YMR1_SCHPO
ID YMR1_SCHPO Reviewed; 559 AA.
AC O13819;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Phosphoinositide 3-phosphatase;
DE EC=3.1.3.64;
GN ORFNames=SPAC19A8.03;
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 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: Lipid phosphatase which dephosphorylates phosphatidylinositol
CC 3-monophosphate (PI3P). Involved in the control of PI3P-dependent
CC signaling and in the maintenance of endosomal system integrity (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB11639.1; -; Genomic_DNA.
DR PIR; T37958; T37958.
DR RefSeq; NP_593789.1; NM_001019218.2.
DR AlphaFoldDB; O13819; -.
DR SMR; O13819; -.
DR BioGRID; 278980; 59.
DR STRING; 4896.SPAC19A8.03.1; -.
DR MaxQB; O13819; -.
DR PaxDb; O13819; -.
DR EnsemblFungi; SPAC19A8.03.1; SPAC19A8.03.1:pep; SPAC19A8.03.
DR GeneID; 2542522; -.
DR KEGG; spo:SPAC19A8.03; -.
DR PomBase; SPAC19A8.03; -.
DR VEuPathDB; FungiDB:SPAC19A8.03; -.
DR eggNOG; KOG1089; Eukaryota.
DR HOGENOM; CLU_001839_5_1_1; -.
DR InParanoid; O13819; -.
DR OMA; EKWFQIE; -.
DR PhylomeDB; O13819; -.
DR Reactome; R-SPO-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR Reactome; R-SPO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-SPO-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-SPO-1660517; Synthesis of PIPs at the late endosome membrane.
DR PRO; PR:O13819; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISO:PomBase.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; ISO:PomBase.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISO:PomBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..559
FT /note="Phosphoinositide 3-phosphatase"
FT /id="PRO_0000356185"
FT DOMAIN 120..541
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT ACT_SITE 342
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
SQ SEQUENCE 559 AA; 64153 MW; 521B7882E97E196E CRC64;
MENIKVAKVG NVKFVNKGNE LNGTLHLTAY HSIFSISENG KEIWTAYSMI NNVKLCSNEK
SFCIRIQCRD FMFFCWRFQS TEDAMDVYDT LQELMSINSI NMLYAFYYMP SGDEEKLPSS
WKSFLLENEY RRMGVGDSTQ ADGAGGNWRI TKINENYSEC HSYPQALAVP ASISDSVIYY
GCKYRSKNRF PTLTYLHKNS FSITRASQPL VGIRQNRSAQ DEKLVEAIFA TSIIPGKENL
IVDARPSTNA MANIAVGAGS ENMDHYRFAK KIYLGIDNIH VMRDSLNKIV NALKNTDISA
APPLIELLNR SSWLKHLANI LQGAVLIVKT VHFRHAHVLV HCSDGWDRTS QLCALPQLCL
DPYYRTIEGF FALVEKDWLS FGHRFAERCC HLPGKRIFTI DSSYSEEPPQ SSPSSTLQYT
FSTVRSALSG FSIDHSEKMM SPVFHQFLDC VWQIMDQFPN CFEFNERFLR RLLYHLYSCQ
YGSFLYNSER ERAQASVSTH TRCIWDYFLS RKDEFKNPNY VPYDDVIMPD PSSLRWWSAS
FAQPDENMNI PSPSESPSL
