BRL3_ARATH
ID BRL3_ARATH Reviewed; 1164 AA.
AC Q9LJF3; B9DHZ3; C0LGN0;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Receptor-like protein kinase BRI1-like 3;
DE EC=2.7.10.1;
DE EC=2.7.11.1;
DE AltName: Full=BRASSINOSTEROID INSENSITIVE 1-like protein 3;
DE Flags: Precursor;
GN Name=BRL3; OrderedLocusNames=At3g13380; ORFNames=MRP15.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-1164.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, STEROID-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=15486337; DOI=10.1242/dev.01403;
RA Cano-Delgado A., Yin Y., Yu C., Vafeados D., Mora-Garcia S., Cheng J.-C.,
RA Nam K.H., Li J., Chory J.;
RT "BRL1 and BRL3 are novel brassinosteroid receptors that function in
RT vascular differentiation in Arabidopsis.";
RL Development 131:5341-5351(2004).
RN [7]
RP AUTOPHOSPHORYLATION.
RX PubMed=19124768; DOI=10.1073/pnas.0810249106;
RA Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.;
RT "Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a
RT component of brassinosteroid signaling in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009).
CC -!- FUNCTION: Receptor with a dual specificity kinase activity acting on
CC both serine/threonine- and tyrosine-containing substrates. Binds
CC brassinolide. Regulates, in response to brassinosteroid binding, a
CC signaling cascade involved in plant development. May be involved in
CC cell growth and vascular differentiation.
CC {ECO:0000269|PubMed:15486337}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- INTERACTION:
CC Q9LJF3; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-20651413, EBI-16902452;
CC Q9LJF3; Q94F62: BAK1; NbExp=2; IntAct=EBI-20651413, EBI-617138;
CC Q9LJF3; O49545: BAM1; NbExp=2; IntAct=EBI-20651413, EBI-17069471;
CC Q9LJF3; Q9M2Z1: BAM2; NbExp=2; IntAct=EBI-20651413, EBI-16933791;
CC Q9LJF3; Q6XAT2: ERL2; NbExp=2; IntAct=EBI-20651413, EBI-16895926;
CC Q9LJF3; C0LGX3: HSL2; NbExp=2; IntAct=EBI-20651413, EBI-16904927;
CC Q9LJF3; Q9C8I6: IOS1; NbExp=2; IntAct=EBI-20651413, EBI-16924837;
CC Q9LJF3; Q8GX94: LRR-RLK; NbExp=2; IntAct=EBI-20651413, EBI-16955556;
CC Q9LJF3; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-20651413, EBI-20651739;
CC Q9LJF3; Q9LFS4: NIK1; NbExp=2; IntAct=EBI-20651413, EBI-16146189;
CC Q9LJF3; Q9FRS6: PXL1; NbExp=3; IntAct=EBI-20651413, EBI-16946268;
CC Q9LJF3; Q9ZRF9: RPK1; NbExp=2; IntAct=EBI-20651413, EBI-1238953;
CC Q9LJF3; Q8LPS5: SERK5; NbExp=2; IntAct=EBI-20651413, EBI-16887868;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15486337};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15486337}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in vascular tissues.
CC Expressed only during postembryonic development with a very discrete
CC pattern of expression, preferentially in the two protophloem cell files
CC at the elongation zone of the root. The expression in these two cell
CC files attenuates as the phloem cells differentiate in the upper root.
CC In cotyledons and leaves, it is expressed in phloem cells, starting at
CC the cotyledons and shoot apex, moving toward the basal part of the
CC leaves, where the expression is weak. Expressed in the secondary and
CC tertiary veins and in the upper part of the cotyledons and leaves.
CC Weakly or not expressed in the inflorescence stems. Has some
CC complementary expression with BRL1. {ECO:0000269|PubMed:15486337}.
CC -!- DOMAIN: Contains two pairs of conservatively spaced Cys (Cys pair 1 and
CC 2) possibly involved in forming some heterodimers. {ECO:0000250}.
CC -!- DOMAIN: A 70 amino acid island between the 18th and the 19th LRR is
CC essential for the binding of brassinosteroids. {ECO:0000250}.
CC -!- PTM: Autophosphorylated on Tyr and Thr residues.
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; FJ708720; ACN59315.1; -; mRNA.
DR EMBL; AP000603; BAB01743.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75340.1; -; Genomic_DNA.
DR EMBL; AY128280; AAM91089.1; -; mRNA.
DR EMBL; AK317701; BAH20360.1; -; mRNA.
DR RefSeq; NP_187946.1; NM_112183.3.
DR AlphaFoldDB; Q9LJF3; -.
DR SMR; Q9LJF3; -.
DR BioGRID; 5872; 43.
DR IntAct; Q9LJF3; 42.
DR STRING; 3702.AT3G13380.1; -.
DR iPTMnet; Q9LJF3; -.
DR PaxDb; Q9LJF3; -.
DR PRIDE; Q9LJF3; -.
DR ProteomicsDB; 240632; -.
DR EnsemblPlants; AT3G13380.1; AT3G13380.1; AT3G13380.
DR GeneID; 820538; -.
DR Gramene; AT3G13380.1; AT3G13380.1; AT3G13380.
DR KEGG; ath:AT3G13380; -.
DR Araport; AT3G13380; -.
DR TAIR; locus:2092810; AT3G13380.
