ID   INP51_YEAST             Reviewed;         946 AA.
AC   P40559; D6VVS9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   04-NOV-2026, entry version 189.
DE   RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase INP51;
DE            EC=3.1.3.36;
DE   AltName: Full=Synaptojanin-like protein 1;
GN   Name=INP51; Synonyms=SJL1; OrderedLocusNames=YIL002C; ORFNames=YIA2C;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7762303; DOI=10.1002/yea.320110109;
RA   Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
RA   Schwager C., Zimmermann J., Sander C., Ansorge W.;
RT   "Nucleotide sequence and analysis of the centromeric region of yeast
RT   chromosome IX.";
RL   Yeast 11:61-78(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870; DOI=10.1038/387s084;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=9265642; DOI=10.1083/jcb.138.4.731;
RA   Luo W.-J., Chang A.;
RT   "Novel genes involved in endosomal traffic in yeast revealed by suppression
RT   of a targeting-defective plasma membrane ATPase mutant.";
RL   J. Cell Biol. 138:731-746(1997).
RN   [5]
RP   FUNCTION.
RX   PubMed=9560389; DOI=10.1093/genetics/148.4.1715;
RA   Stolz L.E., Huynh C.V., Thorner J., York J.D.;
RT   "Identification and characterization of an essential family of inositol
RT   polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the
RT   yeast Saccharomyces cerevisiae.";
RL   Genetics 148:1715-1729(1998).
RN   [6]
RP   FUNCTION.
RX   PubMed=9788876; DOI=10.1242/jcs.111.22.3347;
RA   Singer-Krueger B., Nemoto Y., Daniell L., Ferro-Novick S., De Camilli P.;
RT   "Synaptojanin family members are implicated in endocytic membrane traffic
RT   in yeast.";
RL   J. Cell Sci. 111:3347-3356(1998).
RN   [7]
RP   FUNCTION.
RX   PubMed=11311145; DOI=10.1042/bj3550805;
RA   O'Malley C.J., McColl B.K., Kong A.M., Ellis S.L., Wijayaratnam A.P.W.,
RA   Sambrook J., Mitchell C.A.;
RT   "Mammalian inositol polyphosphate 5-phosphatase II can compensate for the
RT   absence of all three yeast Sac1-like-domain-containing 5-phosphatases.";
RL   Biochem. J. 355:805-817(2001).
RN   [8]
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   [9]
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   [10]
RP   FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH IRS4 AND TAX4.
RX   PubMed=15265867; DOI=10.1074/jbc.m405589200;
RA   Morales-Johansson H., Jenoe P., Cooke F.T., Hall M.N.;
RT   "Negative regulation of phosphatidylinositol 4,5-bisphosphate levels by the
RT   INP51-associated proteins TAX4 and IRS4.";
RL   J. Biol. Chem. 279:39604-39610(2004).
RN   [11]
RP   FUNCTION.
RX   PubMed=15691741; DOI=10.1016/j.femsyr.2004.09.007;
RA   Nguyen P.H., Hasek J., Kohlwein S.D., Romero C., Choi J.H., Vancura A.;
RT   "Interaction of Pik1p and Sjl proteins in membrane trafficking.";
RL   FEMS Yeast Res. 5:363-371(2005).
RN   [12]
RP   FUNCTION.
RX   PubMed=15689497; DOI=10.1091/mbc.e04-07-0564;
RA   Fadri M., Daquinag A., Wang S., Xue T., Kunz J.;
RT   "The pleckstrin homology domain proteins Slm1 and Slm2 are required for
RT   actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-
RT   bisphosphate and TORC2.";
RL   Mol. Biol. Cell 16:1883-1900(2005).
RN   [13]
RP   FUNCTION.
RX   PubMed=17452534; DOI=10.1083/jcb.200611011;
RA   Sun Y., Carroll S., Kaksonen M., Toshima J.Y., Drubin D.G.;
RT   "PtdIns(4,5)P2 turnover is required for multiple stages during
RT   clathrin- and actin-dependent endocytic internalization.";
RL   J. Cell Biol. 177:355-367(2007).
CC   -!- FUNCTION: Controls the cellular levels and subcellular distribution of
CC       phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize
CC       phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor
CC       phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol
CC       4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi
CC       network)-to-early endosome pathway. Involved in endocytosis and acts as
CC       a negative regulator of the Slm pathway which modulates polarized actin
CC       assembly and growth. {ECO:0000269|PubMed:11311145,
CC       ECO:0000269|PubMed:15265867, ECO:0000269|PubMed:15689497,
CC       ECO:0000269|PubMed:15691741, ECO:0000269|PubMed:17452534,
CC       ECO:0000269|PubMed:9265642, ECO:0000269|PubMed:9560389,
CC       ECO:0000269|PubMed:9788876}.
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:0000255|PROSITE-
CC         ProRule:PRU01427};
CC   -!- ACTIVITY REGULATION: IRS4 and TAX4 are both positive regulator of INP51
CC       activity and phosphatidylinositol 4,5-bisphosphate turnover.
CC       {ECO:0000269|PubMed:15265867}.
CC   -!- SUBUNIT: Interacts with IRS4 and TAX4. {ECO:0000269|PubMed:15265867}.
