BRL3_ORYSJ
ID BRL3_ORYSJ Reviewed; 1214 AA.
AC Q6ZCZ2; A3BS52;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Brassinosteroid LRR receptor kinase BRL3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=BRI1-like receptor kinase 3 {ECO:0000303|PubMed:16407447};
DE Flags: Precursor;
GN Name=BRL3 {ECO:0000305};
GN OrderedLocusNames=Os08g0342300 {ECO:0000312|EMBL:BAH94254.1},
GN LOC_Os08g25380 {ECO:0000305};
GN ORFNames=OJ1790_D02.27 {ECO:0000312|EMBL:BAD01717.1},
GN OsJ_26971 {ECO:0000312|EMBL:EAZ42391.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP004553; BAD01717.1; -; Genomic_DNA.
DR EMBL; AP008214; BAH94254.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT05005.1; -; Genomic_DNA.
DR EMBL; CM000145; EAZ42391.1; -; Genomic_DNA.
DR RefSeq; XP_015650921.1; XM_015795435.1.
DR AlphaFoldDB; Q6ZCZ2; -.
DR SMR; Q6ZCZ2; -.
DR STRING; 4530.OS08T0342300-00; -.
DR PaxDb; Q6ZCZ2; -.
DR PRIDE; Q6ZCZ2; -.
DR EnsemblPlants; Os08t0342300-01; Os08t0342300-01; Os08g0342300.
DR GeneID; 9272003; -.
DR Gramene; Os08t0342300-01; Os08t0342300-01; Os08g0342300.
DR KEGG; osa:9272003; -.
DR eggNOG; ENOG502QQ5H; Eukaryota.
DR HOGENOM; CLU_000288_22_4_1; -.
DR InParanoid; Q6ZCZ2; -.
DR OMA; MWANNLS; -.
DR OrthoDB; 104425at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
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; 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; 1.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
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 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 BRL3"
FT /evidence="ECO:0000255"
FT /id="PRO_5008971902"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 103..127
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 131..155
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 156..177
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 178..202
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 204..228
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 230..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 303..325
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 327..351
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 353..375
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 377..400
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 401..427
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 429..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 502..525
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 526..549
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 550..572
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 573..597
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 599..621
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 650..673
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 689..712
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 713..736
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 738..760
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 762..786
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT DOMAIN 913..1196
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 1039
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 919..927
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 941
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 987..989
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 993..996
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 1039..1044
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 1057
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT CARBOHYD 61
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 400
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 512
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 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 108
FT /note="R -> G (in Ref. 4; EAZ42391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1214 AA; 131004 MW; 2E1A21FDED543881 CRC64;
MAAVRVVAPA PSVLLLVAAA VVLLHLARAI AGAADEAAAL LAFKDASVAA DPGGALAGWA
NSTTPGSPCA WAGVSCAAGR VRALDLSGMS LSGRLRLDAL LALSALRRLD LRGNAFHGDL
SRHGSPRRAA PCALVEVDIS SNTFNGTLPR AFLASCGGLQ TLNLSRNSLT GGGYPFPPSL
RRLDMSRNQL SDAGLLNYSL TGCHGIQYLN LSANQFTGSL PGLAPCTEVS VLDLSWNLMS
GVLPPRFVAM APANLTYLSI AGNNFSMDIS DYEFGGCANL TLLDWSYNRL RSTGLPRSLV
DCRRLEALDM SGNKLLSGPI PTFLVELQAL RRLSLAGNRF TGEISDKLSI LCKTLVELDL
SSNQLIGSLP ASFGQCRFLQ VLDLGNNQLS GDFVETVITN ISSLRVLRLP FNNITGANPL
PALASRCPLL EVIDLGSNEF DGEIMPDLCS SLPSLRKLLL PNNYINGTVP SSLSNCVNLE
SIDLSFNLLV GQIPPEILFL LKLVDLVLWA NNLSGEIPDK FCFNSTALET LVISYNSFTG
NIPESITRCV NLIWLSLAGN NLTGSIPSGF GNLQNLAILQ LNKNSLSGKV PAELGSCSNL
IWLDLNSNEL TGTIPPQLAA QAGLITGAIV SGKQFAFLRN EAGNICPGAG VLFEFLDIRP
DRLANFPAVH LCSSTRIYTG TTVYTFRNNG SMIFLDLSYN SLTGTIPASF GNMTYLEVLN
LGHNELTGAI PDAFTGLKGI GALDLSHNHL TGVIPPGFGC LHFLADFDVS NNNLTGEIPT
SGQLITFPAS RYENNSGLCG IPLNPCVHNS GAGGLPQTSY GHRNFARQSV FLAVTLSVLI
LFSLLIIHYK LWKFHKNKTK EIQAGCSESL PGSSKSSWKL SGIGEPLSIN MAIFENPLRK
LTFSDLHQAT NGFCAETLIG SGGFGEVYKA KLKDGNIVAV KKLMHFTGQG DREFTAEMET
IGKIKHRNLV PLLGYCKIGD ERLLVYEYMK NGSLDFVLHD KGEANMDLNW ATRKKIAIGS
ARGLAFLHHS CVPHIIHRDM KSSNVLLDGN FDAYVSDFGM ARLMNALDSH LTVSMLSGTP
GYVPPEYCQD FRCTTKGDVY SYGVVLLELL TGKKPIDPTE FGDSNLVGWV KQMVEDRCSE
IYDPTLMATT SSELELYQYL KIACRCLDDQ PNRRPTMIQV MTMFKEFQVD SGSNFLDDFS
LNSTNMEESS EKSV
