SERK2_ARATH
ID SERK2_ARATH Reviewed; 628 AA.
AC Q9XIC7; Q94F63;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Somatic embryogenesis receptor kinase 2 {ECO:0000303|PubMed:11706164};
DE Short=AtSERK2 {ECO:0000303|PubMed:11706164};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Somatic embryogenesis receptor-like kinase 2 {ECO:0000303|PubMed:11706164};
DE Flags: Precursor;
GN Name=SERK2 {ECO:0000303|PubMed:11706164};
GN OrderedLocusNames=At1g34210 {ECO:0000312|Araport:AT1G34210};
GN ORFNames=F23M19.11 {ECO:0000312|EMBL:AAD39611.1};
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].
RX PubMed=11706164; DOI=10.1104/pp.010324;
RA Hecht V.F.G., Vielle-Calzada J.-P., Hartog M.V., Schmidt E.D.L.,
RA Boutilier K., Grossniklaus U., de Vries S.C.;
RT "The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1 gene is expressed
RT in developing ovules and embryos and enhances embryogenic competence in
RT culture.";
RL Plant Physiol. 127:803-816(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11523644; DOI=10.1007/s004250000471;
RA Baudino S., Hansen S., Brettschneider R., Hecht V.F.G., Dresselhaus T.,
RA Loerz H., Dumas C., Rogowsky P.M.;
RT "Molecular characterisation of two novel maize LRR receptor-like kinases,
RT which belong to the SERK gene family.";
RL Planta 213:1-10(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INTERACTION WITH SERK1, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16284305; DOI=10.1105/tpc.105.036814;
RA Albrecht C., Russinova E., Hecht V.F.G., Baaijens E., de Vries S.;
RT "The Arabidopsis thaliana SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASES1 and
RT 2 control male sporogenesis.";
RL Plant Cell 17:3337-3349(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=16284306; DOI=10.1105/tpc.105.036731;
RA Colcombet J., Boisson-Dernier A., Ros-Palau R., Vera C.E., Schroeder J.I.;
RT "Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASES1 and 2 are essential
RT for tapetum development and microspore maturation.";
RL Plant Cell 17:3350-3361(2005).
RN [9]
RP FUNCTION.
RX PubMed=18667726; DOI=10.1104/pp.108.123216;
RA Albrecht C., Russinova E., Kemmerling B., Kwaaitaal M., de Vries S.C.;
RT "Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve
RT brassinosteroid-dependent and -independent signaling pathways.";
RL Plant Physiol. 148:611-619(2008).
RN [10]
RP AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT THR-302; THR-462; THR-465;
RP THR-466; SER-604; THR-616 AND SER-625.
RX PubMed=19105183; DOI=10.1002/pmic.200701059;
RA Karlova R., Boeren S., van Dongen W., Kwaaitaal M., Aker J., Vervoort J.,
RA de Vries S.C.;
RT "Identification of in vitro phosphorylation sites in the Arabidopsis
RT thaliana somatic embryogenesis receptor-like kinases.";
RL Proteomics 9:368-379(2009).
RN [11]
RP INTERACTION WITH EFR AND FLS2.
RC STRAIN=cv. Columbia;
RX PubMed=21693696; DOI=10.1105/tpc.111.084301;
RA Roux M., Schwessinger B., Albrecht C., Chinchilla D., Jones A., Holton N.,
RA Malinovsky F.G., Tor M., de Vries S., Zipfel C.;
RT "The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and
RT BKK1/SERK4 are required for innate immunity to hemibiotrophic and
RT biotrophic pathogens.";
RL Plant Cell 23:2440-2455(2011).
RN [12]
RP INTERACTION WITH ERECTA; ERL1 AND TMM.
RX PubMed=26320950; DOI=10.1016/j.cub.2015.07.068;
RA Meng X., Chen X., Mang H., Liu C., Yu X., Gao X., Torii K.U., He P.,
RA Shan L.;
RT "Differential function of Arabidopsis SERK family receptor-like kinases in
RT stomatal patterning.";
RL Curr. Biol. 25:2361-2372(2015).
