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INP54_YEAST
ID   INP54_YEAST             Reviewed;         384 AA.
AC   Q08227; D6W202;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase INP54;
DE            EC=3.1.3.36 {ECO:0000269|PubMed:10660045};
GN   Name=INP54; OrderedLocusNames=YOL065C;
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=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., 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., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., 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   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   FUNCTION, AND CATALYTIC ACTIVITY.
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., Sheetz M.P.,
RA   Meyer T.;
RT   "Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that
RT   regulates cytoskeleton-plasma membrane adhesion.";
RL   Cell 100:221-228(2000).
RN   [4]
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 the
RT   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   [5]
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Regulates the phosphatidylinositol (4,5)-diphosphate levels
CC       on the cytoplasmic surface of the endoplasmic reticulum and thereby
CC       regulates secretion. Does not utilize phosphatidylinositol 3,5-
CC       bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate
CC       (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P).
CC       {ECO:0000269|PubMed:10660045, ECO:0000269|PubMed:11116155}.
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         Evidence={ECO:0000269|PubMed:10660045};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22765;
CC         Evidence={ECO:0000305|PubMed:10660045};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:11116155}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:11116155}; Cytoplasmic side
CC       {ECO:0000269|PubMed:11116155}.
CC   -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC       family. {ECO:0000305}.
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DR   EMBL; Z74807; CAA99075.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10718.1; -; Genomic_DNA.
DR   PIR; S66758; S66758.
DR   RefSeq; NP_014576.1; NM_001183320.1.
DR   AlphaFoldDB; Q08227; -.
DR   SMR; Q08227; -.
DR   BioGRID; 34336; 77.
DR   DIP; DIP-2768N; -.
DR   IntAct; Q08227; 5.
DR   MINT; Q08227; -.
DR   STRING; 4932.YOL065C; -.
DR   iPTMnet; Q08227; -.
DR   MaxQB; Q08227; -.
DR   PaxDb; Q08227; -.
DR   PRIDE; Q08227; -.
DR   TopDownProteomics; Q08227; -.
DR   EnsemblFungi; YOL065C_mRNA; YOL065C; YOL065C.
DR   GeneID; 854089; -.
DR   KEGG; sce:YOL065C; -.
DR   SGD; S000005426; INP54.
DR   VEuPathDB; FungiDB:YOL065C; -.
DR   eggNOG; KOG0565; Eukaryota.
DR   GeneTree; ENSGT00940000156762; -.
DR   HOGENOM; CLU_025224_2_0_1; -.
DR   InParanoid; Q08227; -.
DR   OMA; ITIWARC; -.
DR   BioCyc; YEAST:YOL065C-MON; -.
DR   Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane.
DR   Reactome; R-SCE-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR   Reactome; R-SCE-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-SCE-9013423; RAC3 GTPase cycle.
DR   PRO; PR:Q08227; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q08227; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:SGD.
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   Pfam; PF03372; Exo_endo_phos; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; SSF56219; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..384
FT                   /note="Phosphatidylinositol 4,5-bisphosphate 5-phosphatase
FT                   INP54"
FT                   /id="PRO_0000268682"
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
 
 
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