BRI1_ARATH » Protein BRASSINOSTEROID INSENSITIVE 1

BRI1_ARATH » Protein BRASSINOSTEROID INSENSITIVE 1
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
BRI1_ARATH » Protein BRASSINOSTEROID INSENSITIVE 1 » AtBRI1; Brassinosteroid LRR receptor kinase;
Hydrophobic Thickness 30.4 ± 3.2 Å
Tilt Angle 3 ± 1°
ΔGtransfer -38.6 kcal/mol
ΔGfold -16.4 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING
Topology Out
TM Segments 789-817 (789-822)
Pathways

Plant hormone signal transduction (KEGG)

PDB 3rgx (23-784), 3rgz (23-784), 3riz (29-788), 3rj0 (29-788), 4lsa (29-788), 4oa6 (865-1160), 4oa9 (865-1160), 4oab (865-1160), 4oac (865-1160), 4oa2 (865-1196), 4m7e (A/B=24-784), 4lsx (A/B=29-788), 4oh4 (A/B=863-1172), 4q5j (A/B=863-1180)
OPM none
Complexes

BAK1:BRI1_ARATH

SERK1:BRI1_ARATH

Interactions

BAK1, Complex: BAK1:BRI1, PubMed

P2C70, Complex: P2C70:BRI1, PubMed

SERK1, Complex: SERK1:BRI1, PubMed

SERK4, Complex: BRI1:SERK4, PubMed

VA727, Complex: VA727:BRI1

Domains

AA: 33-70, PDBID: 3RGX, Subunit A, Seq Identity:100%, Leucine rich repeat N-terminal domain

AA: 222-264, PDBID: 3RGX, Subunit A, Seq Identity:100%, Leucine Rich repeats (2 copies)

AA: 417-439, PDBID: 3RGX, Subunit A, Seq Identity:100%, Leucine Rich Repeat

AA: 488-548, PDBID: 3RGX, Subunit A, Seq Identity:100%, Leucine rich repeat

AA: 693-738, PDBID: 3RGX, Subunit A, Seq Identity:100%, Leucine rich repeat

AA: 883-1155, PDBID: 4OA2, Subunit A, Seq Identity:100%, Protein kinase domain

UniProt annotation for BRI1_ARATH » Protein BRASSINOSTEROID INSENSITIVE 1
FUNCTION: Receptor with a dual specificity kinase activity acting on both serine/threonine- and tyrosine-containing substrates. 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), Transthyretin-Like protein (TTL) and SERK1 on "Ser-299" and "Thr- 462" in vitro. May have a guanylyl cyclase activity.

CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.

CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

ENZYME REGULATION: Activated by Ser and Thr phosphorylation.

SUBUNIT: Monomer or homodimer in the plasma membrane. Heterodimer with BAK1 in the endosomes. Interacts with SERK1 and TTL in a kinase-dependent manner. Component of the SERK1 signaling complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1. Interacts with CDG1 (PubMed).

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.

DOMAIN: The JM domain (815-883) is a positive regulator of kinase activity and is required for Tyr phosphorylation.

DOMAIN: A guanylyl cyclase domain (1021-1134) having an in vitro activity is included in the C-terminal kinase domain.

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). Homodimerizes in the absence of ligand and binds brassinosteroid in the absence of its coreceptor BAK1.

MISCELLANEOUS: The bri1-9 mutation produces a fully active protein with a subtle conformational change that is recognized for reglucosylation by UGGT, resulting in its endoplasmic reticulum retention via Glc(1)Man(9)GlcNAc(2)-calreticulin/calnexin interaction.

