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UniProtKB/Swiss-Prot entry Q12271


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name INP53_YEAST
Primary accession number Q12271
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 53)
Name and origin of the protein
Protein name Inositol-1,4,5-trisphosphate 5-phosphatase 3
Synonyms EC 3.1.3.36
Synaptojanin-like protein 3
Suppressor of PMA1 protein 2
Gene name
Name: INP53
Synonyms: SJL3, SOP2
OrderedLocusNames: YOR109W
ORFNames: YOR3231w
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/(SICI)1097-0061(19970615)13:7<655::AID-YEA120>3.0.CO;2-I; PubMed=9200815 [NCBI, ExPASy, EBI, Israel, Japan]
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W.;
"DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
Yeast 13:655-672(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
FUNCTION.
DOI=10.1083/jcb.138.4.731; PubMed=9265642 [NCBI, ExPASy, EBI, Israel, Japan]
Luo W.-J., Chang A.;
"Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant.";
J. Cell Biol. 138:731-746(1997).
[4]
FUNCTION.
PubMed=9560389 [NCBI, ExPASy, EBI, Israel, Japan]
Stolz L.E., Huynh C.V., Thorner J., York J.D.;
"Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae.";
Genetics 148:1715-1729(1998).
[5]
FUNCTION.
PubMed=9788876 [NCBI, ExPASy, EBI, Israel, Japan]
Singer-Krueger B., Nemoto Y., Daniell L., Ferro-Novick S., De Camilli P.;
"Synaptojanin family members are implicated in endocytic membrane traffic in yeast.";
J. Cell Sci. 111:3347-3356(1998).
[6]
FUNCTION, AND DOMAIN.
DOI=10.1074/jbc.274.19.12990; PubMed=10224048 [NCBI, ExPASy, EBI, Israel, Japan]
Guo S., Stolz L.E., Lemrow S.M., York J.D.;
"SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases.";
J. Biol. Chem. 274:12990-12995(1999).
[7]
FUNCTION.
DOI=10.1002/(SICI)1097-0061(19990130)15:2<155::AID-YEA342>3.0.CO;2-U; PubMed=10029994 [NCBI, ExPASy, EBI, Israel, Japan]
Saiz J.E., de Los Angeles Santos M., Vazquez de Aldana C.R., Revuelta J.L.;
"Disruption of six unknown open reading frames from Saccharomyces cerevisiae reveals two genes involved in vacuolar morphogenesis and one gene required for sporulation.";
Yeast 15:155-164(1999).
[8]
FUNCTION.
PubMed=10628971 [NCBI, ExPASy, EBI, Israel, Japan]
Bensen E.S., Costaguta G., Payne G.S.;
"Synthetic genetic interactions with temperature-sensitive clathrin in Saccharomyces cerevisiae. Roles for synaptojanin-like Inp53p and dynamin-related Vps1p in clathrin-dependent protein sorting at the trans-Golgi network.";
Genetics 154:83-97(2000).
[9]
FUNCTION.
DOI=10.1074/jbc.275.2.801; PubMed=10625610 [NCBI, ExPASy, EBI, Israel, Japan]
Hughes W.E., Woscholski R., Cooke F.T., Patrick R.S., Dove S.K., McDonald N.Q., Parker P.J.;
"SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in which can be suppressed by the homologous Inp52p and Inp53p phosphatases.";
J. Biol. Chem. 275:801-808(2000).
[10]
FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
DOI=10.1128/MCB.20.24.9376-9390.2000; PubMed=11094088 [NCBI, ExPASy, EBI, Israel, Japan]
Ooms L.M., McColl B.K., Wiradjaja F., Wijayaratnam A.P.W., Gleeson P., Gething M.J., Sambrook J.F., Mitchell C.A.;
"The yeast inositol polyphosphate 5-phosphatases inp52p and inp53p translocate to actin patches following hyperosmotic stress: mechanism for regulating phosphatidylinositol 4,5-bisphosphate at plasma membrane invaginations.";
Mol. Cell. Biol. 20:9376-9390(2000).
[11]
FUNCTION.
PubMed=11598201 [NCBI, ExPASy, EBI, Israel, Japan]
Ha S.-A., Bunch J.T., Hama H., DeWald D.B., Nothwehr S.F.;
"A novel mechanism for localizing membrane proteins to yeast trans-Golgi network requires function of synaptojanin-like protein.";
Mol. Biol. Cell 12:3175-3190(2001).
[12]
INTERACTION WITH BSP1.
DOI=10.1016/S0014-5793(03)00067-X; PubMed=12606027 [NCBI, ExPASy, EBI, Israel, Japan]
Wicky S., Frischmuth S., Singer-Krueger B.;
"Bsp1p/Ypr171p is an adapter that directly links some synaptojanin family members to the cortical actin cytoskeleton in yeast.";
FEBS Lett. 537:35-41(2003).
[13]
FUNCTION, DOMAINS, MUTAGENESIS OF CYS-421; CYS-424; ARG-427; ASP-746 AND ASN-748, AND INTERACTION WITH CHC1.
DOI=10.1091/mbc.E02-10-0686; PubMed=12686590 [NCBI, ExPASy, EBI, Israel, Japan]
Ha S.-A., Torabinejad J., DeWald D.B., Wenk M.R., Lucast L., De Camilli P., Newitt R.A., Aebersold R., Nothwehr S.F.;
"The synaptojanin-like protein Inp53/Sjl3 functions with clathrin in a yeast TGN-to-endosome pathway distinct from the GGA protein-dependent pathway.";
Mol. Biol. Cell 14:1319-1333(2003).
[14]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[15]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[16]
FUNCTION.
DOI=10.1091/mbc.E04-03-0209; PubMed=15169871 [NCBI, ExPASy, EBI, Israel, Japan]
Parrish W.R., Stefan C.J., Emr S.D.;
"Essential role for the myotubularin-related phosphatase Ymr1p and the synaptojanin-like phosphatases Sjl2p and Sjl3p in regulation of phosphatidylinositol 3-phosphate in yeast.";
Mol. Biol. Cell 15:3567-3579(2004).
[17]
FUNCTION.
DOI=10.1016/j.femsyr.2004.09.007; PubMed=15691741 [NCBI, ExPASy, EBI, Israel, Japan]
Nguyen P.H., Hasek J., Kohlwein S.D., Romero C., Choi J.H., Vancura A.;
"Interaction of Pik1p and Sjl proteins in membrane trafficking.";
