BSK4_ARATH
ID BSK4_ARATH Reviewed; 483 AA.
AC F4HU55; Q9LQ82;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Serine/threonine-protein kinase BSK4 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 4 {ECO:0000303|PubMed:23496207};
GN Name=BSK4 {ECO:0000303|PubMed:23496207};
GN OrderedLocusNames=At1g01740 {ECO:0000312|Araport:AT1G01740};
GN ORFNames=T1N6.15 {ECO:0000312|EMBL:AAF78407.1};
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 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, BSK6, BSK7 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:0000305|PubMed:12912986};
CC Lipid-anchor {ECO:0000305|PubMed:12912986}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78407.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009273; AAF78407.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27329.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27330.1; -; Genomic_DNA.
DR PIR; H86148; H86148.
DR RefSeq; NP_001184886.1; NM_001197957.2.
DR RefSeq; NP_171679.1; NM_100057.2.
DR AlphaFoldDB; F4HU55; -.
DR SMR; F4HU55; -.
DR STRING; 3702.AT1G01740.2; -.
DR iPTMnet; F4HU55; -.
DR PaxDb; F4HU55; -.
DR PRIDE; F4HU55; -.
DR ProteomicsDB; 240510; -.
DR EnsemblPlants; AT1G01740.1; AT1G01740.1; AT1G01740.
DR EnsemblPlants; AT1G01740.2; AT1G01740.2; AT1G01740.
DR GeneID; 839253; -.
DR Gramene; AT1G01740.1; AT1G01740.1; AT1G01740.
DR Gramene; AT1G01740.2; AT1G01740.2; AT1G01740.
DR KEGG; ath:AT1G01740; -.
DR Araport; AT1G01740; -.
DR TAIR; locus:2198160; AT1G01740.
DR eggNOG; ENOG502QSE9; Eukaryota.
DR HOGENOM; CLU_000288_15_0_1; -.
DR InParanoid; F4HU55; -.
DR OrthoDB; 478216at2759; -.
DR PRO; PR:F4HU55; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HU55; baseline and differential.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
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; 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; 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:0000269|PubMed:12912986"
FT CHAIN 2..483
FT /note="Serine/threonine-protein kinase BSK4"
FT /id="PRO_0000443234"
FT DOMAIN 56..322
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 62..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 84
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 483 AA; 54039 MW; A8D4CB2A5C1BB8C7 CRC64;
MGGQSSKIGT CCSHKTTALE APDVENKENG EVNGVHSFRE YSLEQLKIAT SCFALENVVS
EHGETAPNVV YQGKLENHMK IAIKRFSGTA WPDPRQFLEE ARLVGQLRSK RMANLLGYCC
EGGERLLVAE FMPNETLAKH LFHWDTEPMK WAMRLRVALY ISEALEYCSN NGHTLYHDLN
AYRVLFDEEC NPRLSTFGLM KNSRDGKSYS TNLAFTPPEY LRTGRITAES VIYSFGTLLL
DLLTGKHIPP SHALDLIRDR NLQTLTDSCL EGQFSDSDGT ELVRLTSCCL QYEARERPNI
KSLVTALISL QKDTEVLSHV LMGLPQSGTF ASPPSPFAEA CSGKDLTSMV EILEKIGYKD
DEDLSFMWTE QMQEAINSKK KGDIAFRRKD FSEAIEFYTQ FLDLGMISAT VLVRRSQSYL
MSNMAKEALD DAMKAQGISP VWYVALYLQS AALSVLGMEK ESQIALTEGS ILEARKISAS
TQN
