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O60172

- PPA3_SCHPO

UniProt

O60172 - PPA3_SCHPO

Protein

Thiamine-repressible acid phosphatase SPBC21H7.03c

Gene

SPBC21H7.03c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    May dephosphorylate thiamine phosphates.By similarity

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei69 – 691NucleophileBy similarity
    Active sitei341 – 3411Proton donorBy similarity

    GO - Molecular functioni

    1. acid phosphatase activity Source: PomBase

    GO - Biological processi

    1. dephosphorylation Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thiamine-repressible acid phosphatase SPBC21H7.03c (EC:3.1.3.2)
    Gene namesi
    ORF Names:SPBC21H7.03c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC21H7.03c.

    Subcellular locationi

    Secretedcell wall By similarity

    GO - Cellular componenti

    1. cell wall-bounded periplasmic space Source: PomBase
    2. external side of plasma membrane Source: PomBase
    3. extracellular region Source: PomBase
    4. fungal-type cell wall Source: PomBase

    Keywords - Cellular componenti

    Cell wall, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 463445Thiamine-repressible acid phosphatase SPBC21H7.03cPRO_0000311718Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi221 – 2211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiO60172.
    PaxDbiO60172.

    Expressioni

    Inductioni

    Repressed by thiamine.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi4896.SPBC21H7.03c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO60172.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidine acid phosphatase family.Sequence Analysis

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG260296.
    HOGENOMiHOG000115655.
    KOiK01078.
    OMAiVESAQWF.
    OrthoDBiEOG7B31X6.
    PhylomeDBiO60172.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    InterProiIPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    IPR016274. Histidine_acid_Pase_euk.
    [Graphical view]
    PfamiPF00328. His_Phos_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
    SUPFAMiSSF53254. SSF53254. 1 hit.
    PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
    PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O60172-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQLCIISLWF LAAFIVNADN VQFEDYESNF FFKEHLGTLS PYHEPYFDGL    50
    DSAFPETCEI QQVHLLQRHG SRNPTGDVTA TDVYSSQYLN NFQEKLLNGS 100
    IPVNFSYPEN PLCFIKQWTP VIDAENADQL SSRGRLELFD LGRQLYQRYY 150
    KLFDSYVYDI NTAEQERVVE SAKWFTYGLF GDKMYEKTNF ILISEGKAAG 200
    ANSLSMYNAC PVFKDNNFHK NATDAAHAVW RNIFIEPIVN RLAKYFDSSY 250
    KLTINDVRSL FYICEYEIAI KDHSDFCSIF TPSEFLNFEY DSDLDQAYGG 300
    GPVSEWASTL GGAYINNLAD SLRNVTNPDF DRKVFLAFTH DSNIIPVEAA 350
    LGFFPDITPQ NPLPTDKNIY TYSQKTSSFV PFAGNLITEL FFCSDSKYYV 400
    RHLVNQQVYP LIDCGYGPSG TSDGLCELQA YLNSPIRANS TSNGISIFNT 450
    ECQARPTNVT IYF 463
    Length:463
    Mass (Da):52,759
    Last modified:August 1, 1998 - v1
    Checksum:i6C41AF422C6D624A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAA18863.1.
    PIRiT39929.
    RefSeqiNP_595928.1. NM_001021836.2.

    Genome annotation databases

    EnsemblFungiiSPBC21H7.03c.1; SPBC21H7.03c.1:pep; SPBC21H7.03c.
    GeneIDi2540420.
    KEGGispo:SPBC21H7.03c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAA18863.1 .
    PIRi T39929.
    RefSeqi NP_595928.1. NM_001021836.2.

    3D structure databases

    ProteinModelPortali O60172.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4896.SPBC21H7.03c-1.

    Proteomic databases

    MaxQBi O60172.
    PaxDbi O60172.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC21H7.03c.1 ; SPBC21H7.03c.1:pep ; SPBC21H7.03c .
    GeneIDi 2540420.
    KEGGi spo:SPBC21H7.03c.

    Organism-specific databases

    PomBasei SPBC21H7.03c.

    Phylogenomic databases

    eggNOGi NOG260296.
    HOGENOMi HOG000115655.
    KOi K01078.
    OMAi VESAQWF.
    OrthoDBi EOG7B31X6.
    PhylomeDBi O60172.

    Miscellaneous databases

    NextBioi 20801547.
    PROi O60172.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    InterProi IPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    IPR016274. Histidine_acid_Pase_euk.
    [Graphical view ]
    Pfami PF00328. His_Phos_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000894. Acid_phosphatase. 1 hit.
    SUPFAMi SSF53254. SSF53254. 1 hit.
    PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
    PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "Activation of AP-1-dependent transcription by a truncated translation initiation factor."
      Jenkins C.C.L., Mata J., Crane R.F., Thomas B., Akoulitchev A., Baehler J., Norbury C.J.
      Eukaryot. Cell 4:1840-1850(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiPPA3_SCHPO
    AccessioniPrimary (citable) accession number: O60172
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3