FEMS Yeast Res. 5:363-371(2005).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1105, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-986, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903; SER-932; SER-933; SER-934; SER-975; SER-986; THR-988; SER-1029; THR-1030; SER-1031; SER-1035; SER-1039 AND THR-1061, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
  • FUNCTION: Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in clathrin-mediated protein sorting at the TGN.
  • CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.
  • SUBUNIT: Interacts with BSP1 and CHC1.
  • SUBCELLULAR LOCATION: Cytoplasm. Note=Cytoplasmic punctate structures. Hyperosmotic stress causes translocation to actin patches.
  • DOMAIN: The SAC1 domain is capable of hydrolyzing phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2).
  • DOMAIN: The 5-phosphatase domain (residues 568 to 856) selectively removes the phosphate group at the 5' position of inositol of phosphatidylinositol 4,5-biphosphate (PtdIns(4,5)P2).
  • DOMAIN: The C-terminal proline-rich domain is required for the function and associates with clathrin heavy chain CHC1.
  • MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the synaptojanin family.
  • SIMILARITY: In the central section; belongs to the inositol-1,4,5-trisphosphate 5-phosphatase family.
  • SIMILARITY: Contains 1 SAC domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X94335; CAA64029.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75017; CAA99307.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61667; S61667.
RefSeq NP_014752.1; -.
3D structure databases
HSSP O43001; 1I9Z. [HSSP ENTRY / PDB]
ModBase Q12271.
Protein-protein interaction databases
DIP DIP:2555N; -.
IntAct Q12271; -.
Organism-specific databases
CYGD YOR109w; -.
SGD S000005635; INP53.
Yeast-GFP YOR109W.
Gene expression databases
ArrayExpress Q12271; -.
GermOnline YOR109W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0030479; Cellular component: actin cortical patch (inferred from direct assay from SGD).
GO:0042598; Cellular component: vesicular fraction (inferred from direct assay from SGD).
GO:0043813; Molecular function: phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity (inferred from direct assay from SGD).
GO:0004438; Molecular function: phosphatidylinositol-3-phosphatase activity (inferred from direct assay from SGD).
GO:0004439; Molecular function: phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity (inferred from electronic annotation from EC).
GO:0043812; Molecular function: phosphatidylinositol-4-phosphate phosphatase activity (inferred from direct assay from SGD).
GO:0006897; Biological process: endocytosis (inferred from electronic annotation from UniProtKB-KW).
GO:0046856; Biological process: phosphoinositide dephosphorylation (inferred from direct assay from SGD).
GO:0015031; Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR005135; Endo/exonuclease/phosphatase.
IPR000300; IPPc.
IPR002013; Syja_N.
Graphical view of domain structure.
Pfam PF03372; Exo_endo_phos; 1.
PF02383; Syja_N; 1.
Pfam graphical view of domain structure.
SMART SM00128; IPPc; 1.
SMART graphical view of domain structure.
PROSITE PS50275; SAC; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q12271.
Proteomic databases
PeptideAtlas Q12271; -.
Genome annotation databases
Ensembl YOR109W; Saccharomyces cerevisiae. [Contig view]
GeneID 854276; -.
GenomeReviews Y13140_GR; YOR109W.
KEGG sce:YOR109W; -.
NMPDR fig|4932.3.peg.5855; -.
Phylogenomic databases
HOGENOM Q12271; -.
Other
LinkHub Q12271; -.
NextBio 976236; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Endocytosis; Hydrolase; Phosphoprotein; Protein transport; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1107  1107     Inositol-1,4,5-trisphosphate 5-phosphatase 3. PRO_0000268681
DOMAIN   142    482  341     SAC. 
COMPBIAS   957    989  33     Pro-rich. 
MOD_RES   903    903        Phosphoserine. 
MOD_RES   932    932        Phosphoserine. 
MOD_RES   933    933        Phosphoserine. 
MOD_RES   934    934        Phosphoserine. 
MOD_RES   975    975        Phosphoserine. 
MOD_RES   986    986        Phosphoserine. 
MOD_RES   988    988        Phosphothreonine. 
MOD_RES   1029   1029        Phosphoserine. 
MOD_RES   1030   1030        Phosphothreonine. 
MOD_RES   1031   1031        Phosphoserine. 
MOD_RES   1035   1035        Phosphoserine. 
MOD_RES   1039   1039        Phosphoserine. 
MOD_RES   1061   1061        Phosphothreonine. 
MOD_RES   1105   1105        Phosphothreonine. 
MUTAGEN   421    421        C->A: Reduces hydrolysis of PtdIns(4)P; when associated with A-424 and A-427. 
MUTAGEN   424    424        C->A: Reduces hydrolysis of PtdIns(4)P; when associated with A-421 and A-427. 
MUTAGEN   427    427        R->A: Reduces hydrolysis of PtdIns(4)P; when associated with A-421 and A-424. 
MUTAGEN   746    746        D->A: Abolishes hydrolysis of PtdIns(4,5)P2; when associated with A-748. 
MUTAGEN   748    748        N->A: Abolishes hydrolysis of PtdIns(4,5)P2; when associated with A-746. 
Sequence information
Length: 1107 AA [This is the length of the unprocessed precursor] Molecular weight: 124577 Da [This is the MW of the unprocessed precursor] CRC64: 1E024F15085261EA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIIFVSEEPE RRLAIVSNLY ALVLKPVGKK PSDKPLCAIE LLQKNDLKKY GFKRLTSHEI 

