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Database: UniProt
Entry: PLCE1_MOUSE
LinkDB: PLCE1_MOUSE
Original site: PLCE1_MOUSE 
ID   PLCE1_MOUSE             Reviewed;        2282 AA.
AC   Q8K4S1; B9EHS1; E9Q5G0; Q3TS68; Q80TC4; Q8BZF3; Q9JKM2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   08-MAY-2019, entry version 142.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1;
DE            EC=3.1.4.11;
DE   AltName: Full=Phosphoinositide phospholipase C-epsilon-1;
DE   AltName: Full=Phospholipase C-epsilon-1;
DE            Short=PLC-epsilon-1;
GN   Name=Plce1; Synonyms=Kiaa1516, Plce;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE,
RP   AND INDUCTION.
RC   TISSUE=Embryo;
RX   PubMed=12752375; DOI=10.1046/j.1460-9568.2003.02591.x;
RA   Wu D., Tadano M., Edamatsu H., Masago-Toda M., Yamawaki-Kataoka Y.,
RA   Terashima T., Mizoguchi A., Minami Y., Satoh T., Kataoka T.;
RT   "Neuronal lineage-specific induction of phospholipase Cepsilon
RT   expression in the developing mouse brain.";
RL   Eur. J. Neurosci. 17:1571-1580(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 919-2282.
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1166-2282.
RC   STRAIN=C57BL/6J; TISSUE=Egg, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1661-2282.
RX   PubMed=11146508;
RX   DOI=10.1002/1097-0177(2000)9999:9999<::AID-DVDY1089>3.3.CO;2-O;
RA   Tidhar A., Reichenstein M., Cohen D., Faerman A., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Shani M.;
RT   "A novel transgenic marker for migrating limb muscle precursors and
RT   for vascular smooth muscle cells.";
RL   Dev. Dyn. 220:60-73(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=12721365; DOI=10.1073/pnas.1031494100;
RA   Czyzyk J., Brogdon J.L., Badou A., Henegariu O., Preston Hurlburt P.,
RA   Flavell R., Bottomly K.;
RT   "Activation of CD4 T cells by Raf-independent effectors of Ras.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:6003-6008(2003).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15604236; DOI=10.1158/0008-5472.CAN-04-3143;
RA   Bai Y., Edamatsu H., Maeda S., Saito H., Suzuki N., Satoh T.,
RA   Kataoka T.;
RT   "Crucial role of phospholipase Cepsilon in chemical carcinogen-induced
RT   skin tumor development.";
RL   Cancer Res. 64:8808-8810(2004).
RN   [9]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=16293787; DOI=10.1161/01.RES.0000196578.15385.bb;
RA   Wang H., Oestreich E.A., Maekawa N., Bullard T.A., Vikstrom K.L.,
RA   Dirksen R.T., Kelley G.G., Blaxall B.C., Smrcka A.V.;
RT   "Phospholipase C epsilon modulates beta-adrenergic receptor-dependent
RT   cardiac contraction and inhibits cardiac hypertrophy.";
RL   Circ. Res. 97:1305-1313(2005).
RN   [10]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15743817; DOI=10.1128/MCB.25.6.2191-2199.2005;
RA   Tadano M., Edamatsu H., Minamisawa S., Yokoyama U., Ishikawa Y.,
RA   Suzuki N., Saito H., Wu D., Masago-Toda M., Yamawaki-Kataoka Y.,
RA   Setsu T., Terashima T., Maeda S., Satoh T., Kataoka T.;
RT   "Congenital semilunar valvulogenesis defect in mice deficient in
RT   phospholipase C epsilon.";
RL   Mol. Cell. Biol. 25:2191-2199(2005).
RN   [11]
RP   INTERACTION WITH IQGAP1.
