SYJ2_SCHPO
ID SYJ2_SCHPO Reviewed; 889 AA.
AC Q9USQ6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Inositol-1,4,5-trisphosphate 5-phosphatase 2;
DE EC=3.1.3.36;
DE AltName: Full=Synaptojanin-like protein 2;
GN Name=syj2; ORFNames=SPBC577.13;
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 INDUCTION.
RX PubMed=12529438; DOI=10.1091/mbc.e02-08-0499;
RA Chen D., Toone W.M., Mata J., Lyne R., Burns G., Kivinen K., Brazma A.,
RA Jones N., Baehler J.;
RT "Global transcriptional responses of fission yeast to environmental
RT stress.";
RL Mol. Biol. Cell 14:214-229(2003).
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: 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 (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: By stress. {ECO:0000269|PubMed:12529438}.
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; CAB54821.1; -; Genomic_DNA.
DR PIR; T40557; T40557.
DR RefSeq; NP_595311.1; NM_001021218.2.
DR AlphaFoldDB; Q9USQ6; -.
DR SMR; Q9USQ6; -.
DR BioGRID; 277613; 20.
DR STRING; 4896.SPBC577.13.1; -.
DR iPTMnet; Q9USQ6; -.
DR MaxQB; Q9USQ6; -.
DR PaxDb; Q9USQ6; -.
DR PRIDE; Q9USQ6; -.
DR EnsemblFungi; SPBC577.13.1; SPBC577.13.1:pep; SPBC577.13.
DR GeneID; 2541098; -.
DR KEGG; spo:SPBC577.13; -.
DR PomBase; SPBC577.13; syj2.
DR VEuPathDB; FungiDB:SPBC577.13; -.
DR eggNOG; KOG0566; Eukaryota.
DR HOGENOM; CLU_003016_2_1_1; -.
DR InParanoid; Q9USQ6; -.
DR OMA; FPYFHEM; -.
DR PhylomeDB; Q9USQ6; -.
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 PRO; PR:Q9USQ6; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; ISS:PomBase.
DR GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
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; ISO: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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Lipid metabolism; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..889
FT /note="Inositol-1,4,5-trisphosphate 5-phosphatase 2"
FT /id="PRO_0000359407"
FT DOMAIN 171..484
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
SQ SEQUENCE 889 AA; 101708 MW; A22120E274337F99 CRC64;
MQCYLKRKER SVAFITEKYA AIIQKPSVKD SDCIITFTCI SLEEFEKIKE YELLFGGEKI
LGTLGLFNYV CEDMKEGVFL CVARKAKLVL RIGNRDPISK LENVSFISLD QELWDEELFE
PMPRNSSPSS TFSTSTSDLN NIEKDNLVNS EYSSKYSSTT RIYPYHSLSQ LTDLLTDGSF
YVSTNISCFS RFQSEQPYGP KDIYCWNRFL ITELDNHFSE AHILEKFPNL LLHCFRGYVE
RMFIDSMSMS IISKVSSYGS RQTYPPSGID DSSYCSMFVE TEFIVEIAQT VFSFVQVRGT
VPCFWEEQFS SWYGPSISFL RSSQASQSLF NFHFSKLYKA YGDIYVIDLL QTKGFEASLY
EAYKHHLMLL PFPAVVKKFH FTPDPARPDI DPRLETDLAD DLKEMGYTQK SIENDMLESF
QKGVFRINDL DCLGRTNVIQ YQISRLVLKD IFFNLQIGVT FNILEYLRHL WSNNGDAIAK
LITGVGSIGS SATRRGRKSI AGSLSDISKS FGRMYVGRYP DVESQNAILL LLGCFPNQSP
VLISESVSSY IQGVLRQRRS EYRVERDFSI FSSTFNANGK VPSTDEFKRL LLPFGERTSA
YDLYVVAVQE IITLNMSHLV SSSNQKLRIW EEKILMILNS RDSNNKYMLI SSIQMAGVFL
GVFIRKDDHL VVSKVTKTTR KTGFGGFSAN KGAVAIEMNV CDSDFCFVSS HFAPKVNNIS
ERNMEYTSIS DNLVFPSGMK IYDHTNILWM GDFNYRIDSD NEEVRKLVEL DDLDKLASYD
QLCTEMKKGT VFHGLVEPQL TFLPTYKFDN GTNDYDTSDK QRVPSWTDRI LATKSFTRNC
YKSCDIRCSD HRPVFATFSL KIFSTCMDKK AGIIRDARIA YIKSKNSNK
