BRL2_ARATH
ID BRL2_ARATH Reviewed; 1143 AA.
AC Q9ZPS9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein kinase BRI1-like 2;
DE EC=2.7.11.1;
DE AltName: Full=BRASSINOSTEROID INSENSITIVE 1-like protein 2;
DE AltName: Full=Protein VASCULAR HIGHWAY 1;
DE Flags: Precursor;
GN Name=BRL2; Synonyms=VH1; OrderedLocusNames=At2g01950; ORFNames=F14H20.2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12417696; DOI=10.1105/tpc.005884;
RA Clay N.K., Nelson T.;
RT "VH1, a provascular cell-specific receptor kinase that influences leaf cell
RT patterns in Arabidopsis.";
RL Plant Cell 14:2707-2722(2002).
RN [5]
RP SUBCELLULAR LOCATION, AND LACK OF STEROID-BINDING.
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 [6]
RP FUNCTION, INTERACTION WITH TTL3, AND TISSUE SPECIFICITY.
RX PubMed=19000166; DOI=10.1111/j.1365-313x.2008.03742.x;
RA Ceserani T., Trofka A., Gandotra N., Nelson T.;
RT "VH1/BRL2 receptor-like kinase interacts with vascular-specific adaptor
RT proteins VIT and VIK to influence leaf venation.";
RL Plant J. 57:1000-1014(2009).
CC -!- FUNCTION: Receptor with a serine/threonine-protein kinase activity,
CC which may transduce extracellular spatial and temporal signals into
CC downstream cell differentiation responses in provascular and procambial
CC cells. In contrast to BRI1, BRL1 and BRL3, it does not bind
CC brassinolide. {ECO:0000269|PubMed:12417696,
CC ECO:0000269|PubMed:19000166}.
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 -!- SUBUNIT: Interacts with TTL3. {ECO:0000269|PubMed:19000166}.
CC -!- INTERACTION:
CC Q9ZPS9; Q9SHI2: At1g17230; NbExp=4; IntAct=EBI-2292728, EBI-20651261;
CC Q9ZPS9; A0A178WLG7: At1g51790; NbExp=3; IntAct=EBI-2292728, EBI-20652336;
CC Q9ZPS9; O65440-2: BAM3; NbExp=2; IntAct=EBI-2292728, EBI-20653325;
CC Q9ZPS9; Q9LHP4: RGI1; NbExp=4; IntAct=EBI-2292728, EBI-20660903;
CC Q9ZPS9; Q9SIN1: TTL3; NbExp=2; IntAct=EBI-2292728, EBI-2292882;
CC Q9ZPS9; Q9XI87: VH1-interacting kinase; NbExp=2; IntAct=EBI-2292728, EBI-2292778;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15486337};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15486337}.
CC -!- TISSUE SPECIFICITY: Expressed in provascular and procambial sites
CC throughout plant development. Expressed throughout globe- to heart-
CC staged embryos. Then, it is restricted to procambial cells by the late
CC torpedo stage, and this pattern persists throughout the duration of
CC embryo development. After germination, it is expressed not only in
CC procambial cells throughout the plant but also in all lateral organ
CC primordia before the onset of vascularization.
CC {ECO:0000269|PubMed:12417696, ECO:0000269|PubMed:19000166}.
CC -!- DOMAIN: Contains two pairs of conservatively spaced Cys (Cys pair 1 and
CC 2) possibly involved in forming some heterodimers. {ECO:0000250}.
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; AC006532; AAD20088.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05526.1; -; Genomic_DNA.
DR EMBL; AY074313; AAL67010.1; -; mRNA.
DR PIR; B84431; B84431.
DR RefSeq; NP_178304.1; NM_126256.4.
DR AlphaFoldDB; Q9ZPS9; -.
DR SMR; Q9ZPS9; -.
DR BioGRID; 129; 91.
DR IntAct; Q9ZPS9; 91.
DR STRING; 3702.AT2G01950.1; -.
DR PaxDb; Q9ZPS9; -.
DR PRIDE; Q9ZPS9; -.
DR ProteomicsDB; 240704; -.
DR EnsemblPlants; AT2G01950.1; AT2G01950.1; AT2G01950.
DR GeneID; 814726; -.
DR Gramene; AT2G01950.1; AT2G01950.1; AT2G01950.
DR KEGG; ath:AT2G01950; -.
DR Araport; AT2G01950; -.
DR TAIR; locus:2041150; AT2G01950.
DR eggNOG; ENOG502QS1K; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9ZPS9; -.
DR OMA; CTGLEWV; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ZPS9; -.
DR PRO; PR:Q9ZPS9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPS9; baseline and differential.
DR Genevisible; Q9ZPS9; AT.