RX   PubMed=17086182; DOI=10.1038/ng1918;
RA   Hinkes B., Wiggins R.C., Gbadegesin R., Vlangos C.N., Seelow D.,
RA   Nuernberg G., Garg P., Verma R., Chaib H., Hoskins B.E., Ashraf S.,
RA   Becker C., Hennies H.C., Goyal M., Wharram B.L., Schachter A.D.,
RA   Mudumana S., Drummond I., Kerjaschki D., Waldherr R., Dietrich A.,
RA   Ozaltin F., Bakkaloglu A., Cleper R., Basel-Vanagaite L., Pohl M.,
RA   Griebel M., Tsygin A.N., Soylu A., Mueller D., Sorli C.S.,
RA   Bunney T.D., Katan M., Liu J., Attanasio M., O'toole J.F.,
RA   Hasselbacher K., Mucha B., Otto E.A., Airik R., Kispert A.,
RA   Kelley G.G., Smrcka A.V., Gudermann T., Holzman L.B., Nuernberg P.,
RA   Hildebrandt F.;
RT   "Positional cloning uncovers mutations in PLCE1 responsible for a
RT   nephrotic syndrome variant that may be reversible.";
RL   Nat. Genet. 38:1397-1405(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1093, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: The production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is
CC       mediated by activated phosphatidylinositol-specific phospholipase
CC       C enzymes. PLCE1 is a bifunctional enzyme which also regulates
CC       small GTPases of the Ras superfamily through its Ras guanine-
CC       exchange factor (RasGEF) activity. As an effector of
CC       heterotrimeric and small G-protein, it may play a role in cell
CC       survival, cell growth, actin organization and T-cell activation.
CC       {ECO:0000269|PubMed:12721365, ECO:0000269|PubMed:15604236,
CC       ECO:0000269|PubMed:15743817, ECO:0000269|PubMed:16293787}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a
CC         1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11;
CC         Evidence={ECO:0000269|PubMed:12752375};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by the heterotrimeric G-protein
CC       subunits GNA12, GNA13 and GNB1-GNG2. Activated by HRAS, RAP1A,
CC       RHOA, RHOB, RHOC, RRAS and RRAS2. Activated by the G(s)-coupled
CC       GPCRs ADRB2, PTGER1 and CHRM3 through cyclic-AMP formation and
CC       RAP2B activation. Inhibited by G(i)-coupled GPCRs (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GTP-bound HRAS, RAP1A, RAP2A, RAP2B and
CC       RHOA (By similarity). Interacts with IQGAP1. {ECO:0000250,
CC       ECO:0000269|PubMed:17086182}.
CC   -!- INTERACTION:
CC       E9Q401:Ryr2; NbExp=2; IntAct=EBI-6902760, EBI-643628;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell
CC       membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}.
CC       Note=Recruited to plasma membrane by activated HRAS and RAP2.
CC       Recruited to perinuclear membrane by activated RAP1A. Associates
CC       with Golgi membranes (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in neurons and to a lower
CC       extent in skin, skeletal muscle and heart (at protein level).
CC       Expressed in the epidermis. {ECO:0000269|PubMed:15604236,
CC       ECO:0000269|PubMed:15743817}.
CC   -!- DEVELOPMENTAL STAGE: Specifically expressed in cells committed to
CC       the neuronal lineage (at protein level). Weakly expressed at 7
CC       dpc, expression strongly increases at later embryonic stages.
CC       Expressed abundantly in almost all neural tissues at 12.5 dpc and
CC       also detected in tongue muscles, genital tubercle and hand plate.
CC       At 15.5 dpc a strong expression in skeletal muscles is detected
CC       together with the strong expression in neural tissues.
CC       {ECO:0000269|PubMed:12752375}.
CC   -!- INDUCTION: Up-regulated during the differentiation of neural
CC       precursor cells into neurons but not glial cells. Up-regulated in
CC       heart upon induced hypertrophy. {ECO:0000269|PubMed:12752375,
CC       ECO:0000269|PubMed:16293787}.
