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UniProtKB/Swiss-Prot entry O22476


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BRI1_ARATH
Primary accession number O22476
Secondary accession numbers None
Integrated into Swiss-Prot on March 28, 2003
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 85)
Name and origin of the protein
Protein name Protein BRASSINOSTEROID INSENSITIVE 1 [Precursor]
Synonyms AtBRI1
EC 2.7.11.1
Brassinosteroid LRR receptor kinase
Gene name
Name: BRI1
OrderedLocusNames: At4g39400
ORFNames: F23K16.30
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND MUTANTS BRI1-101; BRI1-104; BRI1-113 AND BRI1-115.
STRAIN=cv. Columbia;
DOI=10.1016/S0092-8674(00)80357-8; PubMed=9298904 [NCBI, ExPASy, EBI, Israel, Japan]
Li J., Chory J.;
"A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction.";
Cell 90:929-938(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTANTS BRI1-5/DWF2-W41; BRI1-6/BRI1-119/DWF2-399; BRI1-7/DWF2-WM3-2; BRI1-8/DWF2-WM6-2 AND BRI1-9/DWF2-WMB19.
STRAIN=cv. En-2, and cv. Wassilewskija-2;
DOI=10.1104/pp.121.3.743; PubMed=10557222 [NCBI, ExPASy, EBI, Israel, Japan]
Noguchi T., Fujioka S., Choe S., Takatsuto S., Yoshida S., Yuan H., Feldmann K.A., Tax F.E.;
"Brassinosteroid-insensitive dwarf mutants of Arabidopsis accumulate brassinosteroids.";
Plant Physiol. 121:743-752(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTANTS BRI1-1; BRI1-108; BRI1-117 AND BRI1-102.
STRAIN=cv. Columbia;
DOI=10.1104/pp.123.4.1247; PubMed=10938344 [NCBI, ExPASy, EBI, Israel, Japan]
Friedrichsen D.M., Joazeiro C.A.P., Li J., Hunter T., Chory J.;
"BRASSINOSTEROID-INSENSITIVE-1 is a ubiquitously expressed leucine-rich repeat receptor serine/threonine kinase.";
Plant Physiol. 123:1247-1256(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[5]
PHOSPHORYLATION, AND MUTAGENESIS OF LYS-911.
DOI=10.1104/pp.124.2.751; PubMed=11027724 [NCBI, ExPASy, EBI, Israel, Japan]
Oh M.-H., Ray W.K., Huber S.C., Asara J.M., Gage D.A., Clouse S.D.;
"Recombinant BRASSINOSTEROID INSENSITIVE 1 receptor-like kinase autophosphorylates on serine and threonine residues and phosphorylates a conserved peptide motif in vitro.";
Plant Physiol. 124:751-766(2000).
[6]
STEROID-BINDING.
DOI=10.1126/science.288.5475.2360; PubMed=10875920 [NCBI, ExPASy, EBI, Israel, Japan]
He Z., Wang Z.-Y., Li J., Zhu Q., Lamb C., Ronald P., Chory J.;
"Perception of brassinosteroids by the extracellular domain of the receptor kinase BRI1.";
Science 288:2360-2363(2000).
[7]
SUBCELLULAR LOCATION, STEROID-BINDING, AND AUTOPHOSPHORYLATION.
DOI=10.1038/35066597; PubMed=11268216 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Z.-Y., Seto H., Fujioka S., Yoshida S., Chory J.;
"BRI1 is a critical component of a plasma-membrane receptor for plant steroids.";
Nature 410:380-383(2001).
[8]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH BAK1.
DOI=10.1016/S0092-8674(02)00814-0; PubMed=12150928 [NCBI, ExPASy, EBI, Israel, Japan]
Nam K.H., Li J.;
"BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling.";
Cell 110:203-212(2002).
[9]
PHOSPHORYLATION, AND INTERACTION WITH BAK1.
DOI=10.1016/S0092-8674(02)00812-7; PubMed=12150929 [NCBI, ExPASy, EBI, Israel, Japan]
Li J., Wen J., Lease K.A., Doke J.T., Tax F.E., Walker J.C.;
"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling.";
Cell 110:213-222(2002).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH BAK1.
DOI=10.1105/tpc.104.025387; PubMed=15548744 [NCBI, ExPASy, EBI, Israel, Japan]
Russinova E., Borst J.-W., Kwaaitaal M., Cano-Delgado A., Yin Y., Chory J., de Vries S.C.;
"Heterodimerization and endocytosis of Arabidopsis brassinosteroid receptors BRI1 and AtSERK3 (BAK1).";
Plant Cell 16:3216-3229(2004).
