BSK5_ARATH
ID BSK5_ARATH Reviewed; 489 AA.
AC Q9FIL1;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Serine/threonine-protein kinase BSK5 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 5 {ECO:0000303|PubMed:18653891};
GN Name=BSK5 {ECO:0000303|PubMed:18653891};
GN OrderedLocusNames=At5g59010 {ECO:0000312|Araport:AT5G59010};
GN ORFNames=K19M22.7 {ECO:0000312|EMBL:BAB09644.1};
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [7]
RP FUNCTION.
RX PubMed=18653891; DOI=10.1126/science.1156973;
RA Tang W., Kim T.W., Oses-Prieto J.A., Sun Y., Deng Z., Zhu S., Wang R.,
RA Burlingame A.L., Wang Z.Y.;
RT "BSKs mediate signal transduction from the receptor kinase BRI1 in
RT Arabidopsis.";
RL Science 321:557-560(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22982312; DOI=10.1016/j.bbrc.2012.08.118;
RA Li Z.Y., Xu Z.S., He G.Y., Yang G.X., Chen M., Li L.C., Ma Y.Z.;
RT "A mutation in Arabidopsis BSK5 encoding a brassinosteroid-signaling kinase
RT protein affects responses to salinity and abscisic acid.";
RL Biochem. Biophys. Res. Commun. 426:522-527(2012).
RN [9]
RP INTERACTION WITH BRI1; BSK1; BSK6 AND BSK8, AND PHOSPHORYLATION.
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).
CC -!- FUNCTION: Probable serine/threonine kinase that acts as positive
CC regulator of brassinosteroid (BR) signaling downstream of the receptor
CC kinase BRI1 (PubMed:18653891). Involved in abiotic stress tolerance.
CC Required for salt stress and abscisic acid-mediated drought stress
CC tolerance (PubMed:22982312). {ECO:0000269|PubMed:18653891,
CC ECO:0000269|PubMed:22982312}.
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 BRI1, BSK1, BSK6 and BSK8.
CC {ECO:0000269|PubMed:23496207}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22982312};
CC Lipid-anchor {ECO:0000305|PubMed:12912986}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, stems, flowers
CC and siliques. {ECO:0000269|PubMed:22982312}.
CC -!- INDUCTION: Induced by salt stress, drought stress, cold stress,
CC brassinosteroid and abscisic acid (ABA). {ECO:0000269|PubMed:22982312}.
CC -!- PTM: Phosphorylated by BRI1, ASK7/BIN2 and ASK9/BIL2.
CC {ECO:0000269|PubMed:23496207}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings exhibit enhanced sensitivity to salt
CC stress and abscisic acid (ABA).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AB016885; BAB09644.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97129.1; -; Genomic_DNA.
DR EMBL; AY075600; AAL91617.1; -; mRNA.
DR EMBL; BT026380; ABH04487.1; -; mRNA.
DR RefSeq; NP_200709.2; NM_125291.5.
DR AlphaFoldDB; Q9FIL1; -.
DR SMR; Q9FIL1; -.
DR IntAct; Q9FIL1; 2.
DR STRING; 3702.AT5G59010.1; -.
DR iPTMnet; Q9FIL1; -.
DR SwissPalm; Q9FIL1; -.
DR PaxDb; Q9FIL1; -.
DR PRIDE; Q9FIL1; -.
DR ProteomicsDB; 222822; -.
DR EnsemblPlants; AT5G59010.1; AT5G59010.1; AT5G59010.
DR GeneID; 836018; -.
DR Gramene; AT5G59010.1; AT5G59010.1; AT5G59010.
DR KEGG; ath:AT5G59010; -.
DR Araport; AT5G59010; -.
DR TAIR; locus:2154538; AT5G59010.
DR eggNOG; ENOG502QS12; Eukaryota.
DR InParanoid; Q9FIL1; -.
DR OMA; INPEWPT; -.
DR OrthoDB; 560276at2759; -.
DR PhylomeDB; Q9FIL1; -.
DR PRO; PR:Q9FIL1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIL1; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; 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 GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
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 ATP-binding; Brassinosteroid signaling pathway; Cell membrane; Kinase;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12912986"
FT CHAIN 2..489
FT /note="Serine/threonine-protein kinase BSK5"
FT /id="PRO_0000443235"
FT DOMAIN 55..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 61..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q944A7"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12912986"
SQ SEQUENCE 489 AA; 54854 MW; 9FAAC543CA33EB25 CRC64;
MGPRCSKLSL CWWPTHLKST HNEASDLDNG TDDLPSFTEF SFDQLRAATC GFSTDSIVSE
HGVKAPNVVY KGRLEDDRWI AVKRFNRSAW PDTRQFLEEA KAVGQLRNER LANLIGFCCE
GDERLLVAEF MPFETLSKHL FHWDSQPMKW SMRLRVALYL AQALEYCSSK GRALYHDLNA
YRILFDQDGN PRLSCFGLMK NSRDGKSYST NLAFTPPEYL RTGRVIPESV VYSFGTLLLD
LLSGKHIPPS HALDLIRGKN FLMLMDSCLD GHFSNDDGTD LVRLASRCLQ YEARERPNVK
SLVSSLAPLQ KETDIPSHVL MGIPHGAASP KETTSLTPLG DACSRHDLTA IHEILEKVGY
KDDEGVANEL SFQVWTDQIQ ETLNSKKQGD AAFKGKDFVT AVECYTQFIE DGTMVSPTVF
ARRCLCYLMS NMPQEALGDA MQAQVVSPEW PTAFYLQAAA LFSLGMDKDA CETLKDGTSL
EAKKHNNRN
