BSK11_ARATH
ID BSK11_ARATH Reviewed; 507 AA.
AC F4I7Y4; Q9C6I1;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Serine/threonine-protein kinase BSK11 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 11 {ECO:0000303|PubMed:23496207};
GN Name=BSK11 {ECO:0000303|PubMed:23496207};
GN OrderedLocusNames=At1g50990 {ECO:0000312|Araport:AT1G50990};
GN ORFNames=F8A12.21 {ECO:0000312|EMBL:AAG50929.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 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 [4]
RP INTERACTION WITH BRI1; ASK7/BIN2; 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. {ECO:0000250|UniProtKB:Q944A7}.
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, ASK7/BIN2, BSK1, BSK6 and BSK8.
CC {ECO:0000269|PubMed:23496207}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12912986};
CC Lipid-anchor {ECO:0000305|PubMed:12912986}.
CC -!- PTM: Phosphorylated by BRI1, ASK7/BIN2 and ASK9/BIL2.
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=AAG50929.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079284; AAG50929.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32609.1; -; Genomic_DNA.
DR PIR; B96547; B96547.
DR RefSeq; NP_175512.2; NM_103979.3.
DR AlphaFoldDB; F4I7Y4; -.
DR SMR; F4I7Y4; -.
DR STRING; 3702.AT1G50990.1; -.
DR iPTMnet; F4I7Y4; -.
DR PaxDb; F4I7Y4; -.
DR PRIDE; F4I7Y4; -.
DR ProteomicsDB; 240505; -.
DR EnsemblPlants; AT1G50990.1; AT1G50990.1; AT1G50990.
DR GeneID; 841521; -.
DR Gramene; AT1G50990.1; AT1G50990.1; AT1G50990.
DR KEGG; ath:AT1G50990; -.
DR Araport; AT1G50990; -.
DR TAIR; locus:2036426; AT1G50990.
DR eggNOG; ENOG502QQT6; Eukaryota.
DR HOGENOM; CLU_000288_15_0_1; -.
DR InParanoid; F4I7Y4; -.
DR OMA; HKLNVPS; -.
DR OrthoDB; 478216at2759; -.
DR PRO; PR:F4I7Y4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I7Y4; baseline and differential.
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: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; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12912986"
FT CHAIN 2..507
FT /note="Serine/threonine-protein kinase BSK11"
FT /id="PRO_0000443238"
FT DOMAIN 75..332
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 16..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 81..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 106
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:0000269|PubMed:12912986"
SQ SEQUENCE 507 AA; 57611 MW; 6F5B8A57BFC4F81C CRC64;
MGCCQSSFLK PSSLHDKKIT SDDLSGRRGK GAKRGNRHRH ANINEGRGWH FSDVPDFSEF
SASVLRDATN NFNKNAVVSV CSDQEPNLVY QGCIRSDKDK RLIAVKKFSK TTWPDPKQFA
TEARAIGSLR HVRLVNLIGY CCEGDERLLV SEYMPNESLT KHLFHWEKQT MEWAMRLRVA
LYVAEALEYC RQSGLKLYHD LNTCRVLFDE NGSPRLSCFG WMKNSKDGKN FSTNLAYTPP
EYLRSGTLIP ESVVFSFGTF LLDLLSGKHI PPSHAVGTIQ KQNLNVLMDS HLEGNYPEED
AAMVFDLASK CLHNNPNERP EIGDIISVIT TLQQKLDVPS YTMLGISKLE KLEMEHPKSL
IYDACHQMDL AALHQILEAM EYKEDEVTCE LSFQQWAQQI KDVCNTRQQG DSAFRNKHFE
SAIDKYTQFI EIGIMISPTV YARRSMCYLF CDQPDAALRD AMQAQCVYSD WPTAFYLQAV
ALSKLNMVED SATMLKEALI LEDKRGS
