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Reviewed, UniProtKB/Swiss-Prot Q8L7U5 (BSL1_ARATH)

Last modified June 16, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length881 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Phosphatase involved in elongation process, probably by acting as a regulator of brassinolide signaling. Ref.3

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 in mature cauline leaves and at the tip of influorescence, including flowers. Expressed at lower level in young tissues relative to older ones. Ref.3

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 componentNucleus
   DomainKelch repeat
Repeat
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: TAIR

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 881881Serine/threonine-protein phosphatase BSL1
PRO_0000058905

Regions

Repeat60 – 10950Kelch 1
Repeat269 – 32052Kelch 2
Repeat338 – 38548Kelch 3

Sites

Active site6511Proton donor By similarity
Metal binding5841Iron By similarity
Metal binding5861Iron By similarity
Metal binding6181Iron By similarity
Metal binding6181Manganese By similarity
Metal binding6501Manganese By similarity
Metal binding7031Manganese By similarity
Metal binding7821Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8L7U5-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: CFC54406BBFAD6E1

FASTA88196,115
        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 RFAPGQLITL FSATNYCGTA NNAGAILVVG RGLVIVPKLI HPLPPPILSP 

       850        860        870        880 
ENSPEHSGDD AWMQELNIQR PPTPTRGRPQ PDFDRSSLAY I 

« Hide

References

« Hide '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. expand/collapse author list , 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: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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. expand/collapse author list , 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"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: 14977918] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[4]"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: 17368080] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.

Cross-references

Sequence databases

AF069442 Genomic DNA. Translation: AAC79097.1. Sequence problems.
AL161496 Genomic DNA. Translation: CAB77793.1. Sequence problems.
AY126992 mRNA. Translation: AAM83219.1.
IPIIPI00526850.
PIRT01385.

3D structure databases

HSSPHSSP built from PDB template 1IT6 based on UniProtKB P36873.
ModBaseSearch...

Proteomic databases

PRIDEQ8L7U5.
ProMEXQ8L7U5.

Genome annotation databases

GenomeReviewsGene locus AT4G03080 in contig CT486007_GR.

Organism-specific databases

TAIRAt4g03080.

Enzyme and pathway databases

BRENDA3.1.3.16. 302.

Gene expression databases

ArrayExpressQ8L7U5.
GermOnlineAT4G03080. Arabidopsis thaliana.

Family and domain databases

InterProIPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
IPR011498. Kelch_2.
IPR004843. M-pesterase.
IPR012391. PPP_BSU1.
IPR006186. T_phtase_apaH.
[Graphical view]
Gene3DG3DSA:2.120.10.80. Kelch-typ_b-propeller. 2 hits.
PANTHERPTHR11668. T_phtase_apaH. 1 hit.
PfamPF01344. Kelch_1. 1 hit.
PF07646. Kelch_2. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFPIRSF036363. PPP_BSU1. 1 hit.
PRINTSPR00114. STPHPHTASE.
ProDomPD000252. T_phtase_apaH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBSL1_ARATH
AccessionPrimary (citable) accession number: Q8L7U5
Secondary accession number(s): Q9ZTA4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents