FIG4_SCHPO
ID FIG4_SCHPO Reviewed; 832 AA.
AC Q7Z9H9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Polyphosphoinositide phosphatase;
DE EC=3.1.3.-;
DE AltName: Full=Phosphatidylinositol 3,5-bisphosphate 5-phosphatase;
GN ORFNames=SPAC1093.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3-phosphate) + phosphate; Xref=Rhea:RHEA:32955,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57923,
CC ChEBI:CHEBI:58088;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
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DR EMBL; CU329670; CAB60248.4; -; Genomic_DNA.
DR RefSeq; NP_001018284.3; NM_001020079.3.
DR AlphaFoldDB; Q7Z9H9; -.
DR SMR; Q7Z9H9; -.
DR BioGRID; 280477; 39.
DR STRING; 4896.SPAC1093.03.1; -.
DR MaxQB; Q7Z9H9; -.
DR PaxDb; Q7Z9H9; -.
DR PRIDE; Q7Z9H9; -.
DR EnsemblFungi; SPAC1093.03.1; SPAC1093.03.1:pep; SPAC1093.03.
DR GeneID; 3361401; -.
DR KEGG; spo:SPAC1093.03; -.
DR PomBase; SPAC1093.03; -.
DR VEuPathDB; FungiDB:SPAC1093.03; -.
DR eggNOG; KOG1888; Eukaryota.
DR HOGENOM; CLU_003016_0_3_1; -.
DR InParanoid; Q7Z9H9; -.
DR OMA; TRTYWRV; -.
DR PRO; PR:Q7Z9H9; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0070772; C:PAS complex; ISO:PomBase.
DR GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; ISO:PomBase.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISO:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR InterPro; IPR043573; Fig4-like.
DR InterPro; IPR002013; SAC_dom.
DR PANTHER; PTHR45738; PTHR45738; 1.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS50275; SAC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Membrane; Reference proteome; Vacuole.
FT CHAIN 1..832
FT /note="Polyphosphoinositide phosphatase"
FT /id="PRO_0000317231"
FT DOMAIN 145..491
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
SQ SEQUENCE 832 AA; 96035 MW; 0F76CCC03DBFF43E CRC64;
MPATNSDEPL VKFELYQLKK CYYIVSENAT ATIFRILKIT QSEDELSISI EEAAKILFRQ
KLQLYLEKLE NESADGKLIL VTKAYAILGL FRFTAGYYLY LCTERKVVAV IGGHNVYHVD
KTQFIELNPS RRHNTSVERK CMSSIEKVDL ARTFYFSYSY DLSQTIQYGF THPIPQHQVR
DMFVWNWNML RPILDSVGID SPWCIPLIHG FVDQAKLSVY GKPIIVTLIA RRSRHFAGAR
FLRRGIRDDG YVANEVETEQ IVFDGSASSF PISSTTPGIP CYTSYVQHRG SIPLRWSQEF
SNITPKPPIG IDFHDPFYAS TALHFDRLFG HYGIPCIVLN LVKSSEKVKR ESLLLDEFES
AIQYLNQFLK DSQKIQYIAW DMSAASKKKV PVTKTLEQMA SDIVKKTGFF CTADRFFPGT
FQTGVVRTNC VDCLDRTNAA QFVIGKCVLA AQLRALGVLD SPQLDYESDA VRLLAEMYHG
HGDAIALQYG GSLLVNTLDT YRKNNQWSST SRDLIESVKR FYSNSFVDFQ RQEAISLFLG
NFTVHGKIVV FGEKRLQALT EKFKNGQLVR RDYRYWWTPV YVNQELRCKN AYCDSIQRKG
IKFPANYFDN VYTPNSISSF SEVLLPNLIS TLNFAPLSLI PLLRKSFLPL SYNGFGIEAP
SLNPFIPRRN QPRDMFKTSA EEENEDEDED DDKFRRVSLY KWLFNNEERP VHKFIRKRLH
QIPVSNKVQP RDQKQPDFKI PNTDINVYKI HFQYNNISGL ADNYTLLSKH DRAMYNNYAD
YSPDKIKEIK EKELNTYNDY FNSAISENPT LKSDRSEKVA FYSAWITDYK ST
