BSK3_ARATH
ID BSK3_ARATH Reviewed; 489 AA.
AC Q8W4L3; O65280;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Serine/threonine-protein kinase BSK3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 3 {ECO:0000303|PubMed:18653891};
GN Name=BSK3 {ECO:0000303|PubMed:18653891};
GN OrderedLocusNames=At4g00710 {ECO:0000312|Araport:AT4G00710};
GN ORFNames=F6N23.9 {ECO:0000312|EMBL:AAL32573.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 [5]
RP FUNCTION, INTERACTION WITH BRI1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
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 [6]
RP FUNCTION, 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. Mediates signal transduction from BRI1 by functioning as
CC substrate of BRI1 (PubMed:18653891). Functions redundantly with BSK4,
CC BSK6, BSK7 and BSK8 (PubMed:23496207). {ECO:0000269|PubMed:18653891,
CC ECO:0000269|PubMed:23496207}.
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. {ECO:0000269|PubMed:18653891,
CC ECO:0000269|PubMed:23496207}.
CC -!- INTERACTION:
CC Q8W4L3; O22476: BRI1; NbExp=2; IntAct=EBI-1797930, EBI-1797828;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18653891};
CC Lipid-anchor {ECO:0000305|PubMed:12912986}.
CC -!- PTM: Phosphorylated by BRI1 upon brassinolide (BL) treatment
CC (PubMed:18653891). Phosphorylated by ASK7/BIN2 and ASK9/BIL2
CC (PubMed:23496207). {ECO:0000269|PubMed:18653891,
CC ECO:0000269|PubMed:23496207}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13615.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80880.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF058919; AAC13615.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80880.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81924.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67341.1; -; Genomic_DNA.
DR EMBL; AY062495; AAL32573.1; -; mRNA.
DR EMBL; AY093275; AAM13274.1; -; mRNA.
DR PIR; T01235; T01235.
DR RefSeq; NP_001329175.1; NM_001340265.1.
DR RefSeq; NP_191980.2; NM_116296.4.
DR AlphaFoldDB; Q8W4L3; -.
DR SMR; Q8W4L3; -.
DR IntAct; Q8W4L3; 2.
DR STRING; 3702.AT4G00710.1; -.
DR iPTMnet; Q8W4L3; -.
DR PaxDb; Q8W4L3; -.
DR PRIDE; Q8W4L3; -.
DR ProteomicsDB; 240508; -.
DR EnsemblPlants; AT4G00710.1; AT4G00710.1; AT4G00710.
DR EnsemblPlants; AT4G00710.2; AT4G00710.2; AT4G00710.
DR GeneID; 828025; -.
DR Gramene; AT4G00710.1; AT4G00710.1; AT4G00710.
DR Gramene; AT4G00710.2; AT4G00710.2; AT4G00710.
DR KEGG; ath:AT4G00710; -.
DR Araport; AT4G00710; -.
DR TAIR; locus:2127118; AT4G00710.
DR eggNOG; ENOG502QSE9; Eukaryota.
DR HOGENOM; CLU_000288_15_0_1; -.
DR InParanoid; Q8W4L3; -.
DR OMA; HVENGEN; -.
DR OrthoDB; 478216at2759; -.
DR PhylomeDB; Q8W4L3; -.
DR PRO; PR:Q8W4L3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W4L3; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12912986"
FT CHAIN 2..489
FT /note="Serine/threonine-protein kinase BSK3"
FT /id="PRO_0000443233"
FT DOMAIN 58..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 64..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 212
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; 54914 MW; 84C3183CD9FF4165 CRC64;
MGGQCSSLSC CRNTSHKTAV LEAPDVDNGE SSEITDVPNF REYTLEQLKA ATSGFAVEYI
VSEHGEKAPN VVYKGKLENQ KKIAVKRFTR MAWPDSRQFL EEARSVGQLR SERMANLLGC
CCEGDERLLV AEFMPNETLA KHLFHWETQP MKWTMRLRVV LYLAQALEYC TSKGRTLYHD
LNAYRVLFDE ECNPRLSTFG LMKNSRDGKS YSTNLAFTPP EYLRTGRITP ESVIYSFGTL
LLDLLSGKHI PPSHALDLIR DRNLQTLTDS CLDGQFSDSD GTELVRLASR CLQYEARERP
NTKSLVTALT PLQKETEVLS HVLMGLPHSG SVSPLSPLGE ACSRRDLTAM LEILEKLGYK
DDEGVTNELS FHMWTDQMQE SLNSKKKGDV AFRQKDFREA IECYTQFIDG GMISPTVCAR
RSLCYLMSDM PKEALDDAIQ AQVISPVWHV ASYLQSASLG ILGMEKESQI ALKEGSNLEA
KMNGVPRVK
