BSK8_ARATH
ID BSK8_ARATH Reviewed; 487 AA.
AC Q9FHD7; Q8GYJ8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein kinase BSK8 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 8 {ECO:0000303|PubMed:23496207};
GN Name=BSK8 {ECO:0000303|PubMed:23496207};
GN OrderedLocusNames=At5g41260 {ECO:0000312|Araport:AT5G41260};
GN ORFNames=K1O13.5 {ECO:0000312|EMBL:BAB11102.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 269-487.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=12912986; DOI=10.1074/jbc.m307321200;
RA Boisson B., Giglione C., Meinnel T.;
RT "Unexpected protein families including cell defense components feature in
RT the N-myristoylome of a higher eukaryote.";
RL J. Biol. Chem. 278:43418-43429(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP INTERACTION WITH FLS2, AND SUBCELLULAR LOCATION.
RX PubMed=21726371; DOI=10.1111/j.1364-3703.2010.00704.x;
RA Qi Y., Tsuda K., Glazebrook J., Katagiri F.;
RT "Physical association of pattern-triggered immunity (PTI) and effector-
RT triggered immunity (ETI) immune receptors in Arabidopsis.";
RL Mol. Plant Pathol. 12:702-708(2011).
RN [9]
RP FUNCTION, INTERACTION WITH ASK7/BIN2; BSK1; BSK5; BSK6 AND BSK11,
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-213.
RX PubMed=23496207; DOI=10.1111/tpj.12175;
RA Sreeramulu S., Mostizky Y., Sunitha S., Shani E., Nahum H., Salomon D.,
RA Hayun L.B., Gruetter C., Rauh D., Ori N., Sessa G.;
RT "BSKs are partially redundant positive regulators of brassinosteroid
RT signaling in Arabidopsis.";
RL Plant J. 74:905-919(2013).
RN [10]
RP FUNCTION, INTERACTION WITH BSL2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-20 AND SER-213, AND MUTAGENESIS OF SER-20 AND SER-213.
RX PubMed=24924143; DOI=10.1021/pr5003164;
RA Wu X., Sklodowski K., Encke B., Schulze W.X.;
RT "A kinase-phosphatase signaling module with BSK8 and BSL2 involved in
RT regulation of sucrose-phosphate synthase.";
RL J. Proteome Res. 13:3397-3409(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 40-328 IN COMPLEX WITH ATP
RP ANALOG.
RX PubMed=23911552; DOI=10.1016/j.jmb.2013.07.034;
RA Grutter C., Sreeramulu S., Sessa G., Rauh D.;
RT "Structural characterization of the RLCK family member BSK8: a pseudokinase
RT with an unprecedented architecture.";
RL J. Mol. Biol. 425:4455-4467(2013).
CC -!- FUNCTION: Probable serine/threonine kinase that acts as positive
CC regulator of brassinosteroid (BR) signaling downstream of the receptor
CC kinase BRI1. Functions redundantly with BSK3, BSK4, BSK6 and BSK7
CC (PubMed:23496207). Involved in the regulation of sucrose-phosphate
CC synthase 1 (SPS1) in the context of sucrose resuply after starvation.
CC Activates BSL2, a phosphatase that may dephosphorylate SPS1, leading to
CC the activation of SPS1 (PubMed:24924143). {ECO:0000269|PubMed:23496207,
CC ECO:0000269|PubMed:24924143}.
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 -!- SUBUNIT: Interacts with ASK7/BIN2, BSK1, BSK5, BSK6 and BSK11
CC (PubMed:23496207). Interacts with BSL2 (PubMed:24924143).
CC {ECO:0000269|PubMed:23496207, ECO:0000269|PubMed:24924143}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21726371};
CC Lipid-anchor {ECO:0000305|PubMed:12912986}.
CC -!- PTM: Phosphorylated by BRI1, ASK7/BIN2 and ASK9/BIL2.
CC {ECO:0000269|PubMed:23496207}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AB019225; BAB11102.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94658.1; -; Genomic_DNA.
DR EMBL; BT029016; ABI93925.1; -; mRNA.
DR EMBL; AK117571; BAC42231.1; -; mRNA.
DR RefSeq; NP_198942.1; NM_123491.4.
DR PDB; 4I92; X-ray; 1.60 A; A=40-328.
DR PDB; 4I93; X-ray; 1.50 A; A/B=40-328.
DR PDB; 4I94; X-ray; 1.80 A; A/B=40-328.
DR PDBsum; 4I92; -.
DR PDBsum; 4I93; -.
