BSL2_ARATH
ID BSL2_ARATH Reviewed; 1018 AA.
AC Q9SJF0; Q0WKX2;
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 BSL2;
DE EC=3.1.3.16;
DE AltName: Full=BSU1-like protein 2;
GN Name=BSL2; OrderedLocusNames=At1g08420; ORFNames=T27G7.10;
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=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 [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] OF 282-1018.
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].
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 [7]
RP INTERACTION WITH BSK8, AND SUBCELLULAR LOCATION.
RX PubMed=24924143; DOI=10.1021/pr5003164;
RA Wu X., Sklodowski K., Encke B., Schulze W.X.;
RT "A kinase-phosphatase signaling module with BSK8 and BSL2 involved in
RT regulation of sucrose-phosphate synthase.";
RL J. Proteome Res. 13:3397-3409(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 40-328 IN COMPLEX WITH ATP
RP ANALOG.
RX PubMed=23911552; DOI=10.1016/j.jmb.2013.07.034;
RA Grutter C., Sreeramulu S., Sessa G., Rauh D.;
RT "Structural characterization of the RLCK family member BSK8: a pseudokinase
RT with an unprecedented architecture.";
RL J. Mol. Biol. 425:4455-4467(2013).
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 BSK8. {ECO:0000269|PubMed:23911552}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23911552}. Cell
CC membrane {ECO:0000269|PubMed:23911552}. Nucleus {ECO:0000250}.
CC Note=Mainly cytoplasmic. Colocalizes with BSK8 at the plasma membrane.
CC {ECO:0000269|PubMed:23911552}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SJF0-1; Sequence=Displayed;
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=AAF22889.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006932; AAF22889.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28287.1; -; Genomic_DNA.
DR EMBL; AK230437; BAF02235.1; -; mRNA.
DR PIR; E86217; E86217.
DR RefSeq; NP_172318.1; NM_100715.4. [Q9SJF0-1]
DR AlphaFoldDB; Q9SJF0; -.
DR SMR; Q9SJF0; -.
DR BioGRID; 22603; 3.
DR STRING; 3702.AT1G08420.1; -.
DR iPTMnet; Q9SJF0; -.
DR PaxDb; Q9SJF0; -.
DR PRIDE; Q9SJF0; -.
DR ProteomicsDB; 239101; -. [Q9SJF0-1]
DR EnsemblPlants; AT1G08420.1; AT1G08420.1; AT1G08420. [Q9SJF0-1]
DR GeneID; 837362; -.
DR Gramene; AT1G08420.1; AT1G08420.1; AT1G08420. [Q9SJF0-1]
DR KEGG; ath:AT1G08420; -.
DR Araport; AT1G08420; -.
DR TAIR; locus:2201776; AT1G08420.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_004962_7_0_1; -.
DR InParanoid; Q9SJF0; -.
DR OMA; MVPVNDH; -.
DR PhylomeDB; Q9SJF0; -.
DR PRO; PR:Q9SJF0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SJF0; baseline and differential.
DR Genevisible; Q9SJF0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0009742; P:brassinosteroid mediated signaling pathway; IEA:InterPro.
DR CDD; cd07419; MPP_Bsu1_C; 1.
DR Gene3D; 2.120.10.80; -; 3.
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; Cell membrane; Cytoplasm; Hydrolase; Kelch repeat;
KW Manganese; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Repeat.
FT CHAIN 1..1018
FT /note="Serine/threonine-protein phosphatase BSL2"
FT /id="PRO_0000058906"
FT REPEAT 149..195
FT /note="Kelch 1"
FT REPEAT 253..301
FT /note="Kelch 2"
FT REPEAT 306..356
FT /note="Kelch 3"
FT REPEAT 362..409
FT /note="Kelch 4"
FT REPEAT 430..479
FT /note="Kelch 5"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 787
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 720
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 722
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 754
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 754
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 786
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 839
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 918
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LR78"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LR78"
SQ SEQUENCE 1018 AA; 108580 MW; F2D48037DF4FAAB4 CRC64;
MDEDSSMVAD NDQDREFQSL DGGQSPSPME RETPQQMNDQ SPPPEGGSVP TPPPSDPNPA
TSQQQAAAVV GQEQQPALVV GPRCAPTYSV VDAMMDKKED GPGPRCGHTL TAVPAVGDEG
TPGYIGPRLV LFGGATALEG NSGGTGTPTS AGSAGIRLAG ATADVHCYDV LSNKWTRLTP
FGEPPTPRAA HVATAVGTMV VIQGGIGPAG LSAEDLHVLD LTQQRPRWHR VVVQGPGPGP
RYGHVMALVG QRYLMAIGGN DGKRPLADVW ALDTAAKPYE WRKLEPEGEG PPPCMYATAS
ARSDGLLLLC GGRDANSVPL ASAYGLAKHR DGRWEWAIAP GVSPSSRYQH AAVFVNARLH
VSGGALGGGR MVEDSSSVAV LDTAAGVWCD TKSVVTSPRT GRYSADAAGG DASVELTRRC
RHAAAAVGDL IFIYGGLRGG VLLDDLLVAE DLAAAETTYA ASHAAAAAAT NSPPGRLPGR
YGFSDERNRE LSESAADGAV VLGSPVAPPV NGDMHTDISP ENALLPGTRR TNKGVEYLVE
ASAAEAEAIS ATLAAAKARQ VNGEVELPDR DCGAEATPSG KPTFSLIKPD SMGSMSVTPA
GIRLHHRAVV VAAETGGALG GMVRQLSIDQ FENEGRRVSY GTPESATAAR KLLDRQMSIN
SVPKKVIAHL LKPRGWKPPV RRQFFLDCNE IADLCDSAER IFASEPTVLQ LKAPIKIFGD
LHGQFGDLMR LFDEYGSPST AGDISYIDYL FLGDYVDRGQ HSLETISLLL ALKVEYQHNV
HLIRGNHEAA DINALFGFRI ECIERMGERD GIWVWHRINR LFNWLPLAAS IEKKIICMHG
GIGRSINHVE QIENIQRPIT MEAGSIVLMD LLWSDPTEND SVEGLRPNAR GPGLVTFGPD
RVMEFCNNND LQLIVRAHEC VMDGFERFAQ GHLITLFSAT NYCGTANNAG AILVLGRDLV
VVPKLIHPLP PALSSPETSP ERHIEDTWMQ ELNANRPATP TRGRPQNSND RGGSLAWM
