BSK3_ORYSJ
ID BSK3_ORYSJ Reviewed; 494 AA.
AC B9FDE0; A0A0N7KJY5; Q0J8W5; Q7XPV0;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Probable serine/threonine-protein kinase BSK3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 3 {ECO:0000305};
DE Short=OsBSK3 {ECO:0000303|PubMed:26697897};
DE AltName: Full=Receptor-like cytoplasmic kinase 173 {ECO:0000303|PubMed:19825577};
DE Short=OsRLCK173 {ECO:0000303|PubMed:19825577};
GN Name=BSK3 {ECO:0000303|PubMed:26697897};
GN Synonyms=RLCK173 {ECO:0000303|PubMed:19825577};
GN OrderedLocusNames=Os04g0684200 {ECO:0000312|EMBL:BAS91713.1},
GN LOC_Os04g58750 {ECO:0000305};
GN ORFNames=OsJ_16683 {ECO:0000312|EMBL:EEE61937.1},
GN OSJNBa0088H09.6 {ECO:0000312|EMBL:CAE03448.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825577; DOI=10.1093/mp/ssn047;
RA Vij S., Giri J., Dansana P.K., Kapoor S., Tyagi A.K.;
RT "The receptor-like cytoplasmic kinase (OsRLCK) gene family in rice:
RT organization, phylogenetic relationship, and expression during development
RT and stress.";
RL Mol. Plant 1:732-750(2008).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BRI1 AND
RP BSL1, SUBCELLULAR LOCATION, INDUCTION BY 24-EPIBRASSINOLIDE, MYRISTOYLATION
RP AT GLY-2, PHOSPHORYLATION AT SER-213 AND SER-215, AND MUTAGENESIS OF
RP 2-GLY-GLY-3; SER-213 AND SER-215.
RX PubMed=26697897; DOI=10.1104/pp.15.01668;
RA Zhang B., Wang X., Zhao Z., Wang R., Huang X., Zhu Y., Yuan L., Wang Y.,
RA Xu X., Burlingame A.L., Gao Y., Sun Y., Tang W.;
RT "OsBRI1 activates BR signaling by preventing binding between the TPR and
RT kinase domains of OsBSK3 via phosphorylation.";
RL Plant Physiol. 170:1149-1161(2016).
CC -!- FUNCTION: Probable serine/threonine kinase that acts as positive
CC regulator of brassinosteroid (BR) signaling downstream of BRI1.
CC {ECO:0000269|PubMed:26697897}.
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 and BSL1. {ECO:0000269|PubMed:26697897}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26697897};
CC Lipid-anchor {ECO:0000305|PubMed:26697897}. Note=Plasma membrane
CC localization is required for its function in the regulation of
CC brassinosteroid signaling. {ECO:0000269|PubMed:26697897}.
CC -!- INDUCTION: Induced by 24-epibrassinolide in roots and leaves.
CC {ECO:0000269|PubMed:26697897}.
CC -!- PTM: Phosphorylated at Ser-213 and Ser-215 by BRI1. Phosphorylation at
CC Ser-215 is required for its function in the regulation of
CC brassinosteroid signaling. Phosphorylation by BRI1 disrupts the
CC interaction between its TPR and kinase domains, thereby increasing the
CC binding between its kinase domain and BSL1.
CC {ECO:0000269|PubMed:26697897}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF16222.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS91713.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAE03448.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL606651; CAE03448.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF16222.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS91713.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000141; EEE61937.1; -; Genomic_DNA.
DR AlphaFoldDB; B9FDE0; -.
DR SMR; B9FDE0; -.
DR STRING; 4530.OS04T0684200-01; -.
DR iPTMnet; B9FDE0; -.
DR PRIDE; B9FDE0; -.
DR eggNOG; ENOG502QSE9; Eukaryota.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:1900459; P:positive regulation of 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; Cell membrane; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; TPR repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:26697897"
FT CHAIN 2..494
FT /note="Probable serine/threonine-protein kinase BSK3"
FT /id="PRO_0000439010"
FT DOMAIN 61..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 423..456
FT /note="TPR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 67..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26697897"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26697897"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:26697897"
FT MUTAGEN 2..3
FT /note="GG->AA: Loss of plasma membrane localization."
FT /evidence="ECO:0000269|PubMed:26697897"
FT MUTAGEN 213
FT /note="S->A: No effect on its function in the regulation of
FT brassinosteroid signaling."
FT /evidence="ECO:0000269|PubMed:26697897"
FT MUTAGEN 213
FT /note="S->E: No effect on its function in the regulation of
FT brassinosteroid signaling."
FT MUTAGEN 215
FT /note="S->A: Loss of its function in the regulation of
FT brassinosteroid signaling."
FT /evidence="ECO:0000269|PubMed:26697897"
FT MUTAGEN 215
FT /note="S->E: Constitutively active in its function in the
FT regulation of brassinosteroid signaling; increases binding
FT affinity for BSL1."
FT /evidence="ECO:0000269|PubMed:26697897"
SQ SEQUENCE 494 AA; 55412 MW; 29060296A5DA83EF CRC64;
MGGRVSKAVA CCCCRSQHHG VVVESSEKTA EEDHGESYEL PAFQEFSFEQ LRLATSGFAV
ENIVSEHGEK APNVVYKGKL DAQRRIAVKR FNRSAWPDPR QFLEEAKSVG QLRSKRLANL
LGCCCEGDER LLVAEYMPND TLAKHLFHWE AQAMKWPMRL RVVLYLAEAL EYCTSKGRAL
YHDLNAYRVL FDDDCNPRLS CFGLMKNSRD GKSYSTNLAF TPPEYMRTGR ITPESVIYSF
GTLLLDVLSG KHIPPSHALD LIRDRNFNML TDSCLEGQFS NEEGTELVRL ASRCLHYEPR
ERPNVRSLVQ ALAPLQKDLE TPSYELMDIP RGGATSVQSL LLSPLAEACS RKDLTAIHEI
LEKTGYKDDE GTANELSFQM WTNQMQDTLN SKKKGDNAFR QKDFSSAIDC YSQFIEVGTM
VSPTIYARRC LSYLMNDKAE QALSDAMQAL VISPTWPTAF YLQAAALLSL GMENEAQEAI
KDGCAHETSS SSGH
