INP51_YEAST
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 03-AUG-2022, entry version 172.
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;
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 -!- 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=3; 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; 126.
DR DIP; DIP-2677N; -.
DR ELM; P40559; -.
DR IntAct; P40559; 9.
DR MINT; P40559; -.
DR STRING; 4932.YIL002C; -.
DR iPTMnet; P40559; -.
DR MaxQB; P40559; -.
DR PaxDb; P40559; -.
DR PRIDE; P40559; -.
DR EnsemblFungi; YIL002C_mRNA; YIL002C; YIL002C.
DR GeneID; 854815; -.
DR KEGG; sce:YIL002C; -.
DR SGD; S000001264; INP51.
DR VEuPathDB; FungiDB:YIL002C; -.
DR eggNOG; KOG0566; Eukaryota.
DR HOGENOM; CLU_003016_2_1_1; -.
DR InParanoid; P40559; -.
DR OMA; FPYFHEM; -.
DR BioCyc; YEAST:YIL002C-MON; -.
DR Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane.
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: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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:SGD.
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 Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; Lipid metabolism;
KW 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 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 932..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
