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Protein

Inositol-1,4,5-trisphosphate 5-phosphatase 1

Gene

syj1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Involved in distinct membrane trafficking and signal transduction pathways. Highly active against a range of soluble and lipid inositol phosphates. Active in dephosphorylating the 5-position of Ins(1,4,5)P3 and Ins(1,3,4,5)P4 and to a lesser extent Ins(1,4,5,6)P4. The enzyme is also active against PI(4,5)P2 presented in sonicated vesicles and Triton mixed micelles, and somewhat less active against PI(3,5)P2 in unilamellar vesicles. Activity against PI(3,5)P2 drops sharply when this substrate is presented in mixed micelles. Also hydrolyzes PIP3 to produce PI(3,4)P2.1 Publication

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.1 Publication

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=57.8 µM for Ins(1,4,5)P3 (at pH 7.4 and 30 degrees Celsius)1 Publication
  2. KM=10.9 µM for Ins(2,4,5)P3 (at pH 7.4 and 30 degrees Celsius)1 Publication
  3. KM=75.9 µM for Ins(2,4)P2 (at pH 7.4 and 30 degrees Celsius)1 Publication
  4. KM=5860 µM for p-nitrophenyl phosphate (at pH 7 and 30 degrees Celsius)1 Publication
  5. KM=182 µM for 3-O-methylfluorescein phosphate (at pH 7 and 30 degrees Celsius)1 Publication
  6. KM=530 µM for magnesium ions1 Publication
  7. KM=12 µM for manganese ions1 Publication
  8. KM=6.39 µM for nickel ions1 Publication
  9. KM=14.5 µM for cobalt ions1 Publication

    pH dependencei

    Optimum pH is about 7.4.1 Publication

    GO - Molecular functioni

    • calcium ion binding Source: PomBase
    • inositol-1,2,4,5,6-pentakisphosphate 5-phosphatase activity Source: PomBase
    • inositol-1,2,4,5-tetrakisphosphate 5-phosphatase activity Source: PomBase
    • inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity Source: PomBase
    • inositol-1,4,5-trisphosphate 5-phosphatase activity Source: PomBase
    • inositol-2,4,5,6-tetrakisphosphate 5-phosphatase activity Source: PomBase
    • inositol-2,4,5-triphosphate 5-phosphatase activity Source: PomBase
    • inositol-4,5,6-triphosphate 5-phosphatase activity Source: PomBase
    • inositol-4,5-bisphosphate 5-phosphatase activity Source: PomBase
    • phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity Source: PomBase
    • phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Source: PomBase
    • phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: PomBase

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid metabolism, Protein transport, Transport

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    ReactomeiR-SPO-1660499. Synthesis of PIPs at the plasma membrane.
    R-SPO-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
    R-SPO-1855204. Synthesis of IP3 and IP4 in the cytosol.
    SABIO-RKO43001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol-1,4,5-trisphosphate 5-phosphatase 1 (EC:3.1.3.36)
    Alternative name(s):
    Synaptojanin-like protein 1
    Gene namesi
    Name:syj1
    ORF Names:SPBC2G2.02
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    Proteomesi
    • UP000002485 Componenti: Chromosome II

    Organism-specific databases

    EuPathDBiFungiDB:SPBC2G2.02.
    PomBaseiSPBC2G2.02. syj1.

    Subcellular locationi

    GO - Cellular componenti

    • cell division site Source: PomBase
    • cell tip Source: PomBase
    • cytosol Source: PomBase
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi597 – 5971E → A or Q: Reduces the catalytic activity by 3 to 4 orders of magnitude. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10761076Inositol-1,4,5-trisphosphate 5-phosphatase 1PRO_0000209736Add
    BLAST

    Proteomic databases

    MaxQBiO43001.

    Interactioni

    Protein-protein interaction databases

    BioGridi276801. 39 interactions.
    MINTiMINT-4674514.