[11]
INTERACTION WITH TTL.
DOI=10.1105/tpc.104.023903; PubMed=15319482 [NCBI, ExPASy, EBI, Israel, Japan]
Nam K.H., Li J.;
"The Arabidopsis transthyretin-like protein is a potential substrate of BRASSINOSTEROID-INSENSITIVE 1.";
Plant Cell 16:2406-2417(2004).
[12]
PHOSPHORYLATION, INTERACTION WITH BAK1, AND MUTAGENESIS OF SER-838; THR-842; THR-846; SER-858; THR-872; THR-1039; SER-1044; THR-1045; THR-1049; SER-1168; SER-1172; 1179-SER-THR-1180 AND SER-1187.
DOI=10.1105/tpc.105.031393; PubMed=15894717 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Goshe M.B., Soderblom E.J., Phinney B.S., Kuchar J.A., Li J., Asami T., Yoshida S., Huber S.C., Clouse S.D.;
"Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.";
Plant Cell 17:1685-1703(2005).
Comments
  • FUNCTION: Receptor with a serine/threonine-protein kinase activity. Regulates, in response to brassinosteroid binding, a signaling cascade involved in plant development, including expression of light- and stress-regulated genes, promotion of cell elongation, normal leaf and chloroplast senescence, and flowering. Binds brassinolide, and less effectively castasterone, but not 2,3,22,23-O-tetramethylbrassinolide or ecdysone. May be involved in a feedback regulation of brassinosteroid biosynthesis. Phosphorylates BRI1-associated receptor kinase 1 (BAK1) and Transthyretin-Like protein (TTL) in vitro.
  • CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
  • ENZYME REGULATION: Activated by Ser and Thr phosphorylation.
  • SUBUNIT: Homodimer in the plasma membrane (Probable). Heterodimer with BAK1 in the endosomes. Interacts with TTL in a kinase-dependent manner.
  • INTERACTION:
    Self; NbExp=2; IntAct=EBI-1797828, EBI-1797828;
    Q94AG2:-; NbExp=2; IntAct=EBI-1797828, EBI-1555537;
    Q944A7:At4g35230; NbExp=4; IntAct=EBI-1797828, EBI-1797846;
    Q94F62:BAK1; NbExp=4; IntAct=EBI-1797828, EBI-617138;
    O65280:F6N23.9; NbExp=2; IntAct=EBI-1797828, EBI-1797930;
  • SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein.
  • TISSUE SPECIFICITY: Expressed ubiquitously.
  • DEVELOPMENTAL STAGE: Expressed constitutively in either dark- or light-grown seedlings.
  • DOMAIN: Contains one leucine-zipper motif and two pairs of conservatively spaced Cys (Cys pair 1 and 2) involved in forming heterodimers.
  • DOMAIN: A 70 amino acid island between the 20th and the 21th LRR is essential for the binding of brassinosteroids.
  • PTM: Phosphorylated on at least 12 sites, with a preference for Ser residues.
  • MISCELLANEOUS: Binding of brassinosteroid induces intramolecular autophosphorylation of BRI1. Interaction with BAK1 activates both receptor kinases and the full activation of either receptor kinase requires transphosphorylation by their partners. Optimum in vitro phosphorylation of the substrate requires Arg or Lys residues at P-3, P-4, and P+5 (relative to the phosphorylated amino acid at P=0).
  • SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
  • SIMILARITY: Contains 25 LRR (leucine-rich) repeats.
  • SIMILARITY: Contains 1 protein kinase domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF017056; AAC49810.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL078620; CAB44675.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161595; CAB80603.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T09356; T09356.
RefSeq NP_195650.1; -.
UniGene At.27898
3D structure databases
ModBase O22476.
Protein-protein interaction databases
IntAct O22476; 6.
Organism-specific databases
GeneFarm 612; 54.
TAIR At4g39400; -.
Gene expression databases
ArrayExpress O22476; -.
GermOnline AT4G39400; Arabidopsis thaliana.
Ontologies
GO
GO:0010008; Cellular component: endosome membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0043234; Cellular component: protein complex (inferred from physical interaction from TAIR).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from physical interaction from TAIR).
GO:0042803; Molecular function: protein homodimerization activity (inferred from direct assay from TAIR).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from InterPro).
GO:0004872; Molecular function: receptor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005496; Molecular function: steroid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0010268; Biological process: brassinosteroid homeostasis (inferred from expression pattern from TAIR).
GO:0009729; Biological process: detection of brassinosteroid stimulus (inferred from mutant phenotype from TAIR).
