Q9SJF0 (BSL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase BSL2
EC=3.1.3.16

Alternative name(s):
BSU1-like protein 2

Gene names

Name:	BSL2
Ordered Locus Names:	At1g08420
ORF Names:	T27G7.10

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1018 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phosphatase involved in elongation process, probably by acting as a regulator of brassinolide signaling. Ref.4
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Subcellular location	Nucleus By similarity.
Tissue specificity	Expressed throughout the plant, with a higher level in younger parts. Ref.4
Sequence similarities	Belongs to the PPP phosphatase family. BSU subfamily. Contains 5 Kelch repeats.
Sequence caution	The sequence AAF22889.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Kelch repeat Repeat
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 17317660PubMed 17644812. Source: TAIR
Molecular_function	iron ion binding Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: InterPro phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9SJF0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1018	1018	Serine/threonine-protein phosphatase BSL2		PRO_0000058906
Regions
	Repeat	149 – 195	47	Kelch 1
	Repeat	253 – 301	49	Kelch 2
	Repeat	306 – 356	51	Kelch 3
	Repeat	362 – 409	48	Kelch 4
	Repeat	430 – 479	50	Kelch 5
Sites
	Active site	787	1	Proton donor By similarity
	Metal binding	720	1	Iron By similarity
	Metal binding	722	1	Iron By similarity
	Metal binding	754	1	Iron By similarity
	Metal binding	754	1	Manganese By similarity
	Metal binding	786	1	Manganese By similarity
	Metal binding	839	1	Manganese By similarity
	Metal binding	918	1	Manganese By similarity
Amino acid modifications
	Modified residue	975	1	Phosphoserine Ref.6
	Modified residue	978	1	Phosphothreonine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 23, 2007. Version 2. Checksum: F2D48037DF4FAAB4	FASTA	1,018	108,580
	10 20 30 40 50 60 MDEDSSMVAD NDQDREFQSL DGGQSPSPME RETPQQMNDQ SPPPEGGSVP TPPPSDPNPA 70 80 90 100 110 120 TSQQQAAAVV GQEQQPALVV GPRCAPTYSV VDAMMDKKED GPGPRCGHTL TAVPAVGDEG 130 140 150 160 170 180 TPGYIGPRLV LFGGATALEG NSGGTGTPTS AGSAGIRLAG ATADVHCYDV LSNKWTRLTP 190 200 210 220 230 240 FGEPPTPRAA HVATAVGTMV VIQGGIGPAG LSAEDLHVLD LTQQRPRWHR VVVQGPGPGP 250 260 270 280 290 300 RYGHVMALVG QRYLMAIGGN DGKRPLADVW ALDTAAKPYE WRKLEPEGEG PPPCMYATAS 310 320 330 340 350 360 ARSDGLLLLC GGRDANSVPL ASAYGLAKHR DGRWEWAIAP GVSPSSRYQH AAVFVNARLH 370 380 390 400 410 420 VSGGALGGGR MVEDSSSVAV LDTAAGVWCD TKSVVTSPRT GRYSADAAGG DASVELTRRC 430 440 450 460 470 480 RHAAAAVGDL IFIYGGLRGG VLLDDLLVAE DLAAAETTYA ASHAAAAAAT NSPPGRLPGR 490 500 510 520 530 540 YGFSDERNRE LSESAADGAV VLGSPVAPPV NGDMHTDISP ENALLPGTRR TNKGVEYLVE 550 560 570 580 590 600 ASAAEAEAIS ATLAAAKARQ VNGEVELPDR DCGAEATPSG KPTFSLIKPD SMGSMSVTPA 610 620 630 640 650 660 GIRLHHRAVV VAAETGGALG GMVRQLSIDQ FENEGRRVSY GTPESATAAR KLLDRQMSIN 670 680 690 700 710 720 SVPKKVIAHL LKPRGWKPPV RRQFFLDCNE IADLCDSAER IFASEPTVLQ LKAPIKIFGD 730 740 750 760 770 780 LHGQFGDLMR LFDEYGSPST AGDISYIDYL FLGDYVDRGQ HSLETISLLL ALKVEYQHNV 790 800 810 820 830 840 HLIRGNHEAA DINALFGFRI ECIERMGERD GIWVWHRINR LFNWLPLAAS IEKKIICMHG 850 860 870 880 890 900 GIGRSINHVE QIENIQRPIT MEAGSIVLMD LLWSDPTEND SVEGLRPNAR GPGLVTFGPD 910 920 930 940 950 960 RVMEFCNNND LQLIVRAHEC VMDGFERFAQ GHLITLFSAT NYCGTANNAG AILVLGRDLV 970 980 990 1000 1010 VVPKLIHPLP PALSSPETSP ERHIEDTWMQ ELNANRPATP TRGRPQNSND RGGSLAWM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-1018. Strain: cv. Columbia.
[4]	"Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis." Mora-Garcia S., Vert G., Yin Y., Cano-Delgado A., Cheong H., Chory J. Genes Dev. 18:448-460(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[5]	"Arabidopsis PPP family of serine/threonine phosphatases." Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C. Trends Plant Sci. 12:169-176(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[6]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975 AND THR-978, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC006932 Genomic DNA. Translation: AAF22889.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE28287.1. AK230437 mRNA. Translation: BAF02235.1.
IPI	IPI00535417.
PIR	E86217.
RefSeq	NP_172318.1. NM_100715.3.
UniGene	At.27687.
3D structure databases
ProteinModelPortal	Q9SJF0.
SMR	Q9SJF0. Positions 666-968.
ModBase	Search...
Proteomic databases
PaxDb	Q9SJF0.
PRIDE	Q9SJF0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G08420.1; AT1G08420.1; AT1G08420.
GeneID	837362.
KEGG	ath:AT1G08420.
Organism-specific databases
TAIR	At1g08420.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000246464.
InParanoid	Q9SJF0.
OMA	DKEQSPD.
PhylomeDB	Q9SJF0.
ProtClustDB	CLSN2682801.
Gene expression databases
Genevestigator	Q9SJF0.
GermOnline	AT1G08420. Arabidopsis thaliana.
Family and domain databases
Gene3D	2.120.10.80. 1 hit.
InterPro	IPR015915. Kelch-typ_b-propeller. IPR011498. Kelch_2. IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. IPR012391. Ser/Thr_prot_Pase_BSU1. [Graphical view]
Pfam	PF07646. Kelch_2. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view]
PIRSF	PIRSF036363. PPP_BSU1. 1 hit.
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BSL2_ARATH

Accession

Primary (citable) accession number: Q9SJF0
Secondary accession number(s): Q0WKX2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	October 23, 2007
Last modified:	May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program