    Structurei

    Secondary structure

    1
    1076
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi536 – 54712Combined sources
    Helixi548 – 5514Combined sources
    Beta strandi553 – 56614Combined sources
    Helixi577 – 5804Combined sources
    Beta strandi583 – 5853Combined sources
    Beta strandi589 – 5968Combined sources
    Helixi611 – 62717Combined sources
    Beta strandi635 – 6439Combined sources
    Beta strandi646 – 6538Combined sources
    Helixi654 – 6596Combined sources
    Beta strandi660 – 66910Combined sources
    Beta strandi680 – 6889Combined sources
    Beta strandi691 – 6999Combined sources
    Helixi707 – 72014Combined sources
    Helixi724 – 7263Combined sources
    Beta strandi731 – 74010Combined sources
    Beta strandi745 – 7473Combined sources
    Helixi749 – 7579Combined sources
    Helixi761 – 7655Combined sources
    Helixi769 – 7757Combined sources
    Beta strandi778 – 7803Combined sources
    Beta strandi816 – 8238Combined sources
    Beta strandi825 – 8317Combined sources
    Beta strandi836 – 8394Combined sources
    Beta strandi842 – 85312Combined sources
    Helixi855 – 87622Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I9YX-ray2.00A534-880[»]
    1I9ZX-ray1.80A534-880[»]
    ProteinModelPortaliO43001.
    SMRiO43001. Positions 534-878.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43001.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini144 – 474331SACPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni534 – 880347CatalyticAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1000 – 104849Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the synaptojanin family.Curated
    In the central section; belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.Curated
    Contains 1 SAC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOGENOMiHOG000179717.
    InParanoidiO43001.
    OMAiGIMGIAG.
    OrthoDBiEOG7DRJBN.
    PhylomeDBiO43001.

    Family and domain databases

    Gene3Di3.60.10.10. 1 hit.
    InterProiIPR005135. Endo/exonuclease/phosphatase.
    IPR000300. IPPc.
    IPR002013. SAC_dom.
    [Graphical view]
    PfamiPF03372. Exo_endo_phos. 1 hit.
    PF02383. Syja_N. 1 hit.
    [Graphical view]
    SMARTiSM00128. IPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56219. SSF56219. 1 hit.
    PROSITEiPS50275. SAC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O43001-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQCLLREKPR SLALVNKDHA LMFHSVPQNK NSLSVCVAEF TALSEKPLEG
    60 70 80 90 100
    FRKISSHRIY GTLGLIELEG SNFLCVISGA SEVARVRDKE RVFRIMEVCF
    110 120 130 140 150
    YSVNRSNWDH IRQENYSPDI PDGYDTDTQG YDSYKYAAEP FSSLRKLLTN
    160 170 180 190 200
    GSFYFSLDFD ITTRLQLRTS QTMTEPQYDS MHTQFMWNEF MLRQLIKFRS
    210 220 230 240 250
    HLNGDEKSAL DGCRFFTCAI RGFASTEQFK LGIQTIRLSL ISRLSSLRAG
    260 270 280 290 300
    TRFLSRGVDD DGNVANFVET ETILDSSKYC VSYCQVRGSI PIFWEQEGVQ
    310 320 330 340 350
    MFGQKIDITR SLEATRAAFE KHFTSLIEEY GPVHIINLLG TGSGERSLSE
    360 370 380 390 400
    RLRQHIQLSP EKDLIHLTEF DYHSQIRSFE DANKIRPMIY SDAETFGFYF
    410 420 430 440 450
    ENNEGQSIVV QDGVFRTNCL DCLDRTNVIQ NLVSRVFLEQ VMIYTRQNAG
    460 470 480 490 500
    YDFWQVHSTI WANNGDALAR IYTGTGALKS SFTRKGKLSI AGALNDLSKS
    510 520 530 540 550
    VGRMYINNFQ DKGRQETIDL LLGRLIDQHP VILYDPIHEY VNHELRKREN
    560 570 580 590 600
    EFSEHKNVKI FVASYNLNGC SATTKLENWL FPENTPLADI YVVGFQEIVQ
    610 620 630 640 650
    LTPQQVISAD PAKRREWESC VKRLLNGKCT SGPGYVQLRS GQLVGTALMI
    660 670 680 690 700
    FCKESCLPSI KNVEGTVKKT GLGGVSGNKG AVAIRFDYED TGLCFITSHL
    710 720 730 740 750
    AAGYTNYDER DHDYRTIASG LRFRRGRSIF NHDYVVWFGD FNYRISLTYE
    760 770 780 790 800
    EVVPCIAQGK LSYLFEYDQL NKQMLTGKVF PFFSELPITF PPTYKFDIGT
    810 820 830 840 850
    DIYDTSDKHR VPAWTDRILY RGELVPHSYQ SVPLYYSDHR PIYATYEANI
    860 870 880 890 900
    VKVDREKKKI LFEELYNQRK QEVRDASQTS YTLIDIAGSV AGKPNLIPHL
    910 920 930 940 950
    PANGVDKIKQ PSSERSKWWF DDGLPAKSIA APPGPEYRLN PSRPINPFEP
    960 970 980 990 1000
    TAEPDWISNT KQSFDKKSSL IDSIPALSPA PSSLARSSVS SQRSSTSIIP
    1010 1020 1030 1040 1050
    IKPNKPTKPD HLVAPRVKPL LPPRSGSSSS GVPAPNLTPV NVPPTPPPRK
    1060 1070
    SSASQRSGDL LASSPEESSI SWKPLV
    Length:1,076
    Mass (Da):121,822
    Last modified:June 1, 1998 - v1
    Checksum:i5E26C9BF43AF20B8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CU329671 Genomic DNA. Translation: CAA17882.1.
    PIRiT40141.
    RefSeqiNP_596431.1. NM_001022350.2.