CC   -!- DOMAIN: The Ras-associating domain 1 is degenerated and may not
CC       bind HRAS. The Ras-associating domain 2 mediates interaction with
CC       GTP-bound HRAS, RAP1A, RAP2A and RAP2B and recruitment of HRAS to
CC       the cell membrane (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The Ras-GEF domain has a GEF activity towards HRAS and
CC       RAP1A. Mediates activation of the mitogen-activated protein kinase
CC       pathway (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit delayed onset and markedly
CC       reduced incidence of chemically induced skin squamous tumors. They
CC       also display cardiac malformations which mainly affects aortic and
CC       pulmonary valves and enhanced susceptibility to cardiac
CC       hypertrophy and fibrosis in response to chronic stress.
CC       {ECO:0000269|PubMed:15604236, ECO:0000269|PubMed:15743817}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29099.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
DR   EMBL; AB076247; BAC00906.1; -; mRNA.
DR   EMBL; AC111023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC158905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC138349; AAI38350.1; -; mRNA.
DR   EMBL; BC138350; AAI38351.1; -; mRNA.
DR   EMBL; AK122521; BAC65803.1; -; mRNA.
DR   EMBL; AK035546; BAC29099.1; ALT_SEQ; mRNA.
DR   EMBL; AK162236; BAE36807.1; -; mRNA.
DR   EMBL; AF233885; AAF40208.1; -; mRNA.
DR   CCDS; CCDS37973.1; -.
DR   RefSeq; NP_062534.2; NM_019588.2.
DR   RefSeq; XP_011245682.1; XM_011247380.1.
DR   DIP; DIP-60738N; -.
DR   IntAct; Q8K4S1; 5.
DR   MINT; Q8K4S1; -.
DR   STRING; 10090.ENSMUSP00000130604; -.
DR   iPTMnet; Q8K4S1; -.
DR   PhosphoSitePlus; Q8K4S1; -.
DR   MaxQB; Q8K4S1; -.
DR   PaxDb; Q8K4S1; -.
DR   PRIDE; Q8K4S1; -.
DR   Ensembl; ENSMUST00000169713; ENSMUSP00000130604; ENSMUSG00000024998.
DR   Ensembl; ENSMUST00000182481; ENSMUSP00000138360; ENSMUSG00000024998.
DR   GeneID; 74055; -.
DR   KEGG; mmu:74055; -.
DR   UCSC; uc008hjp.1; mouse.
DR   CTD; 51196; -.
DR   MGI; MGI:1921305; Plce1.
DR   eggNOG; KOG0169; Eukaryota.
DR   eggNOG; ENOG410XPSW; LUCA.
DR   GeneTree; ENSGT00940000157356; -.
DR   InParanoid; Q8K4S1; -.
DR   KO; K05860; -.
DR   OrthoDB; 368239at2759; -.
DR   TreeFam; TF314432; -.
DR   BRENDA; 3.1.4.11; 3474.
DR   Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   PRO; PR:Q8K4S1; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000024998; Expressed in 261 organ(s), highest expression level in stria vascularis of cochlear duct.
DR   ExpressionAtlas; Q8K4S1; baseline and differential.
DR   Genevisible; Q8K4S1; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR   GO; GO:0004629; F:phospholipase C activity; ISS:UniProtKB.
DR   GO; GO:0017016; F:Ras GTPase binding; ISO:MGI.
DR   GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0032835; P:glomerulus development; ISO:MGI.
DR   GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007265; P:Ras protein signal transduction; ISO:MGI.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0046578; P:regulation of Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   Gene3D; 2.60.40.150; -; 1.
DR   Gene3D; 3.20.20.190; -; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR028398; PLC-epsilon1.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10336; PTHR10336; 1.
DR   PANTHER; PTHR10336:SF6; PTHR10336:SF6; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   SUPFAM; SSF51695; SSF51695; 1.
DR   SUPFAM; SSF54236; SSF54236; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Complete proteome; Cytoplasm; Golgi apparatus;
KW   Guanine-nucleotide releasing factor; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transducer.