UniProt features for BRI1_ARATH » Protein BRASSINOSTEROID INSENSITIVE 1
SIGNAL 1 23 Potential.
CHAIN 24 1196 Protein BRASSINOSTEROID INSENSITIVE 1.
REPEAT 100 122 LRR 1.
REPEAT 123 145 LRR 2.
REPEAT 149 170 LRR 3.
REPEAT 174 195 LRR 4.
REPEAT 201 222 LRR 5.
REPEAT 223 245 LRR 6.
REPEAT 246 268 LRR 7.
REPEAT 270 291 LRR 8.
REPEAT 292 314 LRR 9.
REPEAT 317 339 LRR 10.
REPEAT 341 363 LRR 11.
REPEAT 366 389 LRR 12.
REPEAT 391 411 LRR 13.
REPEAT 417 440 LRR 14.
REPEAT 441 463 LRR 15.
REPEAT 465 487 LRR 16.
REPEAT 489 512 LRR 17.
REPEAT 513 535 LRR 18.
REPEAT 537 560 LRR 19.
REPEAT 561 583 LRR 20.
REPEAT 655 677 LRR 21.
REPEAT 679 701 LRR 22.
REPEAT 703 725 LRR 23.
REPEAT 727 749 LRR 24.
DOMAIN 883 1158 Protein kinase.
REPEAT 1175 1195 LRR 25.
MOTIF 62 69 Cys pair 1.
MOTIF 763 770 Cys pair 2.
ACT_SITE 1009 1009 Proton acceptor (By similarity).
Amino Acid Sequence for BRI1_ARATH » Protein BRASSINOSTEROID INSENSITIVE 1
MKTFSSFFLS VTTLFFFSFF SLSFQASPSQ SLYREIHQLI SFKDVLPDKN LLPDWSSNKN PCTFDGVTCR DDKVTSIDLS SKPLNVGFSA VSSSLLSLTG LESLFLSNSH INGSVSGFKC SASLTSLDLS RNSLSGPVTT LTSLGSCSGL KFLNVSSNTL DFPGKVSGGL KLNSLEVLDL SANSISGANV VGWVLSDGCG ELKHLAISGN KISGDVDVSR CVNLEFLDVS SNNFSTGIPF LGDCSALQHL DISGNKLSGD FSRAISTCTE LKLLNISSNQ FVGPIPPLPL KSLQYLSLAE NKFTGEIPDF LSGACDTLTG LDLSGNHFYG AVPPFFGSCS LLESLALSSN NFSGELPMDT LLKMRGLKVL DLSFNEFSGE LPESLTNLSA SLLTLDLSSN NFSGPILPNL CQNPKNTLQE LYLQNNGFTG KIPPTLSNCS ELVSLHLSFN YLSGTIPSSL GSLSKLRDLK LWLNMLEGEI PQELMYVKTL ETLILDFNDL TGEIPSGLSN CTNLNWISLS NNRLTGEIPK WIGRLENLAI LKLSNNSFSG NIPAELGDCR SLIWLDLNTN LFNGTIPAAM FKQSGKIAAN FIAGKRYVYI KNDGMKKECH GAGNLLEFQG IRSEQLNRLS TRNPCNITSR VYGGHTSPTF DNNGSMMFLD MSYNMLSGYI PKEIGSMPYL FILNLGHNDI SGSIPDEVGD LRGLNILDLS SNKLDGRIPQ AMSALTMLTE IDLSNNNLSG PIPEMGQFET FPPAKFLNNP GLCGYPLPRC DPSNADGYAH HQRSHGRRPA SLAGSVAMGL LFSFVCIFGL ILVGREMRKR RRKKEAELEM YAEGHGNSGD RTANNTNWKL TGVKEALSIN LAAFEKPLRK LTFADLLQAT NGFHNDSLIG SGGFGDVYKA ILKDGSAVAI KKLIHVSGQG DREFMAEMET IGKIKHRNLV PLLGYCKVGD ERLLVYEFMK YGSLEDVLHD PKKAGVKLNW STRRKIAIGS ARGLAFLHHN CSPHIIHRDM KSSNVLLDEN LEARVSDFGM ARLMSAMDTH LSVSTLAGTP GYVPPEYYQS FRCSTKGDVY SYGVVLLELL TGKRPTDSPD FGDNNLVGWV KQHAKLRISD VFDPELMKED PALEIELLQH LKVAVACLDD RAWRRPTMVQ VMAMFKEIQA GSGIDSQSTI RSIEDGGFST IEMVDMSIKE VPEGKL