BSK7_ARATH
ID BSK7_ARATH Reviewed; 487 AA.
AC F4I3M3; Q9SH35;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Serine/threonine-protein kinase BSK7 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 7 {ECO:0000303|PubMed:23496207};
GN Name=BSK7 {ECO:0000303|PubMed:23496207};
GN OrderedLocusNames=At1g63500 {ECO:0000312|Araport:AT1G63500};
GN ORFNames=F2K11.13 {ECO:0000312|EMBL:AEE34106.1};
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 FUNCTION.
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. Functions redundantly with BSK3, BSK5, BSK6 and BSK8.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19710.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC008047; AAF19710.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34106.1; -; Genomic_DNA.
DR RefSeq; NP_176539.4; NM_105029.7.
DR AlphaFoldDB; F4I3M3; -.
DR SMR; F4I3M3; -.
DR STRING; 3702.AT1G63500.1; -.
DR iPTMnet; F4I3M3; -.
DR SwissPalm; F4I3M3; -.
DR PaxDb; F4I3M3; -.
DR PRIDE; F4I3M3; -.
DR ProteomicsDB; 240438; -.
DR EnsemblPlants; AT1G63500.1; AT1G63500.1; AT1G63500.
DR GeneID; 842656; -.
DR Gramene; AT1G63500.1; AT1G63500.1; AT1G63500.
DR KEGG; ath:AT1G63500; -.
DR Araport; AT1G63500; -.
DR TAIR; locus:2031279; AT1G63500.
DR eggNOG; ENOG502QSE9; Eukaryota.
DR HOGENOM; CLU_000288_15_0_1; -.
DR InParanoid; F4I3M3; -.
DR OMA; RHKEFAN; -.
DR OrthoDB; 478216at2759; -.
DR PRO; PR:F4I3M3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I3M3; baseline and differential.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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 3: Inferred from homology;
KW ATP-binding; Brassinosteroid signaling pathway; Cell membrane; Kinase;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..487
FT /note="Serine/threonine-protein kinase BSK7"
FT /id="PRO_0000443237"
FT DOMAIN 59..325
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 87
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 487 AA; 54798 MW; 37AB95485446FFEF CRC64;
MGCEVSKLCA FCCVSDPEGS NHGVTGLDED RRGEGNDLPQ FREFSIETLR NATSGFATEN
IVSEHGEKAP NVVYKGKLDN QRRIAVKRFN RKAWPDSRQF LEEAKAVGQL RNYRMANLLG
CCYEGEERLL VAEFMPNETL AKHLFHWESQ PMKWAMRLRV ALHIAQALEY CTGKGRALYH
DLNAYRVLFD DDSNPRLSCF GLMKNSRDGK SYSTNLAFTP PEYLRTGRVT PESVMYSYGT
LLLDLLSGKH IPPSHALDLI RDRNIQMLID SCLEGQFSSD DGTELIRLAS RCLQYEPRER
PNPKSLVTAM IPLQKDLETP SHQLMGIPSS ASTTPLSPLG EACLRTDLTA IHEILEKLSY
KDDEGAATEL SFQMWTNQMQ DSLNFKKKGD VAFRHKEFAN AIDCYSQFIE GGTMVSPTVY
ARRSLCYLMN EMPQEALNDA MQAQVISPAW HIASYLQAVA LSALGQENEA HAALKDGSML
ESKRNRL
