BSK12_ORYSJ
ID BSK12_ORYSJ Reviewed; 522 AA.
AC Q336V9; A0A0P0XWR2; Q9FWF0;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine/threonine-protein kinase BSK1-2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 1-2 {ECO:0000303|PubMed:28680425};
DE Short=OsBSK1-2 {ECO:0000303|PubMed:28680425};
GN Name=BSK1-2 {ECO:0000303|PubMed:28680425};
GN OrderedLocusNames=Os10g0542800 {ECO:0000312|EMBL:BAT11880.1},
GN LOC_Os10g39670 {ECO:0000312|EMBL:ABB47948.2};
GN ORFNames=OsJ_32329 {ECO:0000312|EMBL:EAZ16855.1},
GN OSJNBb0015I11.13 {ECO:0000312|EMBL:AAG13605.1};
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=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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 FUNCTION, AND INDUCTION.
RC STRAIN=cv. Kitaake;
RX PubMed=28680425; DOI=10.3389/fpls.2017.00908;
RA Wang J., Shi H., Zhou L., Peng C., Liu D., Zhou X., Wu W., Yin J., Qin H.,
RA Ma W., He M., Li W., Wang J., Li S., Chen X.;
RT "OsBSK1-2, an orthologous of AtBSK1, is involved in rice immunity.";
RL Front. Plant Sci. 8:908-908(2017).
CC -!- FUNCTION: Probable serine/threonine kinase that functions as a positive
CC regulator of plant immunity. May be involved in the regulation of
CC pattern-triggered immunity (PTI). Does not seem to be involved in
CC responses to brassinosteroid (BR) signaling.
CC {ECO:0000269|PubMed:28680425}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by treatment with the elicitors chitin or fagellin22
CC (flg22). {ECO:0000269|PubMed:28680425}.
CC -!- MISCELLANEOUS: Plants silencing BSK1-2 exhibit compromised responses to
CC chitin- or flg22-triggered immunity and resistance to Magnaporthe
CC oryzae. {ECO:0000269|PubMed:28680425}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAT11880.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC051633; AAG13605.1; -; Genomic_DNA.
DR EMBL; DP000086; ABB47948.2; -; Genomic_DNA.
DR EMBL; AP014966; BAT11880.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000147; EAZ16855.1; -; Genomic_DNA.
DR RefSeq; XP_015614505.1; XM_015759019.1.
DR AlphaFoldDB; Q336V9; -.
DR SMR; Q336V9; -.
DR STRING; 4530.OS10T0542800-01; -.
DR PRIDE; Q336V9; -.
DR EnsemblPlants; Os10t0542800-01; Os10t0542800-01; Os10g0542800.
DR GeneID; 9270011; -.
DR Gramene; Os10t0542800-01; Os10t0542800-01; Os10g0542800.
DR KEGG; osa:9270011; -.
DR eggNOG; ENOG502QQT6; Eukaryota.
DR InParanoid; Q336V9; -.
DR OrthoDB; 540417at2759; -.
DR PlantReactome; R-OSA-5632095; Brassinosteroid signaling.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..522
FT /note="Serine/threonine-protein kinase BSK1-2"
FT /id="PRO_0000443239"
FT DOMAIN 79..338
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 85..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 522 AA; 58177 MW; 320E0BE463DBBF59 CRC64;
MGCCGSSLRV GSHAPEKPPR RARPPPPPPQ PHHPRRPSFT LNAHQAAASS SAASAAPAPA
FAEFSLAELR EATGGFAAAN IVSESGEKAP NLVYRGRLQG AGGGGRAIAV KKFGKLAWPD
PKQFAEEARG VGKLRHRRMA NLIGYCCDGD ERLLVAEFMP NDTLAKHLFH WENKAIEWAM
RLRVAYNIAE ALEYCSNEER PLYHDLNAYR VLFDENGDPR LSCFGLMKNS RDGKSYSTNL
AYTPPEYLRN GRVTLESVVF SFGTILIDLL SGKRIPPTLA LDMIRSRSIQ AIMETNLEGK
YSIEEATTLV DLASKCLQYE PRDRPDIKKL VSILQPLQTK SEVPSYVMLG VPKPEEVPKA
PPAPQHPLSP MGEACSRMDL TAIHQILVST HYRDDEGTNE LSFQEWTQQM RDMLDARKRG
DFAFRDKNFK QAIDCYTQFV DVGTMVSPTV YARRSLCHLM CDQPDAALRD AMQAQCVYPD
WPTAFYMQAV ALSKLNMQSD SLDMLNEASQ LEEKRQKSIK GP