FT   CHAIN         1   2282       1-phosphatidylinositol 4,5-bisphosphate
FT                                phosphodiesterase epsilon-1.
FT                                /FTId=PRO_0000256239.
FT   DOMAIN      528    781       Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00168}.
FT   DOMAIN     1373   1521       PI-PLC X-box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00270}.
FT   DOMAIN     1710   1826       PI-PLC Y-box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00271}.
FT   DOMAIN     1836   1936       C2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00041}.
FT   DOMAIN     1992   2094       Ras-associating 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00166}.
FT   DOMAIN     2115   2218       Ras-associating 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00166}.
FT   REGION     1667   1744       Required for activation by RHOA, RHOB,
FT                                GNA12, GNA13 and G-beta gamma.
FT                                {ECO:0000250}.
FT   ACT_SITE   1388   1388       {ECO:0000255|PROSITE-ProRule:PRU00270}.
FT   ACT_SITE   1433   1433       {ECO:0000255|PROSITE-ProRule:PRU00270}.
FT   MOD_RES    1093   1093       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CONFLICT    295    295       N -> S (in Ref. 1; BAC00906 and 3;
FT                                AAI38350/AAI38351). {ECO:0000305}.
FT   CONFLICT   1798   1798       T -> A (in Ref. 6; AAF40208).
FT                                {ECO:0000305}.
FT   CONFLICT   1829   1829       S -> N (in Ref. 6; AAF40208).
FT                                {ECO:0000305}.
FT   CONFLICT   2215   2217       LKE -> VKD (in Ref. 5; BAC29099).
FT                                {ECO:0000305}.
FT   CONFLICT   2233   2233       A -> G (in Ref. 5; BAC29099).
FT                                {ECO:0000305}.
FT   CONFLICT   2236   2236       L -> V (in Ref. 5; BAC29099).
FT                                {ECO:0000305}.
FT   CONFLICT   2239   2239       L -> V (in Ref. 5; BAC29099).
FT                                {ECO:0000305}.
FT   CONFLICT   2275   2275       S -> T (in Ref. 5; BAC29099).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2282 AA;  255047 MW;  AA288A76304E43ED CRC64;
     MTSEEMAASV LIPVTQRKVA SAQSVAEERS VKVSDAGIPR ARAGRQGALI PPTISQWNKH
     KEESSRSDLS KVFSIARGEL VCDENSNEEG WEENAPDSPE NHAMNGNSLV QSHQHQFPRS
     QLCEARDSVT EDPCLQPGIP SPLERKVLPG IQLEMEDSPM DVSPAGSQPR IMESSGPHSD
     RNTAVFHFHY EADRTMSDAF HTLSENLILD DCANCVTLPG GQQNKNCMAY ACKLVELTRT