RN [13]
RP FUNCTION, AND INTERACTION WITH RGI3/RGFR1 AND RGI4/RGFR2/SKM2.
RC STRAIN=cv. Columbia;
RX PubMed=27229311; DOI=10.1038/cr.2016.62;
RA Song W., Liu L., Wang J., Wu Z., Zhang H., Tang J., Lin G., Wang Y.,
RA Wen X., Li W., Han Z., Guo H., Chai J.;
RT "Signature motif-guided identification of receptors for peptide hormones
RT essential for root meristem growth.";
RL Cell Res. 26:674-685(2016).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-216, FUNCTION, GLYCOSYLATION AT
RP ASN-153 AND ASN-187, DISULFIDE BONDS, AND INTERACTION WITH PSKR1.
RX PubMed=26308901; DOI=10.1038/nature14858;
RA Wang J., Li H., Han Z., Zhang H., Wang T., Lin G., Chang J., Yang W.,
RA Chai J.;
RT "Allosteric receptor activation by the plant peptide hormone
RT phytosulfokine.";
RL Nature 525:265-268(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 30-214 IN COMPLEX WITH CLE44 AND
RP TDR, FUNCTION, GLYCOSYLATION AT ASN-153 AND ASN-187, AND DISULFIDE BONDS.
RX PubMed=27449136; DOI=10.1016/j.molp.2016.07.004;
RA Zhang H., Lin X., Han Z., Wang J., Qu L.-J., Chai J.;
RT "SERK family receptor-like kinases function as co-receptors with PXY for
RT plant vascular development.";
RL Mol. Plant 9:1406-1414(2016).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 28-216, AND DISULFIDE BONDS.
RX PubMed=29735985; DOI=10.1038/s41477-018-0150-9;
RA Hohmann U., Nicolet J., Moretti A., Hothorn L.A., Hothorn M.;
RT "The SERK3 elongated allele defines a role for BIR ectodomains in
RT brassinosteroid signalling.";
RL Nat. Plants 4:345-351(2018).
CC -!- FUNCTION: Serine/threonine-kinase involved in brassinosteroid-dependent
CC and -independent signaling pathways. Acts redundantly with SERK1 as a
CC control point for sporophytic development controlling male gametophyte
CC production (PubMed:18667726). Serves as coreceptor to small peptide
CC (e.g. RGF1 and CLE44) signaling (Probable). Involved in the perception
CC of phytosulfokine and subsequent signal transduction (PubMed:26308901).
CC {ECO:0000269|PubMed:18667726, ECO:0000269|PubMed:26308901,
CC ECO:0000305|PubMed:27229311}.
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:0000255|PROSITE-ProRule:PRU00159};
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:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Homo- and heterodimer. Component of the SERK1 signaling
CC complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2,
CC SERK3/BAK1 and BRI1 (By similarity). Bind to BRI1 in a brassinolide-
CC dependent manner (By similarity). Heterodimer with PSKR1
CC (PubMed:26308901). Interacts with the EF-Tu receptor EFR and FLS2 in a
CC specific ligand-induced manner. Interacts with ERECTA in a EPF2-induced
CC manner. Interacts with ERL1 in a EPF1-induced manner. Interacts with
CC TMM (PubMed:26320950). In the presence of the signal peptide RGF1,
CC interacts with RGI3/RGFR1 and RGI4/RGFR2/SKM2 (PubMed:27229311). Binds
CC to the peptide CLE44 in the presence of TDR (PubMed:27449136).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q94AG2,
CC ECO:0000269|PubMed:16284305, ECO:0000269|PubMed:21693696,
CC ECO:0000269|PubMed:26308901, ECO:0000269|PubMed:26320950,
CC ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:27449136}.
