BRL1_ORYSJ
ID BRL1_ORYSJ Reviewed; 1214 AA.
AC Q69JN6; Q0J2V9;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Brassinosteroid LRR receptor kinase BRL1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=BRI1-like receptor kinase 1 {ECO:0000303|PubMed:16407447};
DE Flags: Precursor;
GN Name=BRL1 {ECO:0000303|PubMed:16407447};
GN OrderedLocusNames=Os09g0293500 {ECO:0000312|EMBL:BAF24706.2},
GN LOC_Os09g12240 {ECO:0000305};
GN ORFNames=B1043F11.38 {ECO:0000312|EMBL:BAD34326.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16407447; DOI=10.1104/pp.105.072330;
RA Nakamura A., Fujioka S., Sunohara H., Kamiya N., Hong Z., Inukai Y.,
RA Miura K., Takatsuto S., Yoshida S., Ueguchi-Tanaka M., Hasegawa Y.,
RA Kitano H., Matsuoka M.;
RT "The role of OsBRI1 and its homologous genes, OsBRL1 and OsBRL3, in rice.";
RL Plant Physiol. 140:580-590(2006).
CC -!- FUNCTION: May be involved in brassenosteroid (BR) perception in roots.
CC {ECO:0000269|PubMed:16407447}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. Expressed at low levels
CC in shoots. {ECO:0000269|PubMed:16407447}.
CC -!- DOMAIN: Contains two pairs of conservatively spaced Cys (Cys pair 1 and
CC 2) possibly involved in forming some heterodimers.
CC {ECO:0000250|UniProtKB:O22476}.
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; AP006156; BAD34326.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF24706.2; -; Genomic_DNA.
DR EMBL; AP014965; BAT07298.1; -; Genomic_DNA.
DR RefSeq; XP_015612606.1; XM_015757120.1.
DR AlphaFoldDB; Q69JN6; -.
DR SMR; Q69JN6; -.
DR STRING; 4530.OS09T0293500-01; -.
DR PaxDb; Q69JN6; -.
DR PRIDE; Q69JN6; -.
DR EnsemblPlants; Os09t0293500-01; Os09t0293500-01; Os09g0293500.
DR GeneID; 4346640; -.
DR Gramene; Os09t0293500-01; Os09t0293500-01; Os09g0293500.
DR KEGG; osa:4346640; -.
DR eggNOG; ENOG502QQ5H; Eukaryota.
DR HOGENOM; CLU_000288_22_4_1; -.
DR InParanoid; Q69JN6; -.
DR OMA; WNHMSGA; -.
DR OrthoDB; 104425at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
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: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; IBA:GO_Central.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 2.
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; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 14.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Brassinosteroid signaling pathway; Cell membrane;
KW Glycoprotein; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1214
FT /note="Brassinosteroid LRR receptor kinase BRL1"
FT /evidence="ECO:0000255"
FT /id="PRO_5008971036"
FT TRANSMEM 826..846
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 106..130
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 132..155
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 157..177
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 178..202
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 204..226
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 227..250
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 252..276
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 277..302
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 304..327
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 328..353
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 355..375
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 377..400
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 401..425
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 427..451
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 452..476
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 478..500
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 525..549
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 551..572
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 573..597
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 599..621
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 650..673
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 689..712
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 713..736
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 737..761
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 763..786
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT DOMAIN 912..1189
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 69..76
FT /note="Cys pair 1"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOTIF 799..806
FT /note="Cys pair 2"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT ACT_SITE 1038
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 678
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 918..926
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 940
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 986..988
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 992..995
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 1038..1043
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 1056
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1214 AA; 128941 MW; 98C017FBD31C63B0 CRC64;
MAASPPFMAA AAFLTLVVVL FRAPAPAIAV GEEAAALLAF RRASVADDPD GALASWVLGA
GGANSTAPCS WDGVSCAPPP DGRVAAVDLS GMSLAGELRL DALLALPALQ RLNLRGNAFY
GNLSHAAPSP PCALVEVDIS SNALNGTLPP SFLAPCGVLR SVNLSRNGLA GGGFPFAPSL
RSLDLSRNRL ADAGLLNYSF AGCHGVGYLN LSANLFAGRL PELAACSAVT TLDVSWNHMS
GGLPPGLVAT APANLTYLNI AGNNFTGDVS GYDFGGCANL TVLDWSYNGL SSTRLPPGLI
NCRRLETLEM SGNKLLSGAL PTFLVGFSSL RRLALAGNEF TGAIPVELGQ LCGRIVELDL
SSNRLVGALP ASFAKCKSLE VLDLGGNQLA GDFVASVVST IASLRELRLS FNNITGVNPL
PVLAAGCPLL EVIDLGSNEL DGEIMPDLCS SLPSLRKLLL PNNYLNGTVP PSLGDCANLE
SIDLSFNLLV GKIPTEIIRL PKIVDLVMWA NGLSGEIPDV LCSNGTTLET LVISYNNFTG
SIPRSITKCV NLIWVSLSGN RLTGSVPGGF GKLQKLAILQ LNKNLLSGHV PAELGSCNNL
IWLDLNSNSF TGTIPPQLAG QAGLVPGGIV SGKQFAFLRN EAGNICPGAG VLFEFFGIRP
ERLAEFPAVH LCPSTRIYTG TTVYTFTNNG SMIFLDLSYN GLTGTIPGSL GNMMYLQVLN
LGHNELNGTI PDAFQNLKSI GALDLSNNQL SGGIPPGLGG LNFLADFDVS NNNLTGPIPS
SGQLTTFPPS RYDNNNGLCG IPLPPCGHNP PWGGRPRGSP DGKRKVIGAS ILVGVALSVL
ILLLLLVTLC KLRMNQKTEE VRTGYVESLP TSGTSSWKLS GVREPLSINV ATFEKPLRKL
TFAHLLEATN GFSAETLIGS GGFGEVYKAK LKDGSVVAIK KLIHFTGQGD REFTAEMETI
GKIKHRNLVP LLGYCKIGDE RLLVYEYMKH GSLDVVLHDK AKASVKLDWS ARKKIAIGSA
RGLAFLHHSC IPHIIHRDMK SSNVLLDNNL DARVSDFGMA RLMNALDTHL SVSTLAGTPG
YVPPEYYQSF RCTTKGDVYS YGVVLLELLS GKKPIDPTEF GDNNLVGWVK QMVKENRSSE
IFDPTLTDRK SGEAELYQYL KIACECLDDR PNRRPTMIQV MAMFKELQLD SDSDILDGFS
INSSTIDESG EKSM