DR eggNOG; ENOG502QQ5H; Eukaryota.
DR HOGENOM; CLU_000288_22_4_1; -.
DR InParanoid; Q9LJF3; -.
DR OMA; WNHMSGA; -.
DR OrthoDB; 104425at2759; -.
DR PhylomeDB; Q9LJF3; -.
DR PRO; PR:Q9LJF3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJF3; baseline and differential.
DR Genevisible; Q9LJF3; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
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; 1.
DR Pfam; PF13855; LRR_8; 3.
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; 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; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Steroid-binding; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1164
FT /note="Receptor-like protein kinase BRI1-like 3"
FT /id="PRO_0000024310"
FT TOPO_DOM 24..772
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..1164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 77..98
FT /note="LRR 1"
FT REPEAT 102..123
FT /note="LRR 2"
FT REPEAT 125..146
FT /note="LRR 3"
FT REPEAT 151..173
FT /note="LRR 4"
FT REPEAT 176..197
FT /note="LRR 5"
FT REPEAT 202..224
FT /note="LRR 6"
FT REPEAT 227..248
FT /note="LRR 7"
FT REPEAT 252..274
FT /note="LRR 8"
FT REPEAT 278..300
FT /note="LRR 9"
FT REPEAT 303..325
FT /note="LRR 10"
FT REPEAT 327..347
FT /note="LRR 11"
FT REPEAT 352..375
FT /note="LRR 12"
FT REPEAT 376..397
FT /note="LRR 13"
FT REPEAT 403..424
FT /note="LRR 14"
FT REPEAT 427..448
FT /note="LRR 15"
FT REPEAT 451..473
FT /note="LRR 16"
FT REPEAT 476..498
FT /note="LRR 17"
FT REPEAT 500..523
FT /note="LRR 18"
FT REPEAT 524..546
FT /note="LRR 19"
FT REPEAT 548..570
FT /note="LRR 20"
FT REPEAT 640..662
FT /note="LRR 21"
FT REPEAT 664..686
FT /note="LRR 22"
FT REPEAT 688..711
FT /note="LRR 23"
FT REPEAT 712..734
FT /note="LRR 24"
FT DOMAIN 858..1136
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 65..72
FT /note="Cys pair 1"
FT MOTIF 748..755
FT /note="Cys pair 2"
FT ACT_SITE 985
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 864..872
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 847
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 855
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 931
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 1028
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1011
FT /note="S -> R (in Ref. 5; BAH20360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1164 AA; 126661 MW; 79380581D400EEEC CRC64;
MKQQWQFLIL CLLVLFLTVD SRGRRLLSDD VNDTALLTAF KQTSIKSDPT NFLGNWRYGS
GRDPCTWRGV SCSSDGRVIG LDLRNGGLTG TLNLNNLTAL SNLRSLYLQG NNFSSGDSSS
SSGCSLEVLD LSSNSLTDSS IVDYVFSTCL NLVSVNFSHN KLAGKLKSSP SASNKRITTV
DLSNNRFSDE IPETFIADFP NSLKHLDLSG NNVTGDFSRL SFGLCENLTV FSLSQNSISG
DRFPVSLSNC KLLETLNLSR NSLIGKIPGD DYWGNFQNLR QLSLAHNLYS GEIPPELSLL
CRTLEVLDLS GNSLTGQLPQ SFTSCGSLQS LNLGNNKLSG DFLSTVVSKL SRITNLYLPF
NNISGSVPIS LTNCSNLRVL DLSSNEFTGE VPSGFCSLQS SSVLEKLLIA NNYLSGTVPV
ELGKCKSLKT IDLSFNALTG LIPKEIWTLP KLSDLVMWAN NLTGGIPESI CVDGGNLETL
ILNNNLLTGS LPESISKCTN MLWISLSSNL LTGEIPVGIG KLEKLAILQL GNNSLTGNIP
SELGNCKNLI WLDLNSNNLT GNLPGELASQ AGLVMPGSVS GKQFAFVRNE GGTDCRGAGG
LVEFEGIRAE RLEHFPMVHS CPKTRIYSGM TMYMFSSNGS MIYLDLSYNA VSGSIPLGYG
AMGYLQVLNL GHNLLTGTIP DSFGGLKAIG VLDLSHNDLQ GFLPGSLGGL SFLSDLDVSN
NNLTGPIPFG GQLTTFPLTR YANNSGLCGV PLPPCSSGSR PTRSHAHPKK QSIATGMSAG
IVFSFMCIVM LIMALYRARK VQKKEKQREK YIESLPTSGS SSWKLSSVHE PLSINVATFE
KPLRKLTFAH LLEATNGFSA DSMIGSGGFG DVYKAKLADG SVVAIKKLIQ VTGQGDREFM
AEMETIGKIK HRNLVPLLGY CKIGEERLLV YEYMKYGSLE TVLHEKTKKG GIFLDWSARK
KIAIGAARGL AFLHHSCIPH IIHRDMKSSN VLLDQDFVAR VSDFGMARLV SALDTHLSVS
TLAGTPGYVP PEYYQSFRCT AKGDVYSYGV ILLELLSGKK PIDPEEFGED NNLVGWAKQL
YREKRGAEIL DPELVTDKSG DVELLHYLKI ASQCLDDRPF KRPTMIQVMT MFKELVQVDT
ENDSLDEFLL KETPLVEESR DKEP