        70         80         90        100        110        120 
FGVIGLIEVN GLLFVGAITG KSKVAQPCPG ETVNKIFAVD FFCLNDNSWD FIEIDSSGYP 

       130        140        150        160        170        180 
VLPETASTEY QDALPKHPCY ELKKLLSNGS FYYSSDFDLT STLQHRGYGQ HSLSTDTYEE 

       190        200        210        220        230        240 
EYMWNSFLMQ EMITYRDHLD TNLKQILDDE GFLTTVIRGF AETFVSYVKK LKVALTIISK 

       250        260        270        280        290        300 
QSWKRAGTRF NARGVDDEAN VANFVETEFI MYSSQYCYAF TQIRGSIPVF WEQGTSLINP 

       310        320        330        340        350        360 
RVQITRSFEA TQPVFDKHIM KSVEKYGPVH VVNLLSTKSS EIELSKRYKE HLTHSKKLNF 

       370        380        390        400        410        420 
NKDIFLTEFD FHKETSQEGF SGVRKLIPLI LDSLLSSGYY SYDVREKKNI SEQHGIFRTN 

       430        440        450        460        470        480 
CLDCLDRTNL AQQIISLAAF RTFLEDFRLI SSNSFIDDDD FVSKHNTLWA DHGDQISQIY 

       490        500        510        520        530        540 
TGTNALKSSF SRKGKMSLAG ALSDATKSVS RIYINNFMDK EKQQNIDTLL GRLPYQKAVQ 

       550        560        570        580        590        600 
LYDPVNEYVS TKLQSMSDKF TSTSNINLLI GSFNVNGATK KVDLSKWLFP IGEKFKPDIV 

       610        620        630        640        650        660 
VLGLQEVIEL SAGSILNADY SKSSFWENLV GDCLNQYDDK YLLLRVEQMT SLLILFFVKA 

       670        680        690        700        710        720 
DKAKYVKQVE GATKKTGFRG MAGNKGAVSI RFEYGATSFC FVNSHLAAGA TNVEERRSDY 

       730        740        750        760        770        780 
ESIVRGITFT RTKMIPHHDS IFWLGDMNYR INLPNEDVRR ELLNQEEGYI DKLLHFDQLT 

       790        800        810        820        830        840 
LGINSGSVFE GFKEPTLKFR PTYKYDPGTG TYDSSEKERT PSWTDRIIYK GENLLPLSYS 

       850        860        870        880        890        900 
DAPIMISDHR PVYAAYRAKI TFVDDKERLS LKKRLFTEYK QEHPEEPGSL ISDLLSLDLD 

       910        920        930        940        950        960 
NKSTDGFKSS SESSLLDIDP IMAQPTASSV ASSSPVSSAS ASLQPVRTQN SSQSRTPIKK 

       970        980        990       1000       1010       1020 
PVLRPPPPPA HKSVSAPAPS TSKEKSPTPQ TSTASLSSVT KNIQENKPLA QNRRIPPPGF 

      1030       1040       1050       1060       1070       1080 
SQNILTPKST SNLASPMSSK VDLYNSASES TRSAQDARQQ TPTAFAASRD VNGQPEALLG 

      1090       1100 
DENPIEPEEK AKLNHMTLDS WQPLTPK 

Q12271 in FASTA format

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