CC -!- INTERACTION:
CC Q9XIC7; C0LGE4: At1g12460; NbExp=4; IntAct=EBI-6299033, EBI-17126713;
CC Q9XIC7; Q0WR59: At5g10020; NbExp=3; IntAct=EBI-6299033, EBI-16945916;
CC Q9XIC7; A0A178UFM8: AXX17_At5g50380; NbExp=2; IntAct=EBI-6299033, EBI-20653342;
CC Q9XIC7; C0LGN7: LRR-RLK; NbExp=3; IntAct=EBI-6299033, EBI-20651518;
CC Q9XIC7; Q9FRI1: LRR-RLK; NbExp=4; IntAct=EBI-6299033, EBI-17071528;
CC Q9XIC7; Q93ZS4: NIK3; NbExp=4; IntAct=EBI-6299033, EBI-17121474;
CC Q9XIC7; Q9ZVR7: PSKR1; NbExp=5; IntAct=EBI-6299033, EBI-16172949;
CC Q9XIC7; Q9LZV7: PXC2; NbExp=2; IntAct=EBI-6299033, EBI-1238200;
CC Q9XIC7; P43298: TMK1; NbExp=3; IntAct=EBI-6299033, EBI-2023970;
CC Q9XIC7; Q8LPB4: PSKR; Xeno; NbExp=4; IntAct=EBI-6299033, EBI-16172869;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16284305};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16284305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, tapetum, developing
CC microspores, all cells of the embryo sac, provascular strands and
CC developing vascular bundles. Low expression in adult vascular tissue.
CC {ECO:0000269|PubMed:16284305}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:19105183}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Serk1 and serk2 double
CC mutants are completely male sterile due to a failure in tapetum
CC specification. {ECO:0000269|PubMed:16284305,
CC ECO:0000269|PubMed:16284306}.
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; AF384969; AAK68073.1; -; mRNA.
DR EMBL; FJ708645; ACN59241.1; -; mRNA.
DR EMBL; AC007454; AAD39611.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31686.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57997.1; -; Genomic_DNA.
DR EMBL; AK229715; BAF01553.1; -; mRNA.
DR PIR; D86466; D86466.
DR RefSeq; NP_001320467.1; NM_001333091.1.
DR RefSeq; NP_174683.1; NM_103144.5.
DR PDB; 4Z61; X-ray; 2.75 A; C/D=1-216.
DR PDB; 5GQR; X-ray; 3.50 A; K=30-214.
DR PDB; 6G3W; X-ray; 2.20 A; A/C=28-216.
DR PDBsum; 4Z61; -.
DR PDBsum; 5GQR; -.
DR PDBsum; 6G3W; -.
DR AlphaFoldDB; Q9XIC7; -.
DR SMR; Q9XIC7; -.
DR BioGRID; 25552; 28.
DR DIP; DIP-61781N; -.
DR IntAct; Q9XIC7; 29.
DR STRING; 3702.AT1G34210.1; -.
DR iPTMnet; Q9XIC7; -.
DR PaxDb; Q9XIC7; -.
DR PRIDE; Q9XIC7; -.
DR ProteomicsDB; 234541; -.
DR EnsemblPlants; AT1G34210.1; AT1G34210.1; AT1G34210.
DR EnsemblPlants; AT1G34210.2; AT1G34210.2; AT1G34210.
DR GeneID; 840320; -.
DR Gramene; AT1G34210.1; AT1G34210.1; AT1G34210.
DR Gramene; AT1G34210.2; AT1G34210.2; AT1G34210.
DR KEGG; ath:AT1G34210; -.
DR Araport; AT1G34210; -.
DR TAIR; locus:2026097; AT1G34210.
DR eggNOG; ENOG502QQ7B; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q9XIC7; -.
DR OMA; SNMEGDA; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9XIC7; -.
DR PRO; PR:Q9XIC7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIC7; baseline and differential.
DR Genevisible; Q9XIC7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR GO; GO:0010152; P:pollen maturation; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR031048; SERK.
