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 10-MAY-2017, entry version 41.
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; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
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.,
RA Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y.,
RA Weng Q., Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D.,
RA Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J.,
RA Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H.,
RA Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y.,
RA Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W.,
RA Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W.,
RA Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y.,
RA 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.,
RA McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
RA Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
RA Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
RA Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using
RT next 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.,
RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA 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
RT development and stress.";
RL Mol. Plant 1:732-750(2008).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BRI1
RP AND BSL1, SUBCELLULAR LOCATION, INDUCTION BY 24-EPIBRASSINOLIDE,
RP MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-213 AND SER-215, AND
RP MUTAGENESIS OF 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.,
RA Wang Y., Xu X., Burlingame A.L., Gao Y., Sun Y., Tang W.;
RT "OsBRI1 activates BR signaling by preventing binding between the TPR
RT and kinase domains of OsBSK3 via phosphorylation.";
RL Plant Physiol. 170:1149-1161(2016).
CC -!- FUNCTION: Probable serine/threonine kinase that acts as posisitive
CC regulator of brassinosteroid (BR) signaling downstream of BRI1.
CC {ECO:0000269|PubMed:26697897}.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC {ECO:0000305}.
CC -!- SUBUNIT: Interacts with BRI1 and BSL1.
CC {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.
CC Phosphorylation at Ser-215 is required for its function in the
CC regulation of brassinosteroid signaling. Phosphorylation by BRI1
CC disrupts the interaction between its TPR and kinase domains,
CC thereby increasing the 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 SMR; B9FDE0; -.
DR STRING; 39947.LOC_Os04g58750.1; -.
DR PaxDb; B9FDE0; -.
DR EnsemblPlants; OS04T0684200-01; OS04T0684200-01; OS04G0684200.
DR Gramene; OS04T0684200-01; OS04T0684200-01; OS04G0684200.
DR eggNOG; ENOG410IGD2; Eukaryota.
DR eggNOG; ENOG410XQTV; LUCA.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011990; TPR-like_helical_dom.
DR Pfam; PF07714; Pkinase_Tyr; 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; Complete proteome; Kinase; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; TPR repeat;
KW Transferase.
FT INIT_MET 1 1 Removed. {ECO:0000305|PubMed:26697897}.
FT CHAIN 2 494 Probable serine/threonine-protein kinase
FT BSK3.
FT /FTId=PRO_0000439010.
FT DOMAIN 61 316 Protein kinase. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT REPEAT 423 456 TPR. {ECO:0000255|PROSITE-
FT ProRule:PRU00339}.
FT NP_BIND 67 75 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT COMPBIAS 11 14 Cys-rich. {ECO:0000255|PROSITE-
FT ProRule:PRU00005}.
FT ACT_SITE 183 183 Proton acceptor. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT BINDING 89 89 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT MOD_RES 213 213 Phosphoserine.
FT {ECO:0000269|PubMed:26697897}.
FT MOD_RES 215 215 Phosphoserine.
FT {ECO:0000269|PubMed:26697897}.
FT LIPID 2 2 N-myristoyl glycine.
FT {ECO:0000305|PubMed:26697897}.
FT MUTAGEN 2 3 GG->AA: Loss of plasma membrane
FT localization.
FT {ECO:0000269|PubMed:26697897}.
FT MUTAGEN 213 213 S->A: No effect on its function in the
FT regulation of brassinosteroid signaling.
FT {ECO:0000269|PubMed:26697897}.
FT MUTAGEN 213 213 S->E: No effect on its function in the
FT regulation of brassinosteroid signaling.
FT MUTAGEN 215 215 S->A: Loss of its function in the
FT regulation of brassinosteroid signaling.
FT {ECO:0000269|PubMed:26697897}.
FT MUTAGEN 215 215 S->E: Constitutively active in its
FT function in the regulation of
FT brassinosteroid signaling; increases
FT binding affinity for BSL1.
FT {ECO:0000269|PubMed:26697897}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 74 312 ipfam:Pkinase_Tyr [T]
FT MYHIT 61 316 iprf:PROTEIN_KINASE_DOM [T]
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
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