BSU1_ARATH
ID BSU1_ARATH Reviewed; 793 AA.
AC Q9LR78;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Serine/threonine-protein phosphatase BSU1;
DE EC=3.1.3.16;
DE AltName: Full=Bri1 suppressor protein 1;
GN Name=BSU1; OrderedLocusNames=At1g03445; ORFNames=F21B7.7;
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 [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR
RP LOCATION, 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 [2]
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 [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 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 [5]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH CDG1; CDL1 AND ASK7/BIN2,
RP AND PHOSPHORYLATION AT SER-395; SER-444 AND SER-764.
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 that acts as a positive regulator of
CC brassinosteroid (BR) signaling (PubMed:14977918, PubMed:21855796).
CC Dephosphorylates BES1, a transcription factor that regulates the
CC expression of BR-response genes, thereby playing an important role in
CC the regulation of response to BRs (PubMed:14977918). Inactivates the
CC negative regulator of BR signaling ASK7/BIN2 by dephosphorylation at
CC 'Tyr-200' (PubMed:21855796). {ECO:0000269|PubMed:14977918,
CC ECO:0000269|PubMed:21855796}.
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 Evidence={ECO:0000269|PubMed:14977918};
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 Evidence={ECO:0000269|PubMed:14977918};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation at Ser-764 by CDG1.
CC {ECO:0000269|PubMed:21855796}.
CC -!- SUBUNIT: Interacts with CDG1, CDL1 and ASK7/BIN2.
CC {ECO:0000269|PubMed:21855796}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14977918}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in young, elongating tissues. In
CC young seedlings, it is expressed at the base of the hypocotyl, at the
CC tip and most peripheral cell layers of cotyledons, and in the vascular
CC cylinder of roots, particularly in the elongation zone and at the point
CC of emergence of lateral roots. In mature plants, it is still present in
CC the root vasculature, but almost completely absent in fully expanded
CC stems and leaves. In flowers, it is mainly expressed in sepal veins,
CC anther filaments, and in the style, suggesting that BSU1 is expressed
CC in actively growing regions and apparently enriched in vascular
CC tissues. {ECO:0000269|PubMed:14977918}.
CC -!- PTM: Phosphorylated at Ser-395 and Ser-444. Phosphorylated at Ser-764
CC by CDG1 and CDL1. {ECO:0000269|PubMed:21855796}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY372269; AAR19789.1; -; mRNA.
DR EMBL; AC002560; AAF86539.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27572.1; -; Genomic_DNA.
DR RefSeq; NP_171844.6; NM_100227.6.
DR AlphaFoldDB; Q9LR78; -.
DR SMR; Q9LR78; -.
DR BioGRID; 24043; 4.
DR STRING; 3702.AT1G03445.1; -.
DR iPTMnet; Q9LR78; -.
DR PaxDb; Q9LR78; -.
DR PRIDE; Q9LR78; -.
DR ProteomicsDB; 239132; -.
DR EnsemblPlants; AT1G03445.1; AT1G03445.1; AT1G03445.
DR GeneID; 838804; -.
DR Gramene; AT1G03445.1; AT1G03445.1; AT1G03445.
DR KEGG; ath:AT1G03445; -.
DR Araport; AT1G03445; -.
DR TAIR; locus:2825042; AT1G03445.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_004962_7_1_1; -.
DR InParanoid; Q9LR78; -.
DR OMA; NERGSHI; -.
DR OrthoDB; 124339at2759; -.
DR PhylomeDB; Q9LR78; -.
DR PRO; PR:Q9LR78; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LR78; baseline and differential.
DR Genevisible; Q9LR78; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; IDA:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:InterPro.
DR GO; GO:1900459; P:positive regulation of brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IDA:TAIR.
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; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR012391; Ser/Thr_prot_Pase_BSU1.
DR InterPro; IPR031675; STPPase_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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..793
FT /note="Serine/threonine-protein phosphatase BSU1"
FT /id="PRO_0000058904"
FT REPEAT 53..109
FT /note="Kelch 1"
FT REPEAT 110..160
FT /note="Kelch 2"
FT REPEAT 214..262
FT /note="Kelch 3"
FT REPEAT 264..314
FT /note="Kelch 4"
FT REPEAT 329..388
FT /note="Kelch 5"
FT ACT_SITE 577
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 576
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 629
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21855796"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21855796"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21855796"
SQ SEQUENCE 793 AA; 87789 MW; 07A083BD780EAA79 CRC64;
MAPDQSYQYP SPSYESIQTF YDTDEDWPGP RCGHTLTAVF VNNSHQLILF GGSTTAVANH
NSSLPEISLD GVTNSVHSFD VLTRKWTRLN PIGDVPSPRA CHAAALYGTL ILIQGGIGPS
GPSDGDVYML DMTNNKWIKF LVGGETPSPR YGHVMDIAAQ RWLVIFSGNN GNEILDDTWA
LDTRGPFSWD RLNPSGNQPS GRMYASGSSR EDGIFLLCGG IDHSGVTLGD TYGLKMDSDN
VWTPVPAVAP SPRYQHTAVF GGSKLHVIGG ILNRARLIDG EAVVAVLDTE TGEWVDTNQP
ETSASGANRQ NQYQLMRRCH HAAASFGSHL YVHGGIREDV LLDDLLVAET SQSSSPEPEE
DNPDNYMLLD DYLMDEPKPL SSEPEASSFI MRSTSEIAMD RLAEAHNLPT IENAFYDSAI
EGYVPLQHGA ETVGNRGGLV RTASLDQSTQ DLHKKVISTL LRPKTWTPPA NRDFFLSYLE
VKHLCDEVEK IFMNEPTLLQ LKVPIKVFGD IHGQYGDLMR LFHEYGHPSV EGDITHIDYL
FLGDYVDRGQ HSLEIIMLLF ALKIEYPKNI HLIRGNHESL AMNRIYGFLT ECEERMGESY
GFEAWLKINQ VFDYLPLAAL LEKKVLCVHG GIGRAVTIEE IENIERPAFP DTGSMVLKDI
LWSDPTMNDT VLGIVDNARG EGVVSFGPDI VKAFLERNGL EMILRAHECV IDGFERFADG
RLITVFSATN YCGTAQNAGA ILVIGRDMVI YPKLIHPHPP PISSSEEDYT DKAWMQELNI
EMPPTPARGE SSE
