOLE1 and 2 promote floral meristem fate and
RT   determinacy in a previously undefined pathway targeting APETALA1 and
RT   AGAMOUS-LIKE24.";
RL   Plant J. 63:974-989(2010).
CC   -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC       protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins (By similarity). Acts redundantly with BOP2. BOP1/2 promote
CC       leaf and floral meristem fate and determinacy in a pathway targeting
CC       AP1 and AGL24. BOP1/2 act as transcriptional co-regulators through
CC       direct interaction with TGA factors, including PAN, a direct regulator
CC       of AP1. Controls lateral organ fate through positive regulation of
CC       adaxial-abaxial polarity genes ATHB-14/PHB, YAB1/FIL and YAB3, and
CC       through positive regulation of LOB domain-containing genes LOB,
CC       LBD6/AS2 and LBD36. Promotes and maintains a developmentally
CC       determinate state in leaf cells through the negative regulation of JAG,
CC       JGL and class I KNOX genes. Is also involved in nectary development,
CC       formation of normal abscission zones and suppression of bract
CC       formation. {ECO:0000250, ECO:0000269|PubMed:12441300,
CC       ECO:0000269|PubMed:15564519, ECO:0000269|PubMed:15800002,
CC       ECO:0000269|PubMed:15805484, ECO:0000269|PubMed:17601823,
CC       ECO:0000269|PubMed:18339677, ECO:0000269|PubMed:20118228,
CC       ECO:0000269|PubMed:20610407, ECO:0000269|PubMed:20626659}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Homodimer or heterodimer with BOP2. Interacts with PAN.
CC       {ECO:0000269|PubMed:15805484, ECO:0000269|PubMed:20118228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20118228}. Nucleus
CC       {ECO:0000269|PubMed:20118228}.
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=Q9M1I7-1; Sequence=Displayed;
CC   -!- DEVELOPMENTAL STAGE: Initially detectable in embryos with a
CC       localization to the base of the developing cotyledons near the SAM.
CC       Expressed during vegetative development in young leaf primordia and at
CC       the base of the rosette leaves on the adaxial side. Expressed during
CC       reproductive development in young floral buds, and at the base of the
CC       sepals and petals. {ECO:0000269|PubMed:15564519}.
CC   -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC       of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC   -!- DISRUPTION PHENOTYPE: Defects in rosette leaf development. bop1 and
CC       bop2 double mutant displays leafy petioles, loss of floral organ
CC       abscission, and asymmetric flowers subtended by a bract.
CC       {ECO:0000269|PubMed:15800002, ECO:0000269|PubMed:15805484,
CC       ECO:0000269|PubMed:17601823, ECO:0000269|PubMed:18339677}.
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DR   EMBL; AL138655; CAB72183.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79617.1; -; Genomic_DNA.
DR   EMBL; DQ056629; AAY78777.1; -; mRNA.
DR   EMBL; BT026363; ABH04470.1; -; mRNA.
DR   EMBL; AB493655; BAH30493.1; -; mRNA.
DR   PIR; T47773; T47773.
DR   RefSeq; NP_191272.1; NM_115572.2. [Q9M1I7-1]
DR   AlphaFoldDB; Q9M1I7; -.
DR   SMR; Q9M1I7; -.
DR   BioGRID; 10196; 3.
DR   STRING; 3702.AT3G57130.1; -.
DR   PaxDb; Q9M1I7; -.
DR   PRIDE; Q9M1I7; -.
DR   ProteomicsDB; 250545; -. [Q9M1I7-1]
DR   EnsemblPlants; AT3G57130.1; AT3G57130.1; AT3G57130. [Q9M1I7-1]
DR   GeneID; 824880; -.
DR   Gramene; AT3G57130.1; AT3G57130.1; AT3G57130. [Q9M1I7-1]
DR   KEGG; ath:AT3G57130; -.
DR   Araport; AT3G57130; -.
DR   TAIR; locus:2080595; AT3G57130.
DR   eggNOG; KOG0504; Eukaryota.
DR   HOGENOM; CLU_028148_0_0_1; -.
DR   InParanoid; Q9M1I7; -.
DR   OMA; CSYLIAK; -.
DR   PhylomeDB; Q9M1I7; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9M1I7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M1I7; baseline and differential.
DR   Genevisible; Q9M1I7; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0010434; P:bract formation; IGI:UniProtKB.
DR   GO; GO:0010582; P:floral meristem determinacy; IGI:TAIR.
DR   GO; GO:0010227; P:floral organ abscission; IGI:UniProtKB.
DR   GO; GO:0048439; P:flower morphogenesis; IGI:TAIR.
DR   GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IGI:TAIR.
DR   GO; GO:0009965; P:leaf morphogenesis; IMP:UniProtKB.
DR   GO; GO:0010022; P:meristem determinacy; IMP:TAIR.
DR   GO; GO:0010254; P:nectary development; IGI:TAIR.
DR   GO; GO:0009944; P:polarity specification of adaxial/abaxial axis; IGI:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IGI:TAIR.
DR   Gene3D; 1.25.40.20; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR044284; NPR5/6.
DR   InterPro; IPR024228; NPR_central_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR46668; PTHR46668; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF11900; DUF3420; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cytoplasm; Nucleus; Reference proteome;
KW   Repeat; Ubl conjugation pathway.
FT   CHAIN           1..467
FT                   /note="Regulatory protein NPR6"
FT                   /id="PRO_0000407995"
FT   DOMAIN          27..111
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REPEAT          247..276
FT                   /note="ANK 1"
FT   REPEAT          277..306
FT                   /note="ANK 2"
FT   REPEAT          311..340
FT                   /note="ANK 3"
FT   REGION          434..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  51785 MW;  1A063A205DF86A62 CRC64;
     MSNTFEESLK SMSLDYLNLL INGQAFSDVT FSVEGRLVHA HRCILAARSL FFRKFFCESD
     PSQPGAEPAN QTGSGARAAA VGGVIPVNSV GYEVFLLLLQ FLYSGQVSIV PHKHEPRSNC
     GDRGCWHTHC TAAVDLSLDI LAAARYFGVE QLALLTQKHL TSMVEKASIE DVMKVLIASR
     KQDMHQLWTT CSYLIAKSGL PQEILAKHLP IELVAKIEEL RLKSSMPLRS LMPHHHDLTS
     TLDLEDQKIR RMRRALDSSD VELVKLMVMG EGLNLDESLA LIYAVENCSR EVVKALLELG
     AADVNYPAGP TGKTALHIAA EMVSPDMVAV LLDHHADPNV QTVDGITPLD ILRTLTSDFL
     FKGAIPGLTH IEPNKLRLCL ELVQSAALVI SREEGNNNSN DNNTMIYPRM KDEHTSGSSL
     DSRLVYLNLG ATNRDIGDDN SNQREGMNLH HHHHDPSTMY HHHHHHF
 
 
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