BRI1_SOLLC
ID BRI1_SOLLC Reviewed; 1207 AA.
AC Q8GUQ5;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Brassinosteroid LRR receptor kinase;
DE EC=2.7.11.1;
DE AltName: Full=Altered brassinolide sensitivity 1;
DE AltName: Full=Systemin receptor SR160;
DE AltName: Full=tBRI1;
DE Flags: Precursor;
GN Name=CURL3;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT CU3-ABS/ABS1.
RX PubMed=12468734; DOI=10.1105/tpc.006379;
RA Montoya T., Nomura T., Farrar K., Kaneta T., Yokota T., Bishop G.J.;
RT "Cloning the tomato curl3 gene highlights the putative dual role of the
RT leucine-rich repeat receptor kinase tBRI1/SR160 in plant steroid hormone
RT and peptide hormone signaling.";
RL Plant Cell 14:3163-3176(2002).
RN [2]
RP SUBSTRATE-BINDING.
RX PubMed=12060717; DOI=10.1073/pnas.132266499;
RA Scheer J.M., Ryan C.A. Jr.;
RT "The systemin receptor SR160 from Lycopersicon peruvianum is a member of
RT the LRR receptor kinase family.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9585-9590(2002).
CC -!- FUNCTION: Receptor with a serine/threonine-protein kinase activity.
CC Regulates, in response to brassinosteroid binding, a signaling cascade
CC involved in plant development, including expression of light- and
CC stress-regulated genes, promotion of cell elongation, normal leaf and
CC chloroplast senescence, and flowering. May be involved in a feedback
CC regulation of brassinosteroid biosynthesis. May be also involved in the
CC perception of systemin, a peptide hormone responsible for the systemic
CC activation of defense genes in leaves of wounded plants (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- DOMAIN: A 68 amino acid island between the 20th and the 21th LRR is
CC essential for the binding of brassinosteroids. {ECO:0000250}.
CC -!- MISCELLANEOUS: BRI1 is almost identical to SR160, a systemin receptor
CC identified in Lycopersicon peruvianum. Competition experiments indicate
CC that brassinosteroid and systemin are probably perceived by different
CC regions of the receptor.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AY179606; AAN85409.1; -; Genomic_DNA.
DR RefSeq; NP_001296180.1; NM_001309251.1.
DR AlphaFoldDB; Q8GUQ5; -.
DR SMR; Q8GUQ5; -.
DR STRING; 4081.Solyc04g051510.1.1; -.
DR iPTMnet; Q8GUQ5; -.
DR PaxDb; Q8GUQ5; -.
DR PRIDE; Q8GUQ5; -.
DR EnsemblPlants; Solyc04g051510.1.1; Solyc04g051510.1.1.1; Solyc04g051510.1.
DR GeneID; 101261320; -.
DR Gramene; Solyc04g051510.1.1; Solyc04g051510.1.1.1; Solyc04g051510.1.
DR KEGG; sly:101261320; -.
DR eggNOG; ENOG502QRF2; Eukaryota.
DR HOGENOM; CLU_000288_22_4_1; -.
DR InParanoid; Q8GUQ5; -.
DR OMA; GWVKLHA; -.
DR OrthoDB; 151283at2759; -.
DR PhylomeDB; Q8GUQ5; -.
DR Proteomes; UP000004994; Chromosome 4.
DR GO; GO:0005768; C:endosome; IEA:EnsemblPlants.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:EnsemblPlants.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0048657; P:anther wall tapetum cell differentiation; IEA:EnsemblPlants.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IEA:EnsemblPlants.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProt.
DR GO; GO:0009729; P:detection of brassinosteroid stimulus; IEA:EnsemblPlants.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0048366; P:leaf development; IEA:EnsemblPlants.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:EnsemblPlants.
DR GO; GO:0010584; P:pollen exine formation; IEA:EnsemblPlants.
DR GO; GO:0009911; P:positive regulation of flower development; IEA:EnsemblPlants.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1900140; P:regulation of seedling development; IEA:EnsemblPlants.
