SYJ1_SCHPO
ID SYJ1_SCHPO Reviewed; 1076 AA.
AC O43001;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Inositol-1,4,5-trisphosphate 5-phosphatase 1;
DE EC=3.1.3.36;
DE AltName: Full=Synaptojanin-like protein 1;
GN Name=syj1; ORFNames=SPBC2G2.02;
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 FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND MUTAGENESIS OF
RP GLU-597.
RX PubMed=15316017; DOI=10.1074/jbc.m406416200;
RA Chi Y., Zhou B., Wang W.-Q., Chung S.-K., Kwon Y.-U., Ahn Y.-H.,
RA Chang Y.-T., Tsujishita Y., Hurley J.H., Zhang Z.-Y.;
RT "Comparative mechanistic and substrate specificity study of inositol
RT polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and
RT SHIP2.";
RL J. Biol. Chem. 279:44987-44995(2004).
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 534-880, AND CATALYTIC ACTIVITY.
RX PubMed=11348594; DOI=10.1016/s0092-8674(01)00326-9;
RA Tsujishita Y., Guo S., Stolz L.E., York J.D., Hurley J.H.;
RT "Specificity determinants in phosphoinositide dephosphorylation: crystal
RT structure of an archetypal inositol polyphosphate 5-phosphatase.";
RL Cell 105:379-389(2001).
CC -!- FUNCTION: Controls the cellular levels and subcellular distribution of
CC phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-
CC bisphosphate. Involved in distinct membrane trafficking and signal
CC transduction pathways. Highly active against a range of soluble and
CC lipid inositol phosphates. Active in dephosphorylating the 5-position
CC of Ins(1,4,5)P3 and Ins(1,3,4,5)P4 and to a lesser extent
CC Ins(1,4,5,6)P4. The enzyme is also active against PI(4,5)P2 presented
CC in sonicated vesicles and Triton mixed micelles, and somewhat less
CC active against PI(3,5)P2 in unilamellar vesicles. Activity against
CC PI(3,5)P2 drops sharply when this substrate is presented in mixed
CC micelles. Also hydrolyzes PIP3 to produce PI(3,4)P2.
CC {ECO:0000269|PubMed:15316017}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000269|PubMed:11348594};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15316017};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=57.8 uM for Ins(1,4,5)P3 (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15316017};
CC KM=10.9 uM for Ins(2,4,5)P3 (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15316017};
CC KM=75.9 uM for Ins(2,4)P2 (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15316017};
CC KM=5860 uM for p-nitrophenyl phosphate (at pH 7 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:15316017};
CC KM=182 uM for 3-O-methylfluorescein phosphate (at pH 7 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:15316017};
CC KM=530 uM for magnesium ions {ECO:0000269|PubMed:15316017};
CC KM=12 uM for manganese ions {ECO:0000269|PubMed:15316017};
CC KM=6.39 uM for nickel ions {ECO:0000269|PubMed:15316017};
CC KM=14.5 uM for cobalt ions {ECO:0000269|PubMed:15316017};
CC pH dependence:
CC Optimum pH is about 7.4. {ECO:0000269|PubMed:15316017};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Note=Localizes at the cell tip and the barrier septum.
CC -!- SIMILARITY: Belongs to the synaptojanin family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
CC trisphosphate 5-phosphatase family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17882.1; -; Genomic_DNA.
DR PIR; T40141; T40141.
DR RefSeq; NP_596431.1; NM_001022350.2.
DR PDB; 1I9Y; X-ray; 2.00 A; A=534-880.
DR PDB; 1I9Z; X-ray; 1.80 A; A=534-880.
DR PDBsum; 1I9Y; -.
DR PDBsum; 1I9Z; -.
DR AlphaFoldDB; O43001; -.
DR SMR; O43001; -.
DR BioGRID; 276801; 41.
DR STRING; 4896.SPBC2G2.02.1; -.
DR iPTMnet; O43001; -.
DR MaxQB; O43001; -.
DR PaxDb; O43001; -.
DR PRIDE; O43001; -.
DR EnsemblFungi; SPBC2G2.02.1; SPBC2G2.02.1:pep; SPBC2G2.02.
DR GeneID; 2540270; -.
DR KEGG; spo:SPBC2G2.02; -.
DR PomBase; SPBC2G2.02; syj1.
DR VEuPathDB; FungiDB:SPBC2G2.02; -.
DR eggNOG; KOG0566; Eukaryota.
DR HOGENOM; CLU_003016_2_1_1; -.
DR InParanoid; O43001; -.
DR OMA; EDMLWNS; -.
DR PhylomeDB; O43001; -.
DR Reactome; R-SPO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-SPO-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-SPO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR SABIO-RK; O43001; -.
DR EvolutionaryTrace; O43001; -.
DR PRO; PR:O43001; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:PomBase.
