BSL1_ARATH
ID BSL1_ARATH Reviewed; 881 AA.
AC Q8L7U5; Q9ZTA4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Serine/threonine-protein phosphatase BSL1;
DE EC=3.1.3.16;
DE AltName: Full=BSU1-like protein 1;
GN Name=BSL1; OrderedLocusNames=At4g03080; ORFNames=T4I9.4;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14977918; DOI=10.1101/gad.1174204;
RA Mora-Garcia S., Vert G., Yin Y., Cano-Delgado A., Cheong H., Chory J.;
RT "Nuclear protein phosphatases with Kelch-repeat domains modulate the
RT response to brassinosteroids in Arabidopsis.";
RL Genes Dev. 18:448-460(2004).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17368080; DOI=10.1016/j.tplants.2007.03.003;
RA Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.;
RT "Arabidopsis PPP family of serine/threonine phosphatases.";
RL Trends Plant Sci. 12:169-176(2007).
RN [6]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP INTERACTION WITH CDG1 AND CDL1.
RX PubMed=21855796; DOI=10.1016/j.molcel.2011.05.037;
RA Kim T.W., Guan S., Burlingame A.L., Wang Z.Y.;
RT "The CDG1 kinase mediates brassinosteroid signal transduction from BRI1
RT receptor kinase to BSU1 phosphatase and GSK3-like kinase BIN2.";
RL Mol. Cell 43:561-571(2011).
CC -!- FUNCTION: Phosphatase involved in elongation process, probably by
CC acting as a regulator of brassinolide signaling.
CC {ECO:0000269|PubMed:14977918}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with CDG1 and CDL1. {ECO:0000269|PubMed:21855796}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19245862}.
CC -!- TISSUE SPECIFICITY: Expressed in mature cauline leaves and at the tip
CC of influorescence, including flowers. Expressed at lower level in young
CC tissues relative to older ones. {ECO:0000269|PubMed:14977918}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79097.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77793.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF069442; AAC79097.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161496; CAB77793.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82268.1; -; Genomic_DNA.
DR EMBL; AY126992; AAM83219.1; -; mRNA.
DR PIR; T01385; T01385.
DR RefSeq; NP_192217.2; NM_116542.5.
DR AlphaFoldDB; Q8L7U5; -.
DR SMR; Q8L7U5; -.
DR BioGRID; 13388; 4.
DR IntAct; Q8L7U5; 1.
DR STRING; 3702.AT4G03080.1; -.
DR iPTMnet; Q8L7U5; -.
DR PaxDb; Q8L7U5; -.
DR PRIDE; Q8L7U5; -.
DR ProteomicsDB; 240511; -.
DR EnsemblPlants; AT4G03080.1; AT4G03080.1; AT4G03080.
DR GeneID; 828097; -.
DR Gramene; AT4G03080.1; AT4G03080.1; AT4G03080.
DR KEGG; ath:AT4G03080; -.
DR Araport; AT4G03080; -.
DR TAIR; locus:2139399; AT4G03080.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_004962_7_1_1; -.
DR InParanoid; Q8L7U5; -.
DR OMA; YGFQDEC; -.
DR OrthoDB; 124339at2759; -.
DR PRO; PR:Q8L7U5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7U5; baseline and differential.
DR Genevisible; Q8L7U5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:InterPro.
DR CDD; cd07419; MPP_Bsu1_C; 1.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041758; MPP_BSL_C.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR012391; Ser/Thr_prot_Pase_BSU1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036363; PPP_BSU1; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Kelch repeat; Manganese; Metal-binding; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Repeat.
FT CHAIN 1..881
FT /note="Serine/threonine-protein phosphatase BSL1"
FT /id="PRO_0000058905"
FT REPEAT 60..109
FT /note="Kelch 1"
FT REPEAT 269..320
FT /note="Kelch 2"
FT REPEAT 338..385
FT /note="Kelch 3"
FT REGION 368..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 651
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 584
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 586
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 618
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 618
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 650
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 782
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LR78"
FT CONFLICT 794
FT /note="Q -> P (in Ref. 1; AAM83219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 881 AA; 96146 MW; 6EC45417BAEBD6E0 CRC64;
MGSKPWLHPA PQYKTLETFW DDEDDAPGPR CAHTLTAVAA TKTHGPRLIL FGGATAIEGG
SSSVPGIRLA GVTNTVHSYD ILTRKWTRLK PAGEPPSPRA AHAAAAVGTM VVFQGGIGPA
GHSTDDLYVL DMTNDKFKWH RVVVQGDGPG PRYGHVMDLV SQRYLVTVTG NDGKRALSDA
WALDTAQKPY VWQRLNPDGD RPSARMYASG SARSDGMFLL CGGRDTLGAP LGDAYGLLMH
RNGQWEWTLA PGVAPSPRYQ HAAVFVGARL HVSGGVLRGG RVIDAEASVA VLDTAAGVWL
DRNGQVTSAR GSKGQIDQDP SFELMRRCRH GAASVGIRIY VHGGLRGDVL LDDFLVAENS
TFQSDISSPL LASDRTQQSS TPRFSYAARP PSGSEPSFSM SEGLSLDENS LEKLTEASAA
EAEVASSVWR AAQLGAGTLD EEPSTSDASS PIVESTTDGT ANEGDVRLHP RAVVVAKETV
GSLGGMVRQL SLDQFQNESR RMVPMNNSDV PQPTKKFTRQ KSPQGLHKKV IAALLRPRNW
KPPGNRKFFL DSYEVGELCY AAEQIFMHEQ TVLQLKAPIK VFGDLHGQFG DLMRLFDEYG
FPSTAGDITY IDYLFLGDYV DRGQHSLETI TLLLALKIEY PENVHLIRGN HEAADINALF
GFRLECIERM GENDGIWAWT RFNQLFNYLP LAALIENKII CMHGGIGRSI STVEQIEKIE
RPITMDAGSL VLMDLLWSDP TENDSIEGLR PNARGPGLVT FGPDRVTEFC KRNKLQLIIR
AHECVMDGFE RFAQGQLITL FSATNYCGTA NNAGAILVVG RGLVIVPKLI HPLPPPILSP
ENSPEHSGDD AWMQELNIQR PPTPTRGRPQ PDFDRSSLAY I
