SIW14_YEAST
ID SIW14_YEAST Reviewed; 281 AA.
AC P53965; D6W1E7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Inositol phosphatase SIW14 {ECO:0000303|PubMed:30548067};
DE EC=3.6.1.52;
DE AltName: Full=5-PP-InsP phosphatase {ECO:0000303|PubMed:29540476};
DE AltName: Full=Inositol pyrophosphate phosphatase SIW14 {ECO:0000303|PubMed:26828065};
DE AltName: Full=Oxidant-induced cell-cycle arrest protein 3;
DE AltName: Full=Synthetic interaction with WHI2 protein 14;
GN Name=SIW14; Synonyms=OCA3;
GN OrderedLocusNames=YNL032W {ECO:0000312|SGD:S000004977}; ORFNames=N2746;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION.
RX PubMed=15020461; DOI=10.1534/genetics.166.2.707;
RA Care A., Vousden K.A., Binley K.M., Radcliffe P., Trevethick J.,
RA Mannazzu I., Sudbery P.E.;
RT "A synthetic lethal screen identifies a role for the cortical actin
RT patch/endocytosis complex in the response to nutrient deprivation in
RT Saccharomyces cerevisiae.";
RL Genetics 166:707-719(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=21409566; DOI=10.1007/s00438-011-0611-6;
RA Roma-Mateo C., Sacristan-Reviriego A., Beresford N.J.,
RA Caparros-Martin J.A., Culianez-Macia F.A., Martin H., Molina M.,
RA Tabernero L., Pulido R.;
RT "Phylogenetic and genetic linkage between novel atypical dual-specificity
RT phosphatases from non-metazoan organisms.";
RL Mol. Genet. Genomics 285:341-354(2011).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-214.
RX PubMed=26828065; DOI=10.1074/jbc.m116.714907;
RA Steidle E.A., Chong L.S., Wu M., Crooke E., Fiedler D., Resnick A.C.,
RA Rolfes R.J.;
RT "A novel inositol pyrophosphate phosphatase in Saccharomyces cerevisiae:
RT Siw14 protein selectively cleaves the beta-phosphate from 5-
RT diphosphoinositol pentakisphosphate (5pp-ip5).";
RL J. Biol. Chem. 291:6772-6783(2016).
RN [10]
RP FUNCTION IN PRION SUPPRESSION.
RX PubMed=28923943; DOI=10.1073/pnas.1714361114;
RA Wickner R.B., Kelly A.C., Bezsonov E.E., Edskes H.K.;
RT "[PSI+] prion propagation is controlled by inositol polyphosphates.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E8402-E8410(2017).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 116-281, SUBUNIT, AND MUTAGENESIS
RP OF CYS-214 AND ARG-220.
RX PubMed=29540476; DOI=10.1074/jbc.ra117.001670;
RA Wang H., Gu C., Rolfes R.J., Jessen H.J., Shears S.B.;
RT "Structural and biochemical characterization of Siw14: A protein-tyrosine
RT phosphatase fold that metabolizes inositol pyrophosphates.";
RL J. Biol. Chem. 293:6905-6914(2018).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 113-281.
RX PubMed=30548067; DOI=10.1021/acs.biochem.8b01044;
RA Florio T.J., Lokareddy R.K., Gillilan R.E., Cingolani G.;
RT "Molecular architecture of the inositol phosphatase Siw14.";
RL Biochemistry 58:534-545(2019).
CC -!- FUNCTION: Selectively cleaves the beta-phosphate at the 5-position of
CC soluble inositol pyrophosphates. Converts 5-diphosphoinositol
CC tetrakisphosphate (5-PP-InsP(4)) into inositol pentakisphosphate
CC (InsP(5)), 5-diphosphoinositol pentakisphosphate (5-PP-IP(5) or 5-
CC InsP(7)) into inositol hexakisphosphate (IP(6) or InsP(6)), and 1,5-
CC bisdiphosphoinositol tetrakisphosphate (1,5-PP-IP(5) or InsP(8)) into
CC 1-diphosphoinositol pentakisphosphate (1-PP-IP(5) or 1-InsP(7))
CC (PubMed:26828065, PubMed:29540476). Modulates inositol pyrophosphate
CC metabolism that may have an influence in stress response
CC (PubMed:26828065). Plays a role in actin filament organization and
CC endocytosis (PubMed:15020461). Functions as a prion suppressing factor
CC possibly due to its phosphatase activity against inositol
CC pyrophosphates, which are signal transduction molecules involved in
CC prion propagation (PubMed:28923943). {ECO:0000269|PubMed:15020461,
CC ECO:0000269|PubMed:26828065, ECO:0000269|PubMed:28923943,
CC ECO:0000269|PubMed:29540476}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + H2O
CC = 1D-myo-inositol hexakisphosphate + H(+) + phosphate;
CC Xref=Rhea:RHEA:22384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628; EC=3.6.1.52;
CC Evidence={ECO:0000269|PubMed:26828065, ECO:0000269|PubMed:29540476};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-diphospho-1D-myo-inositol 1,3,4,6-tetrakisphosphate + H2O =
CC 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H(+) + phosphate;
CC Xref=Rhea:RHEA:59500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57733, ChEBI:CHEBI:142939;
CC EC=3.6.1.52; Evidence={ECO:0000269|PubMed:29540476};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,5-bis(diphospho)-1D-myo-inositol 1,2,4,6-tetrakisphosphate +
CC H2O = 3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 2
CC H(+) + phosphate; Xref=Rhea:RHEA:56312, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:140372,
CC ChEBI:CHEBI:140374; EC=3.6.1.52;
CC Evidence={ECO:0000269|PubMed:29540476};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 uM for 5-diphosphoinositol pentakisphosphate
CC {ECO:0000269|PubMed:26828065};
CC KM=10.4 uM for 5-diphosphoinositol pentakisphosphate
CC {ECO:0000269|PubMed:29540476};
CC KM=56.8 uM for 5-diphosphoinositol tetrakisphosphate
CC {ECO:0000269|PubMed:29540476};
CC KM=10.1 uM for 1,5-bisdiphosphoinositol tetrakisphosphate
CC {ECO:0000269|PubMed:29540476};
CC Note=kcat is 0.0025 sec(-1) with 5-diphosphoinositol
CC pentakisphosphate as substrate (PubMed:26828065). kcat is 1.31 sec(-
CC 1) with 5-diphosphoinositol pentakisphosphate as substrate, 0.77
CC sec(-1) with 5-diphosphoinositol tetrakisphosphate as substrate, and
CC 0.63 sec(-1) with 1,5-bisdiphosphoinositol tetrakisphosphate as
CC substrate (PubMed:29540476). {ECO:0000269|PubMed:26828065,
CC ECO:0000269|PubMed:29540476};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:26828065};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:26828065};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:29540476}.