DR GO; GO:1990651; F:inositol-1,2,4,5,6-pentakisphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:1990649; F:inositol-1,2,4,5-tetrakisphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:1990650; F:inositol-2,4,5,6-tetrakisphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:1990640; F:inositol-2,4,5-triphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:1990648; F:inositol-4,5,6-triphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:0030487; F:inositol-4,5-bisphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:PomBase.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IC:PomBase.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR002013; SAC_dom.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF02383; Syja_N; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Lipid metabolism; Magnesium;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1076
FT /note="Inositol-1,4,5-trisphosphate 5-phosphatase 1"
FT /id="PRO_0000209736"
FT DOMAIN 144..474
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT REGION 534..880
FT /note="Catalytic"
FT REGION 930..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 597
FT /note="E->A,Q: Reduces the catalytic activity by 3 to 4
FT orders of magnitude."
FT /evidence="ECO:0000269|PubMed:15316017"
FT HELIX 536..547
FT /evidence="ECO:0007829|PDB:1I9Z"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 553..566
FT /evidence="ECO:0007829|PDB:1I9Z"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 589..596
FT /evidence="ECO:0007829|PDB:1I9Z"
FT HELIX 611..627
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 635..643
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 646..653
FT /evidence="ECO:0007829|PDB:1I9Z"
FT HELIX 654..659
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 660..669
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 680..688
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 691..699
FT /evidence="ECO:0007829|PDB:1I9Z"
FT HELIX 707..720
FT /evidence="ECO:0007829|PDB:1I9Z"
FT HELIX 724..726
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 731..740
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:1I9Z"
FT HELIX 749..757
FT /evidence="ECO:0007829|PDB:1I9Z"
FT HELIX 761..765
FT /evidence="ECO:0007829|PDB:1I9Z"
FT HELIX 769..775
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 778..780
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 816..823
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 825..831
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 836..839
FT /evidence="ECO:0007829|PDB:1I9Z"
FT STRAND 842..853
FT /evidence="ECO:0007829|PDB:1I9Z"
FT HELIX 855..876
FT /evidence="ECO:0007829|PDB:1I9Z"
SQ SEQUENCE 1076 AA; 121822 MW; 5E26C9BF43AF20B8 CRC64;
MQCLLREKPR SLALVNKDHA LMFHSVPQNK NSLSVCVAEF TALSEKPLEG FRKISSHRIY
GTLGLIELEG SNFLCVISGA SEVARVRDKE RVFRIMEVCF YSVNRSNWDH IRQENYSPDI
PDGYDTDTQG YDSYKYAAEP FSSLRKLLTN GSFYFSLDFD ITTRLQLRTS QTMTEPQYDS
MHTQFMWNEF MLRQLIKFRS HLNGDEKSAL DGCRFFTCAI RGFASTEQFK LGIQTIRLSL
ISRLSSLRAG TRFLSRGVDD DGNVANFVET ETILDSSKYC VSYCQVRGSI PIFWEQEGVQ
MFGQKIDITR SLEATRAAFE KHFTSLIEEY GPVHIINLLG TGSGERSLSE RLRQHIQLSP
EKDLIHLTEF DYHSQIRSFE DANKIRPMIY SDAETFGFYF ENNEGQSIVV QDGVFRTNCL
DCLDRTNVIQ NLVSRVFLEQ VMIYTRQNAG YDFWQVHSTI WANNGDALAR IYTGTGALKS
SFTRKGKLSI AGALNDLSKS VGRMYINNFQ DKGRQETIDL LLGRLIDQHP VILYDPIHEY
VNHELRKREN EFSEHKNVKI FVASYNLNGC SATTKLENWL FPENTPLADI YVVGFQEIVQ
LTPQQVISAD PAKRREWESC VKRLLNGKCT SGPGYVQLRS GQLVGTALMI FCKESCLPSI
KNVEGTVKKT GLGGVSGNKG AVAIRFDYED TGLCFITSHL AAGYTNYDER DHDYRTIASG
LRFRRGRSIF NHDYVVWFGD FNYRISLTYE EVVPCIAQGK LSYLFEYDQL NKQMLTGKVF
PFFSELPITF PPTYKFDIGT DIYDTSDKHR VPAWTDRILY RGELVPHSYQ SVPLYYSDHR
PIYATYEANI VKVDREKKKI LFEELYNQRK QEVRDASQTS YTLIDIAGSV AGKPNLIPHL
PANGVDKIKQ PSSERSKWWF DDGLPAKSIA APPGPEYRLN PSRPINPFEP TAEPDWISNT
KQSFDKKSSL IDSIPALSPA PSSLARSSVS SQRSSTSIIP IKPNKPTKPD HLVAPRVKPL
LPPRSGSSSS GVPAPNLTPV NVPPTPPPRK SSASQRSGDL LASSPEESSI SWKPLV