DR PDBsum; 4I94; -.
DR AlphaFoldDB; Q9FHD7; -.
DR SMR; Q9FHD7; -.
DR BioGRID; 19378; 11.
DR STRING; 3702.AT5G41260.1; -.
DR iPTMnet; Q9FHD7; -.
DR SwissPalm; Q9FHD7; -.
DR PaxDb; Q9FHD7; -.
DR PRIDE; Q9FHD7; -.
DR ProteomicsDB; 240290; -.
DR EnsemblPlants; AT5G41260.1; AT5G41260.1; AT5G41260.
DR GeneID; 834127; -.
DR Gramene; AT5G41260.1; AT5G41260.1; AT5G41260.
DR KEGG; ath:AT5G41260; -.
DR Araport; AT5G41260; -.
DR TAIR; locus:2155115; AT5G41260.
DR eggNOG; ENOG502QSE9; Eukaryota.
DR HOGENOM; CLU_000288_15_0_1; -.
DR InParanoid; Q9FHD7; -.
DR OMA; PAFCEFT; -.
DR OrthoDB; 478216at2759; -.
DR PhylomeDB; Q9FHD7; -.
DR PRO; PR:Q9FHD7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHD7; baseline and differential.
DR Genevisible; Q9FHD7; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; 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; IEA:UniProtKB-KW.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR045845; BSK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR45863; PTHR45863; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Brassinosteroid signaling pathway;
KW Cell membrane; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12912986"
FT CHAIN 2..487
FT /note="Serine/threonine-protein kinase BSK8"
FT /id="PRO_0000324845"
FT DOMAIN 59..325
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23911552,
FT ECO:0007744|PDB:4I94"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:23911552, ECO:0007744|PDB:4I94"
FT BINDING 133..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23911552,
FT ECO:0007744|PDB:4I94"
FT BINDING 185..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23911552,
FT ECO:0007744|PDB:4I94"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23911552,
FT ECO:0007744|PDB:4I94"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24924143,
FT ECO:0007744|PubMed:17586839"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24924143"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12912986"
FT MUTAGEN 20
FT /note="S->A: Phosphorylation null-mimic mutant."
FT /evidence="ECO:0000269|PubMed:24924143"
FT MUTAGEN 20
FT /note="S->D: Constitutive phosphorylation-mimic mutant."
FT /evidence="ECO:0000269|PubMed:24924143"
FT MUTAGEN 213
FT /note="S->A: Phosphorylation null-mimic mutant."
FT /evidence="ECO:0000269|PubMed:24924143"
FT MUTAGEN 213
FT /note="S->A: Slightly reduces BSK8 protein
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:23496207"
FT MUTAGEN 213
FT /note="S->D: Constitutive phosphorylation-mimic mutant."
FT /evidence="ECO:0000269|PubMed:24924143"
FT CONFLICT 286
FT /note="I -> V (in Ref. 4; BAC42231)"
FT /evidence="ECO:0000305"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:4I93"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4I93"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4I93"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4I93"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:4I93"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4I94"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:4I93"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4I93"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:4I93"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 154..173
FT /evidence="ECO:0007829|PDB:4I93"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:4I93"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:4I93"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:4I92"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 231..247
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:4I93"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:4I93"
SQ SEQUENCE 487 AA; 54625 MW; 7619F9C5B8ED5334 CRC64;
MGCEVSKLSA LCCVSESGRS NPDVTGLDEE GRGESNDLPQ FREFSIETIR NATSGFAAEN
IVSEHGERAP NVVYKGKLEN QRRIAVKRFN RKSWPDSRQF LEEAKAVGQL RNHRMANLLG
CCYEDEERLL IAEFMPNETL AKHLFHWESQ PMKWAMRLRV ALHIAQALEY CTSKGRALYH
DLNAYRVLFD DDANPRLSCF GLMKNSRDGK SYSTNLAFTP PEYLRTGRVT PESVIYSFGT
LLLDLLSGKH IPPSHALDLI RDRNIQMLMD SGLEGQFSSD DGTELIRLAS RCLQYEPRER
PNPKSLVSAM IPLQKDLEIA SHQLLGVPNS ATTTALSPLG EACLRSDLTA IHEIIEKLGY
KDDEGATTEL SFQMWTDQMQ DTLVFKKKGD SAFRHKDFAK AIECYSQFIE VGTMGSPTVH
ARQSLCYLMN DMPREALNNA MQAQVISPAW HIASYLQAVA LSALGQENEA HTALKDGAML
ESKRNPL
