ID   BSL3_ARATH              Reviewed;        1006 AA.
AC   Q9SHS7; Q0WPF9;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Serine/threonine-protein phosphatase BSL3;
DE            EC=3.1.3.16;
DE   AltName: Full=BSU1-like protein 3;
GN   Name=BSL3; OrderedLocusNames=At2g27210; ORFNames=T22O13.2;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Root;
RX   PubMed=18433157; DOI=10.1021/pr8000173;
RA   de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA   Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA   Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT   spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [7]
RP   SUBCELLULAR LOCATION.
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).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19245862}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SHS7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SHS7-2; Sequence=VSP_028729, VSP_028730;
CC   -!- TISSUE SPECIFICITY: Expressed throughout the plant, with a higher level
CC       in younger parts. {ECO:0000269|PubMed:14977918}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD26883.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007290; AAD26883.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07953.1; -; Genomic_DNA.
DR   EMBL; AK229113; BAF00990.1; -; mRNA.
DR   PIR; B84670; B84670.
DR   RefSeq; NP_180289.3; NM_128279.4. [Q9SHS7-1]
DR   AlphaFoldDB; Q9SHS7; -.
DR   SMR; Q9SHS7; -.
DR   BioGRID; 2615; 2.
DR   STRING; 3702.Q9SHS7; -.
DR   iPTMnet; Q9SHS7; -.
DR   PaxDb; 3702-AT2G27210-1; -.
DR   ProteomicsDB; 240635; -. [Q9SHS7-1]
DR   EnsemblPlants; AT2G27210.1; AT2G27210.1; AT2G27210. [Q9SHS7-1]
DR   GeneID; 817263; -.
DR   Gramene; AT2G27210.1; AT2G27210.1; AT2G27210. [Q9SHS7-1]
DR   KEGG; ath:AT2G27210; -.
DR   Araport; AT2G27210; -.
DR   TAIR; AT2G27210; BSL3.
DR   eggNOG; KOG0374; Eukaryota.
DR   eggNOG; KOG0379; Eukaryota.
DR   HOGENOM; CLU_004962_7_0_1; -.
DR   InParanoid; Q9SHS7; -.
DR   OrthoDB; 311640at2759; -.
DR   PhylomeDB; Q9SHS7; -.
DR   PRO; PR:Q9SHS7; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SHS7; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
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:0009742; P:brassinosteroid mediated signaling pathway; IEA:InterPro.
DR   CDD; cd07419; MPP_Bsu1_C; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR011498; Kelch_2.
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   PANTHER; PTHR46422; SERINE/THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR   PANTHER; PTHR46422:SF4; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR   Pfam; PF07646; Kelch_2; 1.
DR   Pfam; PF13415; Kelch_3; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF036363; PPP_BSU1; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   Genevisible; Q9SHS7; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Kelch repeat; Manganese; Metal-binding;
KW   Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome; Repeat.
FT   CHAIN           1..1006
FT                   /note="Serine/threonine-protein phosphatase BSL3"
FT                   /id="PRO_0000058907"
FT   REPEAT          138..184
FT                   /note="Kelch 1"
FT   REPEAT          242..290
FT                   /note="Kelch 2"
FT   REPEAT          295..345
FT                   /note="Kelch 3"
FT   REPEAT          351..398
FT                   /note="Kelch 4"
FT   REPEAT          419..465
FT                   /note="Kelch 5"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1006
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        982..997
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        776
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         709
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         711
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         743
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         743
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         775
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         828
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         907
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         616
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LR78"
FT   MOD_RES         964
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LR78"
FT   VAR_SEQ         655..707
FT                   /note="VVAHLLKPRGWKPPVRRQFFLDCNEIADLCDSAERIFSSEPTVLQLKAPIKI
FT                   F -> NVSSQANLLCYSLKLLLRYLVICMASLGISCAFLMNMVHHQQLETYHTSITSS
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_028729"
FT   VAR_SEQ         708..1006
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_028730"
SQ   SEQUENCE   1006 AA;  107523 MW;  E855AC8655715F64 CRC64;
     MDLDSSMVPE NDQDPIATSE NQSPMEEKEE ASEQQTGSES ESASLTPSLP PPSQQQQQQQ
     QQPQVTAVVG PRCAPTYSVV NAIIEKKEDG PGPRCGHTLT AVPAVGEEGT SSYIGPRLIL
     FGGATALEGN SGGTGTPTSA GSAGIRLAGA TADVHCYDVL SNKWSRLTPY GEPPSPRAAH
     VATAVGTMVV IQGGIGPAGL SAEDLHVLDL TQQRPRWHRV VVQGPGPGPR YGHVMALVGQ
     RYLMAIGGND GKRPLADVWA LDTAAKPYEW RKLEPEGEGP PPCMYATASA RSDGLLLLCG
     GRDANSVPLA SAYGLAKHRD GRWEWAIAPG VSPSARYQHA AVFVNARLHV SGGALGGGRM
     VEDSSSVAVL DTAAGVWCDT KSVVTSPRTG RYSADAAGGD ASVELTRRCR HAAAAVGDLI
     FIYGGLRGGV LLDDLLVAED LAAAETTSAA SHAAAAAAAT NTPPGRSPGR YGFSDERTGE
     LPESAPDAVV LGSPVAPPVN GDMYTDISTE NAMVPGIRRT SKGVEYLVEA SAAEAEAISA
     TLAAAKARQV NGEVELPDRD RGAEATPSGK PSLSLIKPDS AVPNSVIPAG VRLHHRAVVV
     AAETGGALGG MVRQLSIDQF ENEGRRVSYG TPESATAARK LLDRQMSINS VPKKVVAHLL
     KPRGWKPPVR RQFFLDCNEI ADLCDSAERI FSSEPTVLQL KAPIKIFGDL HGQFGDLMRL
     FDEYGSPSTA GDISYIDYLF LGDYVDRGQH SLETITLLLA LKVEYQHNVH LIRGNHEAAD
     INALFGFRIE CIERMGERDG IWVWHRINRL FNWLPLAALI EKKIICMHGG IGRSINHVEQ
     IENIQRPITM EAGSIVLMDL LWSDPTENDS VEGLRPNARG PGLVTFGPDR VMEFCNNNDL
     QLIVRAHECV MDGFERFAQG HLITLFSATN YCGTANNAGA ILVLGRDLVV VPKLIHPLPP
     AITSPETSPE RHIEDTWMQE LNVNRPPTPT RGRPQNPNDR GSLAWI
//