BSL3_ARATH
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 03-AUG-2022, entry version 150.
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; 1.
DR STRING; 3702.AT2G27210.1; -.
DR iPTMnet; Q9SHS7; -.
DR PaxDb; Q9SHS7; -.
DR PRIDE; Q9SHS7; -.
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; locus:2059610; AT2G27210.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_004962_7_0_1; -.
DR InParanoid; Q9SHS7; -.
DR OrthoDB; 124339at2759; -.
DR PhylomeDB; Q9SHS7; -.
DR PRO; PR:Q9SHS7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SHS7; baseline and differential.
DR Genevisible; Q9SHS7; AT.
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; 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; 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 Pfam; PF07646; Kelch_2; 1.
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 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
