BLUS1_ARATH
ID BLUS1_ARATH Reviewed; 487 AA.
AC O23304;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Serine/threonine-protein kinase BLUS1;
DE EC=2.7.11.1;
DE AltName: Full=Protein BLUE LIGHT SIGNALING 1;
GN Name=BLUS1; OrderedLocusNames=At4g14480; ORFNames=dl3280c;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP FUNCTION, MUTAGENESIS OF ASP-157; ALA-192; GLU-194 AND SER-348, DISRUPTION
RP PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-348,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH PHOT1.
RC STRAIN=cv. Columbia;
RX PubMed=23811955; DOI=10.1038/ncomms3094;
RA Takemiya A., Sugiyama N., Fujimoto H., Tsutsumi T., Yamauchi S., Hiyama A.,
RA Tada Y., Christie J.M., Shimazaki K.;
RT "Phosphorylation of BLUS1 kinase by phototropins is a primary step in
RT stomatal opening.";
RL Nat. Commun. 4:2094-2094(2013).
CC -!- FUNCTION: Ser/Thr protein kinase mediating a primary step for
CC phototropin signaling in guard cells. Essential for stomatal opening.
CC {ECO:0000269|PubMed:23811955}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with PHOT1 in the presence and absence of blue
CC light. {ECO:0000269|PubMed:23811955}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23811955}.
CC -!- TISSUE SPECIFICITY: Expressed in guard cells. Not detected in mesophyll
CC cells. {ECO:0000269|PubMed:23811955}.
CC -!- PTM: Phosphorylated at Ser-348 by both PHOT1 and PHOT2.
CC {ECO:0000269|PubMed:23811955}.
CC -!- DISRUPTION PHENOTYPE: Defective in leaf temperature decreases and
CC stomatal opening in response to blue light.
CC {ECO:0000269|PubMed:23811955}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; Z97336; CAB10227.1; -; Genomic_DNA.
DR EMBL; AL161539; CAB78490.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83449.1; -; Genomic_DNA.
DR PIR; A71407; A71407.
DR RefSeq; NP_193184.1; NM_117528.2.
DR AlphaFoldDB; O23304; -.
DR SMR; O23304; -.
DR BioGRID; 12392; 29.
DR IntAct; O23304; 21.
DR STRING; 3702.AT4G14480.1; -.
DR iPTMnet; O23304; -.
DR PaxDb; O23304; -.
DR PRIDE; O23304; -.
DR ProteomicsDB; 222816; -.
DR EnsemblPlants; AT4G14480.1; AT4G14480.1; AT4G14480.
DR GeneID; 827095; -.
DR Gramene; AT4G14480.1; AT4G14480.1; AT4G14480.
DR KEGG; ath:AT4G14480; -.
DR Araport; AT4G14480; -.
DR TAIR; locus:2129780; AT4G14480.
DR eggNOG; KOG0582; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; O23304; -.
DR OMA; YKAVCLP; -.
DR OrthoDB; 855861at2759; -.
DR PhylomeDB; O23304; -.
DR PRO; PR:O23304; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23304; baseline and differential.
DR Genevisible; O23304; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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-EC.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1902456; P:regulation of stomatal opening; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..487
FT /note="Serine/threonine-protein kinase BLUS1"
FT /id="PRO_0000423824"
FT DOMAIN 15..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 363..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..477
FT /evidence="ECO:0000255"
FT COMPBIAS 371..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23811955"
FT MUTAGEN 157
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:23811955"
FT MUTAGEN 192
FT /note="A->T: In blus1-2; loss of stomatal response to blue
FT light."
FT /evidence="ECO:0000269|PubMed:23811955"
FT MUTAGEN 194
FT /note="E->K: In blus1-1; loss of stomatal response to blue
FT light."
FT /evidence="ECO:0000269|PubMed:23811955"
FT MUTAGEN 348
FT /note="S->A: Loss of stomatal response to blue light."
FT /evidence="ECO:0000269|PubMed:23811955"
SQ SEQUENCE 487 AA; 54381 MW; 77D21D39D2FB4F20 CRC64;
MARNKLEFPL DAEAYEIICK IGVGVSASVY KAICIPMNSM VVAIKAIDLD QSRADFDSLR
RETKTMSLLS HPNILNAYCS FTVDRCLWVV MPFMSCGSLH SIVSSSFPSG LPENCISVFL
KETLNAISYL HDQGHLHRDI KAGNILVDSD GSVKLADFGV SASIYEPVTS SSGTTSSSLR
LTDIAGTPYW MAPEVVHSHT GYGFKADIWS FGITALELAH GRPPLSHLPP LKSLLMKITK
RFHFSDYEIN TSGSSKKGNK KFSKAFREMV GLCLEQDPTK RPSAEKLLKH PFFKNCKGLD
FVVKNVLHSL SNAEQMFMES QILIKSVGDD DEEEEEEDEE IVKNRRISGW NFREDDLQLS
PVFPATESDS SESSPREEDQ SKDKKEDDNV TITGYELGLG LSNEEAKNQE GEVVGFDKDL
VLEKLKVLKK SLEHQRARVS IIIEALSGDK EEKSREEELL EMVEKLKIEL ETEKLKTLRA
DKDSVLG