GO:0009911; Biological process: positive regulation of flower development (inferred from genetic interaction from TAIR).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0010224; Biological process: response to UV-B (inferred from genetic interaction from TAIR).
QuickGo view.
Family and domain databases
InterPro IPR001611; LRR.
IPR013210; LRR_N.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.
Pfam PF00560; LRR_1; 19.
PF08263; LRRNT_2; 1.
PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
PRINTS PR00019; LEURICHRPT.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE O22476; -.
Genome annotation databases
GeneID 830095; -.
GenomeReviews CT486007_GR; AT4G39400.
KEGG ath:AT4G39400; -.
NMPDR fig|3702.1.peg.22077; -.
Other
ProtoNet O22476.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell membrane; Complete proteome; Endosome; Glycoprotein; Kinase; Leucine-rich repeat; Lipid-binding; Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Serine/threonine-protein kinase; Signal; Steroid-binding; Transferase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     23  23     Potential. 
CHAIN   24   1196  1173     Protein BRASSINOSTEROID INSENSITIVE 1. PRO_0000024305
TRANSMEM   793    813  21     Potential. 
REPEAT   98    121  24     LRR 1. 
REPEAT   122    146  25     LRR 2. 
REPEAT   148    169  22     LRR 3. 
REPEAT   172    197  26     LRR 4. 
REPEAT   199    221  23     LRR 5. 
REPEAT   222    244  23     LRR 6. 
REPEAT   245    268  24     LRR 7. 
REPEAT   269    290  22     LRR 8. 
REPEAT   291    314  24     LRR 9. 
REPEAT   316    338  23     LRR 10. 
REPEAT   339    363  25     LRR 11. 
REPEAT   364    388  25     LRR 12. 
REPEAT   390    413  24     LRR 13. 
REPEAT   415    439  25     LRR 14. 
REPEAT   441    463  23     LRR 15. 
REPEAT   464    487  24     LRR 16. 
REPEAT   488    511  24     LRR 17. 
REPEAT   513    535  23     LRR 18. 
REPEAT   536    559  24     LRR 19. 
REPEAT   561    583  23     LRR 20. 
REPEAT   653    677  25     LRR 21. 
REPEAT   678    701  24     LRR 22. 
REPEAT   702    725  24     LRR 23. 
REPEAT   727    750  24     LRR 24. 
DOMAIN   883   1158  276     Protein kinase. 
REPEAT   1175   1195  21     LRR 25. 
NP_BIND   889    897  9     ATP (By similarity). 
MOTIF   62     69  8     Cys pair 1. 
MOTIF   763    770  8     Cys pair 2. 
ACT_SITE   1009   1009        Proton acceptor (By similarity). 
BINDING   911    911        ATP (By similarity). 
MOD_RES   838    838        Phosphoserine. 
MOD_RES   842    842        Phosphothreonine. 
MOD_RES   846    846        Phosphothreonine. 
MOD_RES   851    851        Phosphothreonine (Potential). 
MOD_RES   858    858        Phosphoserine. 
MOD_RES   872    872        Phosphothreonine. 
MOD_RES   880    880        Phosphothreonine. 
MOD_RES   887    887        Phosphoserine (Potential). 
MOD_RES   891    891        Phosphoserine (Potential). 
MOD_RES   981    981        Phosphoserine (Potential). 
MOD_RES   982    982        Phosphothreonine. 
MOD_RES   1035   1035        Phosphoserine (Potential). 
MOD_RES   1039   1039        Phosphothreonine (Potential). 
MOD_RES   1042   1042        Phosphoserine (Potential). 
MOD_RES   1044   1044        Phosphoserine (Potential). 
MOD_RES   1045   1045        Phosphothreonine (Potential). 
MOD_RES   1049   1049        Phosphothreonine (Potential). 
MOD_RES   1060   1060        Phosphoserine (Potential). 
MOD_RES   1166   1166        Phosphoserine (Potential). 
MOD_RES   1168   1168        Phosphoserine. 
MOD_RES   1169   1169        Phosphothreonine (Potential). 
MOD_RES   1172   1172        Phosphoserine (Potential). 
MOD_RES   1179   1179        Phosphoserine (Potential). 
MOD_RES   1180   1180        Phosphothreonine (Potential). 
MOD_RES   1187   1187        Phosphoserine (Potential). 
CARBOHYD   112    112        N-linked (GlcNAc...) (Potential). 
CARBOHYD   154    154        N-linked (GlcNAc...) (Potential). 
CARBOHYD   233    233        N-linked (GlcNAc...) (Potential).