CC   -!- INTERACTION:
CC       P40559; P36115: IRS4; NbExp=4; IntAct=EBI-24915, EBI-27090;
CC       P40559; P47030: TAX4; NbExp=3; IntAct=EBI-24915, EBI-25970;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 98 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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; X79743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z38062; CAA86201.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08545.1; -; Genomic_DNA.
DR   PIR; S48433; S48433.
DR   RefSeq; NP_012264.3; NM_001179352.3.
DR   AlphaFoldDB; P40559; -.
DR   SMR; P40559; -.
DR   BioGRID; 34990; 141.
DR   DIP; DIP-2677N; -.
DR   ELM; P40559; -.
DR   FunCoup; P40559; 55.
DR   IntAct; P40559; 19.
DR   STRING; 4932.YIL002C; -.
DR   iPTMnet; P40559; -.
DR   PaxDb; 4932-YIL002C; -.
DR   PeptideAtlas; P40559; -.
DR   EnsemblFungi; YIL002C_mRNA; YIL002C; YIL002C.
DR   GeneID; 854815; -.
DR   KEGG; sce:YIL002C; -.
DR   AGR; SGD:S000001264; -.
DR   SGD; S000001264; INP51.
DR   VEuPathDB; FungiDB:YIL002C; -.
DR   eggNOG; KOG0566; Eukaryota.
DR   HOGENOM; CLU_003016_2_1_1; -.
DR   InParanoid; P40559; -.
DR   OMA; AFPRWRM; -.
DR   OrthoDB; 405996at2759; -.
DR   BioCyc; YEAST:YIL002C-MONOMER; -.
DR   Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane.
DR   BioGRID-ORCS; 854815; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40559; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40559; protein.
DR   GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IDA:SGD.
DR   GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IBA:GO_Central.
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; IDA:SGD.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:SGD.
DR   CDD; cd09090; INPP5c_ScInp51p-like; 1.
DR   FunFam; 3.60.10.10:FF:000029; Inositol polyphosphate 5-phosphatase; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR046985; IP5.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR002013; SAC_dom.
DR   PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR   PANTHER; PTHR11200:SF269; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 5-PHOSPHATASE INP51; 1.
DR   Pfam; PF22669; Exo_endo_phos2; 1.
DR   Pfam; PF02383; Syja_N; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   PROSITE; PS52082; 5_PPASE; 1.
DR   PROSITE; PS50275; SAC; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; Lipid metabolism;
KW   Magnesium; Metal-binding; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..946
FT                   /note="Phosphatidylinositol 4,5-bisphosphate 5-phosphatase
FT                   INP51"
FT                   /id="PRO_0000209741"
FT   DOMAIN          151..480
FT                   /note="SAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT   DOMAIN          522..827
FT                   /note="5-PPase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01427"
FT   REGION          872..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          927..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..946
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        712
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01427"
FT   BINDING         570
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01427"
SQ   SEQUENCE   946 AA;  108430 MW;  A833C39B0A62543F CRC64;
     MRLFIGRRSR SIVISSNNYC LSFQRLRSIP GASSQQRQLS KTPSVTIKSY PDTDLSSDSN
     YLEVKSCIFN GLLGLVCLNG DIYVAVISGV QNVGFPRWKL IDHQVRPSES IYKVLDVDFY
     SLENDVFDYL LCERSEQNYD KLIHEHPCGP LKKLFSDGTF YYSRDFDISN IVKNHGLSHN
     LEYTVDNQDL SFIWNANLAS EVINWRSKIS NEEKQLFANA GFLTFVIRGY CKTALIEDGP
     NTASITIISR ISTESKQDTL ELEGISEDGR VSLFVETEIV VTTEKFIFSY TQVNGSIPLF
     WESVESQLLY GKKIKVTKDS IEAQGAFDRH FDNLTSKYGV VSIVNIIKPK SESQEKLALT
     YKDCAESKGI KITNIEYSSS VLTKSPHKLL YLLKQDIYEF GAFAYDISRG IYFAKQTGVL
     RISAFDSIEK PNTVERLVSK EVLELTTNEI DVFELTSPFL DAHDKLWSEN YYWLDRTYTK
     HTKNSGKYTK VYSKLFGSRV RLYDPLHIYI SQYLKQLRSK YTFEKDISIF AGTFNISGKI
     PKDDIKDWIF PKSMSKEDEM ADLYVIGLEE VVELTPGHML ATDPYVRQFW EKKILTLLNG
     PGRKKKYIRL WSTQLGGILL LLFMNETEYS KVKHIEGDVK KTGFGGMASN KGAVAVSFKY
     SATRFCVLVS HLAAGLENVE QRHNDYKTIA KSIRFSKGLR IKDHDAIIWM GDFNYRILMS
     NEDVRRKIVS KEYASLFEKD QLNQQMIAGE SFPYFHEMAI DFPPTYKFDP GTKNYDTSEK
     MRIPAWTDRI LSRGEVLEQL EYKCCEDILF SDHRPVYAIF RARVTVVDEQ KKTTLGTQIY
     EKIMERLEGL DDDEKIAVLS DDAFVIESFE GSDSIAGPTH SPTPIPEPKR GRKLPPPSSD
     LKKWWIGSGK QVKVVLDVDP AVYMINPKRD PNPFVENEDE PLFIER
//