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   27-MAR-2024, entry version 164.
DE   RecName: Full=Serine/threonine-protein kinase BRI1-like 2;
DE            EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12417696, ECO:0000269|PubMed:19000166};
DE   AltName: Full=BRASSINOSTEROID INSENSITIVE 1-like protein 2 {ECO:0000303|PubMed:15486337};
DE   AltName: Full=Protein VASCULAR HIGHWAY 1 {ECO:0000303|PubMed:12417696};
DE   Flags: Precursor;
GN   Name=BRL2 {ECO:0000303|PubMed:15486337};
GN   Synonyms=VH1 {ECO:0000303|PubMed:12417696};
GN   OrderedLocusNames=At2g01950 {ECO:0000312|Araport:AT2G01950};
GN   ORFNames=F14H20.2 {ECO:0000312|EMBL:AAD20088.1};
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 [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, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
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, TISSUE SPECIFICITY, AND CATALYTIC
RP   ACTIVITY.
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         Evidence={ECO:0000269|PubMed:12417696, ECO:0000269|PubMed:19000166};
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:0000269|PubMed:12417696,
CC         ECO:0000269|PubMed:19000166};
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: VIK; 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.Q9ZPS9; -.
DR   GlyCosmos; Q9ZPS9; 12 sites, No reported glycans.
DR   PaxDb; 3702-AT2G01950-1; -.
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; AT2G01950; BRL2.
DR   eggNOG; ENOG502QS1K; Eukaryota.
DR   HOGENOM; CLU_000288_22_1_1; -.
DR   InParanoid; Q9ZPS9; -.
DR   OMA; DGFLACY; -.
DR   OrthoDB; 385706at2759; -.
DR   PhylomeDB; Q9ZPS9; -.
DR   PRO; PR:Q9ZPS9; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZPS9; baseline and differential.
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: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:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR   GO; GO:0010233; P:phloem transport; IDA:TAIR.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
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; PTHR48053; LEUCINE RICH REPEAT FAMILY PROTEIN, EXPRESSED; 1.
DR   PANTHER; PTHR48053:SF55; SERINE_THREONINE-PROTEIN KINASE BRI1-LIKE 2; 1.
DR   Pfam; PF20141; Island; 1.
DR   Pfam; PF00560; LRR_1; 6.
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; 5.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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.
DR   Genevisible; Q9ZPS9; AT.
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          77..101
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          102..125
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          126..150
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          151..175
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          177..200
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          203..227
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          228..250
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          251..275
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          277..299
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          300..324
FT                   /note="LRR 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          326..349
FT                   /note="LRR 11"
FT                   /evidence="ECO:0000255"
FT   REPEAT          351..373
FT                   /note="LRR 12"
FT                   /evidence="ECO:0000255"
FT   REPEAT          374..398
FT                   /note="LRR 13"
FT                   /evidence="ECO:0000255"
FT   REPEAT          399..422
FT                   /note="LRR 14"
FT                   /evidence="ECO:0000255"
FT   REPEAT          424..446
FT                   /note="LRR 15"
FT                   /evidence="ECO:0000255"
FT   REPEAT          447..470
FT                   /note="LRR 16"
FT                   /evidence="ECO:0000255"
FT   REPEAT          472..493
FT                   /note="LRR 17"
FT                   /evidence="ECO:0000255"
FT   REPEAT          494..518
FT                   /note="LRR 18"
FT                   /evidence="ECO:0000255"
FT   REPEAT          520..542
FT                   /note="LRR 19"
FT                   /evidence="ECO:0000255"
FT   REPEAT          570..594
FT                   /note="LRR 20"
FT                   /evidence="ECO:0000255"
FT   REPEAT          610..634
FT                   /note="LRR 21"
FT                   /evidence="ECO:0000255"
FT   REPEAT          635..660
FT                   /note="LRR 22"
FT                   /evidence="ECO:0000255"
FT   REPEAT          662..681
FT                   /note="LRR 23"
FT                   /evidence="ECO:0000255"
FT   REPEAT          682..707
FT                   /note="LRR 24"
FT                   /evidence="ECO:0000255"
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|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        118
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        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        412
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        681
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
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
//