CC -!- INTERACTION:
CC P53965; P50946: OCA1; NbExp=4; IntAct=EBI-28668, EBI-28814;
CC P53965; P53949: OCA2; NbExp=3; IntAct=EBI-28668, EBI-28725;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 4070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z71308; CAA95895.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10513.1; -; Genomic_DNA.
DR PIR; S62954; S62954.
DR RefSeq; NP_014366.3; NM_001182871.3.
DR PDB; 6BYF; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I=116-281.
DR PDB; 6E3B; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W/X/Y=113-281.
DR PDBsum; 6BYF; -.
DR PDBsum; 6E3B; -.
DR AlphaFoldDB; P53965; -.
DR SMR; P53965; -.
DR BioGRID; 35795; 454.
DR DIP; DIP-1990N; -.
DR IntAct; P53965; 30.
DR MINT; P53965; -.
DR STRING; 4932.YNL032W; -.
DR iPTMnet; P53965; -.
DR MaxQB; P53965; -.
DR PaxDb; P53965; -.
DR PRIDE; P53965; -.
DR EnsemblFungi; YNL032W_mRNA; YNL032W; YNL032W.
DR GeneID; 855699; -.
DR KEGG; sce:YNL032W; -.
DR SGD; S000004977; SIW14.
DR VEuPathDB; FungiDB:YNL032W; -.
DR eggNOG; KOG1572; Eukaryota.
DR GeneTree; ENSGT00940000176301; -.
DR HOGENOM; CLU_047845_1_0_1; -.
DR InParanoid; P53965; -.
DR OMA; DDPFQMD; -.
DR BioCyc; MetaCyc:G3O-33069-MON; -.
DR BioCyc; YEAST:G3O-33069-MON; -.
DR BRENDA; 3.1.3.48; 984.
DR PRO; PR:P53965; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53965; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; IBA:GO_Central.
DR GO; GO:0052847; F:inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity; IDA:SGD.
DR GO; GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IDA:SGD.
DR GO; GO:0106211; F:inositol-5-diphosphate-1,3,4,6-tetrakisphosphate diphosphatase activity; IDA:SGD.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0007015; P:actin filament organization; IMP:SGD.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020428; PFA-DSPs.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR004861; Siw14-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF03162; Y_phosphatase2; 1.
DR PRINTS; PR01911; PFDSPHPHTASE.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..281
FT /note="Inositol phosphatase SIW14"
FT /id="PRO_0000094922"
FT DOMAIN 121..271
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 214
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000305|PubMed:29540476"
FT SITE 220
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:29540476"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 214
FT /note="C->S: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26828065,
FT ECO:0000269|PubMed:29540476"
FT MUTAGEN 220
FT /note="R->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29540476"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6BYF"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:6BYF"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6BYF"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:6BYF"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6BYF"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6BYF"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:6BYF"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:6BYF"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6E3B"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:6BYF"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6BYF"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:6BYF"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:6BYF"
FT HELIX 220..231
FT /evidence="ECO:0007829|PDB:6BYF"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:6BYF"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:6BYF"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:6BYF"
SQ SEQUENCE 281 AA; 32755 MW; 88BD8AFC620B4570 CRC64;
MGLYQAKNDE GSDPKSSSKI DDLIENEAEI IRLIKEDGKL LIDNGDGRDI HNIIQEDKLL
SVEFNEVLKR FHGEEKSDIP RKEFDEDEDD GYDSNEHHQK TIEVMNTLNH VINKEVIPPE
NFSHVVGEIY RSSFPRQENF SFLHERLKLK SILVLIPEEY PQENLNFLKL TGIKLYQVGM
SGNKEPFVNI PSHLLTKALE IVLNPANQPI LIHCNRGKHR TGCLIGCIRK LQNWSLTMIF
DEYRRFAFPK ARALDQQFIE MYDDDEIKRI ASKNNWLPLQ W
