GenomeNet

Database: UniProt
Entry: BSU1_ARATH
LinkDB: BSU1_ARATH
Original site: 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   26-FEB-2020, entry version 139.
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};
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   SMR; Q9LR78; -.
DR   BioGrid; 24043; 4.
DR   STRING; 3702.AT1G03445.1; -.
DR   iPTMnet; Q9LR78; -.
DR   PaxDb; Q9LR78; -.
DR   PRIDE; Q9LR78; -.
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   eggNOG; ENOG410Z3NZ; LUCA.
DR   HOGENOM; CLU_004962_7_1_1; -.
DR   InParanoid; Q9LR78; -.
DR   KO; K14501; -.
DR   OMA; NERGSHI; -.
DR   OrthoDB; 124339at2759; -.
DR   PhylomeDB; Q9LR78; -.
DR   PRO; PR:Q9LR78; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Proteomes; UP000007605; Chromosome 1 top arm.
DR   Proteomes; UP000007605; Chromosome 1, ARATH_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: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   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   METAL           510
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250"
FT   METAL           512
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250"
FT   METAL           544
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250"
FT   METAL           544
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250"
FT   METAL           576
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250"
FT   METAL           629
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250"
FT   METAL           707
FT                   /note="Manganese 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
//
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