    Genome annotation databases

    EnsemblFungiiSPBC2G2.02.1; SPBC2G2.02.1:pep; SPBC2G2.02.
    GeneIDi2540270.
    KEGGispo:SPBC2G2.02.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CU329671 Genomic DNA. Translation: CAA17882.1.
    PIRiT40141.
    RefSeqiNP_596431.1. NM_001022350.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I9YX-ray2.00A534-880[»]
    1I9ZX-ray1.80A534-880[»]
    ProteinModelPortaliO43001.
    SMRiO43001. Positions 534-878.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi276801. 39 interactions.
    MINTiMINT-4674514.

    Proteomic databases

    MaxQBiO43001.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiSPBC2G2.02.1; SPBC2G2.02.1:pep; SPBC2G2.02.
    GeneIDi2540270.
    KEGGispo:SPBC2G2.02.

    Organism-specific databases

    EuPathDBiFungiDB:SPBC2G2.02.
    PomBaseiSPBC2G2.02. syj1.

    Phylogenomic databases

    HOGENOMiHOG000179717.
    InParanoidiO43001.
    OMAiGIMGIAG.
    OrthoDBiEOG7DRJBN.
    PhylomeDBiO43001.

    Enzyme and pathway databases

    ReactomeiR-SPO-1660499. Synthesis of PIPs at the plasma membrane.
    R-SPO-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
    R-SPO-1855204. Synthesis of IP3 and IP4 in the cytosol.
    SABIO-RKO43001.

    Miscellaneous databases

    EvolutionaryTraceiO43001.
    PROiO43001.

    Family and domain databases

    Gene3Di3.60.10.10. 1 hit.
    InterProiIPR005135. Endo/exonuclease/phosphatase.
    IPR000300. IPPc.
    IPR002013. SAC_dom.
    [Graphical view]
    PfamiPF03372. Exo_endo_phos. 1 hit.
    PF02383. Syja_N. 1 hit.
    [Graphical view]
    SMARTiSM00128. IPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56219. SSF56219. 1 hit.
    PROSITEiPS50275. SAC. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. "Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2."
      Chi Y., Zhou B., Wang W.-Q., Chung S.-K., Kwon Y.-U., Ahn Y.-H., Chang Y.-T., Tsujishita Y., Hurley J.H., Zhang Z.-Y.
      J. Biol. Chem. 279:44987-44995(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF GLU-597.
    3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
      Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
      Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    4. "Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-phosphatase."
      Tsujishita Y., Guo S., Stolz L.E., York J.D., Hurley J.H.
      Cell 105:379-389(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 534-880, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiSYJ1_SCHPO
    AccessioniPrimary (citable) accession number: O43001
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: June 1, 1998
    Last modified: June 8, 2016
    This is version 98 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.