ID INP54_YEAST Reviewed; 384 AA. AC Q08227; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 46. DE RecName: Full=Inositol-1,4,5-trisphosphate 5-phosphatase 4; DE EC=3.1.3.36; GN Name=INP54; OrderedLocusNames=YOL065C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97313270; PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., RA Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., RA Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., RA Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., RA Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., RA Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., RA Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., RA Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., RA Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., RA Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., RA Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., RA Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., RA Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., RA Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., RA Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). RN [2] RP FUNCTION. RX PubMed=10660045; DOI=10.1016/S0092-8674(00)81560-3; RA Raucher D., Stauffer T., Chen W., Shen K., Guo S., York J.D., RA Sheetz M.P., Meyer T.; RT "Phosphatidylinositol 4,5-bisphosphate functions as a second messenger RT that regulates cytoskeleton-plasma membrane adhesion."; RL Cell 100:221-228(2000). RN [3] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11116155; DOI=10.1074/jbc.M010471200; RA Wiradjaja F., Ooms L.M., Whisstock J.C., McColl B.K., Helfenbaum L., RA Sambrook J.F., Gething M.J., Mitchell C.A.; RT "The yeast inositol polyphosphate 5-phosphatase Inp54p localizes to RT the endoplasmic reticulum via a C-terminal hydrophobic anchoring tail: RT regulation of secretion from the endoplasmic reticulum."; RL J. Biol. Chem. 276:7643-7653(2001). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220 AND SER-221, AND RP MASS SPECTROMETRY. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). CC -!- FUNCTION: Regulates the phosphatidylinositol (4,5)-diphosphate CC levels on the cytoplasmic surface of the endoplasmic reticulum and CC thereby regulates secretion. CC -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5- CC bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 4-phosphate CC + phosphate. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein; Cytoplasmic side. CC -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the inositol-1,4,5-trisphosphate 5- CC phosphatase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z74807; CAA99075.1; -; Genomic_DNA. DR PIR; S66758; S66758. DR RefSeq; NP_014576.1; -. DR HSSP; O43001; 1I9Z. DR DIP; DIP:2768N; -. DR IntAct; Q08227; 6. DR Ensembl; YOL065C; Saccharomyces cerevisiae. DR GeneID; 854089; -. DR GenomeReviews; Y13140_GR; YOL065C. DR KEGG; sce:YOL065C; -. DR NMPDR; fig|4932.3.peg.5668; -. DR CYGD; YOL065c; -. DR SGD; S000005426; INP54. DR HOGENOM; Q08227; -. DR OMA; Q08227; HLNANEG. DR BRENDA; 3.1.3.36; 250. DR NextBio; 975740; -. DR GermOnline; YOL065C; Saccharomyces cerevisiae. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-pho...; IDA:SGD. DR GO; GO:0046856; P:phosphoinositide dephosphorylation; IDA:SGD. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR InterPro; IPR000300; IPPc. DR Pfam; PF03372; Exo_endo_phos; 1. DR SMART; SM00128; IPPc; 1. PE 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; Hydrolase; Membrane; KW Phosphoprotein; Protein transport; Transport. FT CHAIN 1 384 Inositol-1,4,5-trisphosphate 5- FT phosphatase 4. FT /FTId=PRO_0000268682. FT MOD_RES 220 220 Phosphoserine. FT MOD_RES 221 221 Phosphoserine. SQ SEQUENCE 384 AA; 43799 MW; C77711D57C64B365 CRC64; MNKTNWKVSV TTFNCGKEFP VENSKAIVKQ LLFPYDDGIS QLELQDLYVL GFQEVVPIWQ GSFPAVNRDL IDRITTTAVN CLNEKVSATQ GDEQYSCLGV NSLGAITIIV LYNNNALKVK DDILKRNGKC GWFGTHLKGG TLISFQMTRN GEENWERFSY ICAHLNANEG VNNRNQRIDD YKRIMSEVCD SEVAKSDHFF FLGDLNFRVT STYDPTTNYS STTTLRRLLE NHEELNLLRK GEDEPLCKGF QELKITFPPT YKFKLFEKET YNTKRIPSWC DRILYKSYAV PTFAQEGTYH SVPRSNALLF SDHQPVNLTV RLPRSTGTPV PLSLHIEKYP LSWSSGLIGQ IGDAVIGYCG WLVTKNVHYW ILGSLLLYLL LKIL //