     CGSKNGQVQC EHCTSLRDEY LCFESSCSKA DEVCSGGGFC EDGFAHGPAA KTFLNPLEDF
     SDNCEDVDDF FKSKKERSTL LVRRFCKNDR EVKKSVYTGT RAIMRTLPSG CIGPAAWNYV
     DQKKAGLLWP CGNVMGTLSA MDIRQSGSQR LSEAQWCLIY SAVRRGEEIE DTVGSLLHCS
     TQLPNSETAH GRIEDGPCLK QCVRDTECEF RATLQRTSIA QYITGSLLEA TTSLGARSGL
     LSSFGGSTGR IMLKERQLGT SMANSNPVPS SSAGISKELI DLQPLIQFPE EVASILTEQE
     QNIYRRVLPM DYLCFLTRDL SSPECQRSLP RLKASISESI LTSQSGEHNA LEDLVMRFNE
     VSSWVTWLIL TAGSMEEKRE VFSYLVHVAK CCWNMGNYNA VMEFLAGLRS RKVLKMWQFM
     DQSDIETMRS LKDAMAQHES SVEYKKVVTR ALHIPGCKVV PFCGVFLKEL CEVLDGASGL
     LKLCPRYSSQ EEALEFVADY SGQDNFLQRV GQNGLKNSEK ELTVNSIFQV IRSCSRSLEM
     EEEDSASEGS GSRKNSLKDK ARWQFIIGDL LDSENDIFEK SKECDPHGSE ESQKAFDHGT
     ELIPWYVLSI QADVHQFLLQ GATVIHYDQD THLSARCFLQ LQPDNSTLTW MKPPTASPAG
     ARPKLGVLSN MAEPGKFPSP GNAGVSGLAE GILDLFSVKA VYMGHPGIDI HTVCVQNKLS
     SMLLSETGVT LLYGLQTTDN RLLHFVAPKH TAEMLFSGLL ELTTAVRKIR RFPDQRQQWL
     RKQYVSLYQE DGRYEGPTLA HAVELFGGRR WSTRNPSPGM SAKNAEKPNM QRNNTLGIST
     TKKKKKMLMR GESGEVTDDE MATRKAKMYR ECRSRSGSDP QDVNEQEESE ANVITNPPNP
     LHSRRAYSLT TAGSPNLATG MSSPISAWSS SSWHGRIRGG MQGFQSFMVS DSNMSFVEFV
     ELFKSFSIRS RKDLKDIFDI YSVPCNRSAS ESAPLYTNLT IEENTSDLQP DLDLLTRNVS
     DLGLFIKSKQ QLSDNQRQIS DAIAAASIVT NGTGIESTSL GIFGVGILQL NDFLVNCQGE
     HCTYDEILSI IQKFEPSVSM CHQGLLSFEG FARFLMDKDN FASKNDESRE NKKELQLPLS
     YYYIESSHNT YLTGHQLKGE SSVELYSQVL LQGCRSIELD CWDGDDGMPI IYHGHTLTTK
     IPFKEVVEAI DRSAFITSDL PIIISIENHC SLPQQRKMAE IFKSVFGEKL VAKFLFETDF
     SDDPMLPSPD QLRRKVLLKN KKLKAHQTPV DILKQKAHQL ASMQAQAFTG GNANPPPASN
     EEEEDEEDEY DYDYESLSDD NILEDRPENK SCADKLQFEY NEEVPKRIKK ADNSSGNKGK
     VYDMELGEEF YLPQNKKESR QIAPELSDLV IYCQAVKFPG LSTLNSSGSS RGKERKSRKS
     IFGNNPGRMS PGETAPFNRT SGKGSCEGMR HTWEESSPLS PSTSLSAIIR TPKCYHISSL
     NENAAKRLCR RGSQKLIQHT AYQLLRTYPA ATRIDSSNPN PIMFWLHGIQ LVALNYQTDD
     LPLHLNAAMF EANGGCGYVL KPPVLWDKSC PMYQKFSPLE RDLDNLDPAI YSLTIISGQN
     VCPSNSTGSP CIEVDVLGMP LDSCHFRTKP IHRNTLNPMW NEQFLFRVHF EDLVFLRFAV
     VENNSSAITA QRIIPLRALK RGYRHLQLRN LHNEILEISS LFINSRRMEE NPSGSSMPAS
     LMFNTEERKC SQTHKVTVHG VPGPEPFAVF TINEGTKAKQ LLQQVLAVDQ DTKCTATDYF
     LMEEKHFISK EKNECRKQPF QRAVGPEEDI VQILNSWFPE EGYVGRIVLK PQQETLEEKS
     IVFDDKEVIL SSEEESFFVQ VHDVSPEQPR TVIKAPRVST AQDVIQQTLC KAKYSYSILN
     NPNPCDYVLL EEVLKDAANK KSSTPKSSQR ILLDQECVFQ AQSKWKGAGK FILKLKEQVQ
     ASREDKRRGI SFASELKKLT KSTKQSRGLP SPPQLVASES VQSKEEKPVG ALSSSDTVGY
     QQ
//
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