DR PANTHER; PTHR47988:SF34; PTHR47988:SF34; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Kinase; Leucine-rich repeat; Lipid-binding; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..628
FT /note="Somatic embryogenesis receptor kinase 2"
FT /id="PRO_0000380725"
FT TOPO_DOM 30..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..628
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 95..119
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 121..143
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 144..167
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 168..192
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 305..592
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 45..85
FT /note="PSKR1 binding"
FT /evidence="ECO:0000269|PubMed:26308901,
FT ECO:0007744|PDB:4Z61"
FT REGION 56..58
FT /note="CLE44 binding"
FT /evidence="ECO:0000269|PubMed:27449136,
FT ECO:0007744|PDB:5GQR"
FT REGION 62..81
FT /note="Leucine-rich repeat receptor-like protein kinase
FT binding"
FT /evidence="ECO:0000269|PubMed:27449136,
FT ECO:0000269|PubMed:29735985, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:6G3W"
FT REGION 100..105
FT /note="Leucine-rich repeat receptor-like protein kinase
FT binding"
FT /evidence="ECO:0000269|PubMed:27449136,
FT ECO:0000269|PubMed:29735985, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:6G3W"
FT REGION 126..129
FT /note="Leucine-rich repeat receptor-like protein kinase
FT binding"
FT /evidence="ECO:0000269|PubMed:27449136,
FT ECO:0000269|PubMed:29735985, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:6G3W"
FT REGION 148..150
FT /note="Leucine-rich repeat receptor-like protein kinase
FT binding"
FT /evidence="ECO:0000269|PubMed:27449136,
FT ECO:0000269|PubMed:29735985, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:6G3W"
FT REGION 174..197
FT /note="Leucine-rich repeat receptor-like protein kinase
FT binding"
FT /evidence="ECO:0000269|PubMed:29735985,
FT ECO:0007744|PDB:6G3W"
FT ACT_SITE 432
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 64..65
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT BINDING 311..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 462
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 479
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 562
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 616
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT CARBOHYD 107
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 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:26308901, ECO:0000269|PubMed:27449136,
FT ECO:0007744|PDB:4Z61, ECO:0007744|PDB:5GQR"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:26308901, ECO:0000269|PubMed:27449136,
FT ECO:0007744|PDB:4Z61, ECO:0007744|PDB:5GQR"
FT DISULFID 61..68
FT /evidence="ECO:0000269|PubMed:26308901,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:29735985,
FT ECO:0007744|PDB:4Z61, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:6G3W"
FT DISULFID 205..213
FT /evidence="ECO:0000269|PubMed:26308901,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:29735985,
FT ECO:0007744|PDB:4Z61, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:6G3W"
FT CONFLICT 47
FT /note="N -> Y (in Ref. 1, 2 and 3; AAK68073)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="M -> T (in Ref. 1, 2 and 3; AAK68073)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="S -> G (in Ref. 1, 2 and 3; AAK68073)"
FT /evidence="ECO:0000305"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:6G3W"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5GQR"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6G3W"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:6G3W"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:6G3W"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:6G3W"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:6G3W"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:6G3W"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:6G3W"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6G3W"
SQ SEQUENCE 628 AA; 69403 MW; 23F6C0DC3717C74F CRC64;
MGRKKFEAFG FVCLISLLLL FNSLWLASSN MEGDALHSLR ANLVDPNNVL QSWDPTLVNP
CTWFHVTCNN ENSVIRVDLG NADLSGQLVP QLGQLKNLQY LELYSNNITG PVPSDLGNLT
NLVSLDLYLN SFTGPIPDSL GKLFKLRFLR LNNNSLTGPI PMSLTNIMTL QVLDLSNNRL
SGSVPDNGSF SLFTPISFAN NLDLCGPVTS RPCPGSPPFS PPPPFIPPPI VPTPGGYSAT
GAIAGGVAAG AALLFAAPAL AFAWWRRRKP QEFFFDVPAE EDPEVHLGQL KRFSLRELQV
ATDSFSNKNI LGRGGFGKVY KGRLADGTLV AVKRLKEERT PGGELQFQTE VEMISMAVHR
NLLRLRGFCM TPTERLLVYP YMANGSVASC LRERPPSQLP LAWSIRQQIA LGSARGLSYL
HDHCDPKIIH RDVKAANILL DEEFEAVVGD FGLARLMDYK DTHVTTAVRG TIGHIAPEYL
STGKSSEKTD VFGYGIMLLE LITGQRAFDL ARLANDDDVM LLDWVKGLLK EKKLEMLVDP
DLQSNYTEAE VEQLIQVALL CTQSSPMERP KMSEVVRMLE GDGLAEKWDE WQKVEVLRQE
VELSSHPTSD WILDSTDNLH AMELSGPR