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:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0010233; P:phloem transport; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
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; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 17.
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 Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1143
FT /note="Serine/threonine-protein kinase BRI1-like 2"
FT /id="PRO_0000024309"
FT TOPO_DOM 32..756
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 757..777
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 778..1143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 79..100
FT /note="LRR 1"
FT REPEAT 104..126
FT /note="LRR 2"
FT REPEAT 128..150
FT /note="LRR 3"
FT REPEAT 153..175
FT /note="LRR 4"
FT REPEAT 178..200
FT /note="LRR 5"
FT REPEAT 205..228
FT /note="LRR 6"
FT REPEAT 229..251
FT /note="LRR 7"
FT REPEAT 253..275
FT /note="LRR 8"
FT REPEAT 278..299
FT /note="LRR 9"
FT REPEAT 302..323
FT /note="LRR 10"
FT REPEAT 327..349
FT /note="LRR 11"
FT REPEAT 351..372
FT /note="LRR 12"
FT REPEAT 376..398
FT /note="LRR 13"
FT REPEAT 400..422
FT /note="LRR 14"
FT REPEAT 424..446
FT /note="LRR 15"
FT REPEAT 448..470
FT /note="LRR 16"
FT REPEAT 472..494
FT /note="LRR 17"
FT REPEAT 496..518
FT /note="LRR 18"
FT REPEAT 520..542
FT /note="LRR 19"
FT REPEAT 612..634
FT /note="LRR 20"
FT REPEAT 636..658
FT /note="LRR 21"
FT REPEAT 660..682
FT /note="LRR 22"
FT REPEAT 684..706
FT /note="LRR 23"
FT DOMAIN 838..1129
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 68..75
FT /note="Cys pair 1"
FT MOTIF 720..727
FT /note="Cys pair 2"
FT ACT_SITE 966
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 844..852
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 866
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 835
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 911
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 1009
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
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 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1143 AA; 125676 MW; 7D1C88493F27A94E CRC64;
MTTSPIRVRI RTRIQISFIF LLTHLSQSSS SDQSSLKTDS LSLLSFKTMI QDDPNNILSN
WSPRKSPCQF SGVTCLGGRV TEINLSGSGL SGIVSFNAFT SLDSLSVLKL SENFFVLNST
SLLLLPLTLT HLELSSSGLI GTLPENFFSK YSNLISITLS YNNFTGKLPN DLFLSSKKLQ
TLDLSYNNIT GPISGLTIPL SSCVSMTYLD FSGNSISGYI SDSLINCTNL KSLNLSYNNF
DGQIPKSFGE LKLLQSLDLS HNRLTGWIPP EIGDTCRSLQ NLRLSYNNFT GVIPESLSSC
SWLQSLDLSN NNISGPFPNT ILRSFGSLQI LLLSNNLISG DFPTSISACK SLRIADFSSN
RFSGVIPPDL CPGAASLEEL RLPDNLVTGE IPPAISQCSE LRTIDLSLNY LNGTIPPEIG
NLQKLEQFIA WYNNIAGEIP PEIGKLQNLK DLILNNNQLT GEIPPEFFNC SNIEWVSFTS
NRLTGEVPKD FGILSRLAVL QLGNNNFTGE IPPELGKCTT LVWLDLNTNH LTGEIPPRLG
RQPGSKALSG LLSGNTMAFV RNVGNSCKGV GGLVEFSGIR PERLLQIPSL KSCDFTRMYS
GPILSLFTRY QTIEYLDLSY NQLRGKIPDE IGEMIALQVL ELSHNQLSGE IPFTIGQLKN
LGVFDASDNR LQGQIPESFS NLSFLVQIDL SNNELTGPIP QRGQLSTLPA TQYANNPGLC
GVPLPECKNG NNQLPAGTEE GKRAKHGTRA ASWANSIVLG VLISAASVCI LIVWAIAVRA
RRRDADDAKM LHSLQAVNSA TTWKIEKEKE PLSINVATFQ RQLRKLKFSQ LIEATNGFSA
ASMIGHGGFG EVFKATLKDG SSVAIKKLIR LSCQGDREFM AEMETLGKIK HRNLVPLLGY
CKIGEERLLV YEFMQYGSLE EVLHGPRTGE KRRILGWEER KKIAKGAAKG LCFLHHNCIP
HIIHRDMKSS NVLLDQDMEA RVSDFGMARL ISALDTHLSV STLAGTPGYV PPEYYQSFRC
TAKGDVYSIG VVMLEILSGK RPTDKEEFGD TNLVGWSKMK AREGKHMEVI DEDLLKEGSS
ESLNEKEGFE GGVIVKEMLR YLEIALRCVD DFPSKRPNML QVVASLRELR GSENNSHSHS
NSL
