ID BRI1_SOLPE Reviewed; 1207 AA.
AC Q8L899;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Systemin receptor SR160;
DE EC=2.7.11.1;
DE AltName: Full=Brassinosteroid LRR receptor kinase;
DE Flags: Precursor;
OS Solanum peruvianum (Peruvian tomato) (Lycopersicon peruvianum).
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=4082;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 301-311; 432-440; 548-554
RP AND 862-874, GLYCOSYLATION, AND 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 Involved in the perception of systemin, a peptide hormone responsible
CC for the systemic activation of defense genes in leaves of wounded
CC plants. May also regulate, in response to brassinosteroid binding, a
CC signaling cascade involved in plant development (By similarity).
CC {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 21st LRR is
CC essential for the binding of brassinosteroids. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:12060717}.
CC -!- MISCELLANEOUS: SR160 is almost identical to BRI1, a brassinosteroid
CC receptor identified in Lycopersicon esculentum. Competition experiments
CC indicate that brassinosteroid and systemin are probably perceived by
CC different 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; AY112661; AAM48285.1; -; mRNA.
DR AlphaFoldDB; Q8L899; -.
DR SMR; Q8L899; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.30.1490.310; -; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF18; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF20141; Island; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 2.
DR PROSITE; PS51450; LRR; 20.
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; Direct protein sequencing; Glycoprotein;
KW Kinase; Leucine-rich repeat; Lipid-binding; Membrane; Nucleotide-binding;
KW Plant defense; Receptor; 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="Systemin receptor SR160"
FT /id="PRO_0000024307"
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..375
FT /note="LRR 11"
FT REPEAT 378..401
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"
SQ SEQUENCE 1207 AA; 131964 MW; 1422D1DFDA458073 CRC64;
MKAHKTVFNQ HPLSLNKLFF VLLLIFFLPP ASPAASVNGL YKDSQQLLSF KAALPPTPTL
LQNWLSSTDP CSFTGVSCKN SRVSSIDLSN TFLSVDFSLV TSYLLPLSNL ESLVLKNANL
SGSLTSAAKS QCGVTLDSID LAENTISGPI SDISSFGVCS NLKSLNLSKN FLDPPGKEML
KGATFSLQVL DLSYNNISGF NLFPWVSSMG FVELEFFSIK GNKLAGSIPE LDFKNLSYLD
LSANNFSTVF PSFKDCSNLQ HLDLSSNKFY GDIGSSLSSC GKLSFLNLTN NQFVGLVPKL
PSESLQYLYL RGNDFQGVYP NQLADLCKTV VELDLSYNNF SGMVPESLGE CSSLELVDIS
NNNFSGKLPV DTLLKLSNIK TMVLSFNKFV GGLPDSFSNL PKLETLDMSS NNLTGIIPSG
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 CGYPLPLPCS
SGPKSDANQH QKSHRRQASL AGSVAMGLLF SLFCIFGLII VAIETKKRRR KKEAALEAYM
DGHSHSATAN SAWKFTSARE ALSINLAAFE KPLRKLTFAD LLEATNGFHN DSLVGSGGFG
DVYKAQLKDG SVVAIKKLIH VSGQGDREFT AEMETIGKIK HRNLVPLLGY CKVGEERLLV
YEYMKYGSLE DVLHDRKKTG IKLNWPARRK IAIGAARGLA FLHHNCIPHI IHRDMKSSNV
LLDENLEARV SDFGMARLMS AMDTHLSVST LAGTPGYVPP EYYQSFRCST KGDVYSYGVV
LLELLTGKQP TDSADFGDNN LVGWVKLHAK GKITDVFDRE LLKEDASIEI ELLQHLKVAC
ACLDDRHWKR PTMIQVMAMF KEIQAGSGMD STSTIGADDV NFSGVEGGIE MGINGSIKEG
NELSKHL
//