DR GO; GO:0010224; P:response to UV-B; IEA:EnsemblPlants.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR045381; BRI1_island_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF20141; Island; 1.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Lipid-binding; Membrane; Nucleotide-binding; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Steroid-binding; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1207
FT /note="Brassinosteroid LRR receptor kinase"
FT /id="PRO_0000024306"
FT TRANSMEM 803..823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 109..131
FT /note="LRR 1"
FT REPEAT 135..157
FT /note="LRR 2"
FT REPEAT 161..181
FT /note="LRR 3"
FT REPEAT 186..207
FT /note="LRR 4"
FT REPEAT 213..234
FT /note="LRR 5"
FT REPEAT 235..257
FT /note="LRR 6"
FT REPEAT 258..280
FT /note="LRR 7"
FT REPEAT 282..304
FT /note="LRR 8"
FT REPEAT 305..325
FT /note="LRR 9"
FT REPEAT 329..350
FT /note="LRR 10"
FT REPEAT 353..374
FT /note="LRR 11"
FT REPEAT 378..400
FT /note="LRR 12"
FT REPEAT 402..423
FT /note="LRR 13"
FT REPEAT 428..450
FT /note="LRR 14"
FT REPEAT 452..474
FT /note="LRR 15"
FT REPEAT 476..499
FT /note="LRR 16"
FT REPEAT 500..523
FT /note="LRR 17"
FT REPEAT 524..547
FT /note="LRR 18"
FT REPEAT 548..570
FT /note="LRR 19"
FT REPEAT 572..594
FT /note="LRR 20"
FT REPEAT 664..686
FT /note="LRR 21"
FT REPEAT 688..711
FT /note="LRR 22"
FT REPEAT 712..735
FT /note="LRR 23"
FT REPEAT 736..758
FT /note="LRR 24"
FT DOMAIN 888..1163
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 71..78
FT /note="Cys pair 1"
FT MOTIF 771..779
FT /note="Cys pair 2"
FT ACT_SITE 1014
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 894..902
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 916
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 1012
FT /note="H->Y: In cu3-abs; brassinosteroid-insensitive semi-
FT dwarf mutant."
SQ SEQUENCE 1207 AA; 131957 MW; 6C370BA048060B7F CRC64;
MKAHKTVFNQ HPLSLNKLFF VLLLIFFLPP ASPAASVNGL YKDSQQLLSF KAALPPTPTL
LQNWLSSTGP CSFTGVSCKN SRVSSIDLSN TFLSVDFSLV TSYLLPLSNL ESLVLKNANL
SGSLTSAAKS QCGVTLDSID LAENTISGPI SDISSFGVCS NLKSLNLSKN FLDPPGKEML
KAATFSLQVL DLSYNNISGF NLFPWVSSMG FVELEFFSLK GNKLAGSIPE LDFKNLSYLD
LSANNFSTVF PSFKDCSNLQ HLDLSSNKFY GDIGSSLSSC GKLSFLNLTN NQFVGLVPKL
PSESLQYLYL RGNDFQGVYP NQLADLCKTV VELDLSYNNF SGMVPESLGE CSSLELVDIS
YNNFSGKLPV DTLSKLSNIK TMVLSFNKFV GGLPDSFSNL LKLETLDMSS NNLTGVIPSG
ICKDPMNNLK VLYLQNNLFK GPIPDSLSNC SQLVSLDLSF NYLTGSIPSS LGSLSKLKDL
ILWLNQLSGE IPQELMYLQA LENLILDFND LTGPIPASLS NCTKLNWISL SNNQLSGEIP
ASLGRLSNLA ILKLGNNSIS GNIPAELGNC QSLIWLDLNT NFLNGSIPPP LFKQSGNIAV
ALLTGKRYVY IKNDGSKECH GAGNLLEFGG IRQEQLDRIS TRHPCNFTRV YRGITQPTFN
HNGSMIFLDL SYNKLEGSIP KELGAMYYLS ILNLGHNDLS GMIPQQLGGL KNVAILDLSY
NRFNGTIPNS LTSLTLLGEI DLSNNNLSGM IPESAPFDTF PDYRFANNSL CGYPLPIPCS
SGPKSDANQH QKSHRRQASL AGSVAMGLLF SLFCIFGLII VAIETKKRRR KKEAALEAYM
DGHSHSATAN SAWKFTSARE ALSINLAAFE KPLRKLTFAD LLEATNGFHN DSLVGSGGFG
DVYKAQLKDG SVVAIKKLIH VSGQGDREFT AEMETIGKIK HRNLVPLLGY CKVGEERLLV
YEYMKYGSLE DVLHDRKKIG IKLNWPARRK IAIGAARGLA FLHHNCIPHI IHRDMKSSNV
LLDENLEARV SDFGMARLMS AMDTHLSVST LAGTPGYVPP EYYQSFRCST KGDVYSYGVV
LLELLTGKQP TDSADFGDNN LVGWVKLHAK GKITDVFDRE LLKEDASIEI ELLQHLKVAC
ACLDDRHWKR PTMIQVMAMF KEIQAGSGMD STSTIGADDV NFSGVEGGIE MGINGSIKEG
NELSKHL
