Q8L7U5 (BSL1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase BSL1
EC=3.1.3.16

Alternative name(s):
BSU1-like protein 1

Gene names

Name:	BSL1
Ordered Locus Names:	At4g03080
ORF Names:	T4I9.4

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	881 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.
Tissue specificity	Expressed in mature cauline leaves and at the tip of influorescence, including flowers. Expressed at lower level in young tissues relative to older ones. Ref.4
Sequence similarities	Belongs to the PPP phosphatase family. BSU subfamily. Contains 3 Kelch repeats.
Sequence caution	The sequence AAC79097.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB77793.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Nucleus
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 17317660. 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 881	881	Serine/threonine-protein phosphatase BSL1		PRO_0000058905
Regions
	Repeat	60 – 109	50	Kelch 1
	Repeat	269 – 320	52	Kelch 2
	Repeat	338 – 385	48	Kelch 3
Sites
	Active site	651	1	Proton donor By similarity
	Metal binding	584	1	Iron By similarity
	Metal binding	586	1	Iron By similarity
	Metal binding	618	1	Iron By similarity
	Metal binding	618	1	Manganese By similarity
	Metal binding	650	1	Manganese By similarity
	Metal binding	703	1	Manganese By similarity
	Metal binding	782	1	Manganese By similarity
Amino acid modifications
	Modified residue	491	1	Phosphoserine Ref.6 Ref.7
Experimental info
	Sequence conflict	794	1	Q → P in AAM83219. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8L7U5 [UniParc]. Last modified May 3, 2011. Version 2. Checksum: 6EC45417BAEBD6E0	FASTA	881	96,146
	10 20 30 40 50 60 MGSKPWLHPA PQYKTLETFW DDEDDAPGPR CAHTLTAVAA TKTHGPRLIL FGGATAIEGG 70 80 90 100 110 120 SSSVPGIRLA GVTNTVHSYD ILTRKWTRLK PAGEPPSPRA AHAAAAVGTM VVFQGGIGPA 130 140 150 160 170 180 GHSTDDLYVL DMTNDKFKWH RVVVQGDGPG PRYGHVMDLV SQRYLVTVTG NDGKRALSDA 190 200 210 220 230 240 WALDTAQKPY VWQRLNPDGD RPSARMYASG SARSDGMFLL CGGRDTLGAP LGDAYGLLMH 250 260 270 280 290 300 RNGQWEWTLA PGVAPSPRYQ HAAVFVGARL HVSGGVLRGG RVIDAEASVA VLDTAAGVWL 310 320 330 340 350 360 DRNGQVTSAR GSKGQIDQDP SFELMRRCRH GAASVGIRIY VHGGLRGDVL LDDFLVAENS 370 380 390 400 410 420 TFQSDISSPL LASDRTQQSS TPRFSYAARP PSGSEPSFSM SEGLSLDENS LEKLTEASAA 430 440 450 460 470 480 EAEVASSVWR AAQLGAGTLD EEPSTSDASS PIVESTTDGT ANEGDVRLHP RAVVVAKETV 490 500 510 520 530 540 GSLGGMVRQL SLDQFQNESR RMVPMNNSDV PQPTKKFTRQ KSPQGLHKKV IAALLRPRNW 550 560 570 580 590 600 KPPGNRKFFL DSYEVGELCY AAEQIFMHEQ TVLQLKAPIK VFGDLHGQFG DLMRLFDEYG 610 620 630 640 650 660 FPSTAGDITY IDYLFLGDYV DRGQHSLETI TLLLALKIEY PENVHLIRGN HEAADINALF 670 680 690 700 710 720 GFRLECIERM GENDGIWAWT RFNQLFNYLP LAALIENKII CMHGGIGRSI STVEQIEKIE 730 740 750 760 770 780 RPITMDAGSL VLMDLLWSDP TENDSIEGLR PNARGPGLVT FGPDRVTEFC KRNKLQLIIR 790 800 810 820 830 840 AHECVMDGFE RFAQGQLITL FSATNYCGTA NNAGAILVVG RGLVIVPKLI HPLPPPILSP 850 860 870 880 ENSPEHSGDD AWMQELNIQR PPTPTRGRPQ PDFDRSSLAY I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [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]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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]	"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana." Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C. J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, SUBCELLULAR LOCATION, MASS SPECTROMETRY. Strain: cv. Columbia.
[7]	"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-491, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF069442 Genomic DNA. Translation: AAC79097.1. Sequence problems. AL161496 Genomic DNA. Translation: CAB77793.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE82268.1. AY126992 mRNA. Translation: AAM83219.1.
IPI	IPI00526850.
PIR	T01385.
RefSeq	NP_192217.2. NM_116542.4.
UniGene	At.26278. At.48826.
3D structure databases
ProteinModelPortal	Q8L7U5.
SMR	Q8L7U5. Positions 129-352, 550-832.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8L7U5. 1 interaction.
STRING	3702.AT4G03080.1-P.
Proteomic databases
PaxDb	Q8L7U5.
PRIDE	Q8L7U5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G03080.1; AT4G03080.1; AT4G03080.
GeneID	828097.
KEGG	ath:AT4G03080.
Organism-specific databases
TAIR	At4g03080.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000246464.
InParanoid	Q8L7U5.
KO	K01090.
OMA	EQIFMHE.
Gene expression databases
Genevestigator	Q8L7U5.
GermOnline	AT4G03080. Arabidopsis thaliana.
Family and domain databases
Gene3D	2.120.10.80. 2 hits.
InterPro	IPR015915. Kelch-typ_b-propeller. IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. IPR012391. Ser/Thr_prot_Pase_BSU1. [Graphical view]
Pfam	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

BSL1_ARATH

Accession

Primary (citable) accession number: Q8L7U5
Secondary accession number(s): Q9ZTA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	May 3, 2011
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program