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 03-AUG-2022, entry version 159.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:12752375};
DE AltName: Full=Phosphoinositide phospholipase C-epsilon-1;
DE AltName: Full=Phospholipase C-epsilon-1;
DE Short=PLC-epsilon-1;
GN Name=Plce1 {ECO:0000312|MGI:MGI:1921305}; Synonyms=Kiaa1516, Plce;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND
RP 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 expression
RT 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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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 project:
RT 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: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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>3.0.co;2-x;
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 for
RT 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., Kataoka T.;
RT "Crucial role of phospholipase Cepsilon in chemical carcinogen-induced skin
RT 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., Suzuki N.,
RA Saito H., Wu D., Masago-Toda M., Yamawaki-Kataoka Y., Setsu T.,
RA 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., Bunney T.D.,
RA Katan M., Liu J., Attanasio M., O'toole J.F., Hasselbacher K., Mucha B.,
RA Otto E.A., Airik R., Kispert A., Kelley G.G., Smrcka A.V., Gudermann T.,
RA Holzman L.B., Nuernberg P., Hildebrandt F.;
RT "Positional cloning uncovers mutations in PLCE1 responsible for a nephrotic
RT 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 BY
RP 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 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 mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes.
CC PLCE1 is a bifunctional enzyme which also regulates small GTPases of
CC the Ras superfamily through its Ras guanine-exchange factor (RasGEF)
CC activity. As an effector of heterotrimeric and small G-protein, it may
CC play a role in cell survival, cell growth, actin organization and T-
CC cell activation. In podocytes, is involved in the regulation of
CC lamellipodia formation. Acts downtream of AVIL to allow ARP2/3 complex
CC assembly (By similarity). {ECO:0000250|UniProtKB:Q9P212,
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 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC 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 subunits
CC GNA12, GNA13 and GNB1-GNG2. Activated by HRAS, RAP1A, RHOA, RHOB, RHOC,
CC RRAS and RRAS2. Activated by the G(s)-coupled GPCRs ADRB2, PTGER1 and
CC CHRM3 through cyclic-AMP formation and RAP2B activation. Inhibited by
CC G(i)-coupled GPCRs (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RHOA (By similarity). Interacts with IQGAP1,
CC HRAS, RAP1A, RAP2A, RAP2B and RRAS (By similarity). Interacts with
CC IQGAP1 (PubMed:17086182). Interacts with AVIL (By similarity).
CC {ECO:0000250|UniProtKB:Q99P84, ECO:0000250|UniProtKB:Q9P212,
CC ECO:0000269|PubMed:17086182}.
CC -!- INTERACTION:
CC Q8K4S1; E9Q401: Ryr2; NbExp=2; IntAct=EBI-6902760, EBI-643628;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9P212}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9P212}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9P212}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q9P212}. Note=Recruited to plasma membrane by
CC activated HRAS and RAP2. Recruited to perinuclear membrane by activated
CC RAP1A. Isoform 1 and isoform 2 associates with Golgi membranes.
CC {ECO:0000250|UniProtKB:Q9P212}.
CC -!- TISSUE SPECIFICITY: Highly expressed in neurons and to a lower extent
CC in skin, skeletal muscle and heart (at protein level). Expressed in the
CC epidermis. {ECO:0000269|PubMed:15604236, ECO:0000269|PubMed:15743817}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in cells committed to the
CC neuronal lineage (at protein level). Weakly expressed at 7 dpc,
CC expression strongly increases at later embryonic stages. Expressed
CC abundantly in almost all neural tissues at 12.5 dpc and also detected
CC in tongue muscles, genital tubercle and hand plate. At 15.5 dpc a
CC strong expression in skeletal muscles is detected together with the
CC strong expression in neural tissues. {ECO:0000269|PubMed:12752375}.
CC -!- INDUCTION: Up-regulated during the differentiation of neural precursor
CC cells into neurons but not glial cells. Up-regulated in heart upon
CC induced hypertrophy. {ECO:0000269|PubMed:12752375,
CC ECO:0000269|PubMed:16293787}.
CC -!- DOMAIN: The Ras-associating domain 1 is degenerated and may not bind
CC HRAS. The Ras-associating domain 2 mediates interaction with GTP-bound
CC HRAS, RAP1A, RAP2A and RAP2B and recruitment of HRAS to the cell
CC membrane (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The Ras-GEF domain has a GEF activity towards HRAS and RAP1A.
CC Mediates activation of the mitogen-activated protein kinase pathway (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit delayed onset and markedly reduced
CC incidence of chemically induced skin squamous tumors. They also display
CC cardiac malformations which mainly affects aortic and pulmonary valves
CC and enhanced susceptibility to cardiac hypertrophy and fibrosis in
CC response to chronic stress. {ECO:0000269|PubMed:15604236,
CC ECO:0000269|PubMed:15743817}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29099.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q8K4S1; -.
DR SMR; Q8K4S1; -.
DR BioGRID; 216456; 2.
DR DIP; DIP-60738N; -.
DR IntAct; Q8K4S1; 3.
DR STRING; 10090.ENSMUSP00000130604; -.
DR iPTMnet; Q8K4S1; -.
DR PhosphoSitePlus; Q8K4S1; -.
DR MaxQB; Q8K4S1; -.
DR PaxDb; Q8K4S1; -.
DR PRIDE; Q8K4S1; -.
DR ProteomicsDB; 289677; -.
DR Antibodypedia; 2889; 48 antibodies from 15 providers.
DR DNASU; 74055; -.
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 VEuPathDB; HostDB:ENSMUSG00000024998; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000157356; -.
DR InParanoid; Q8K4S1; -.
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 BioGRID-ORCS; 74055; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Plce1; mouse.
DR PRO; PR:Q8K4S1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K4S1; protein.
DR Bgee; ENSMUSG00000024998; Expressed in pigmented layer of retina and 227 other tissues.
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:0030027; C:lamellipodium; ISS:UniProtKB.
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:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; 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: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:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; 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 Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
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; IPR015359; PLC_EF-hand-like.
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; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10336; PTHR10336; 2.
DR PANTHER; PTHR10336:SF6; PTHR10336:SF6; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 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; SSF49562; SSF49562; 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; Cell projection; 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
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase epsilon-1"
FT /id="PRO_0000256239"
FT DOMAIN 528..781
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 1373..1521
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 1710..1826
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 1831..1956
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1992..2094
FT /note="Ras-associating 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 2115..2218
FT /note="Ras-associating 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 31..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1548..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1744
FT /note="Required for activation by RHOA, RHOB, GNA12, GNA13
FT and G-beta gamma"
FT /evidence="ECO:0000250"
FT REGION 2239..2282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 1433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 295
FT /note="N -> S (in Ref. 1; BAC00906 and 3; AAI38350/
FT AAI38351)"
FT /evidence="ECO:0000305"
FT CONFLICT 1798
FT /note="T -> A (in Ref. 6; AAF40208)"
FT /evidence="ECO:0000305"
FT CONFLICT 1829
FT /note="S -> N (in Ref. 6; AAF40208)"
FT /evidence="ECO:0000305"
FT CONFLICT 2215..2217
FT /note="LKE -> VKD (in Ref. 5; BAC29099)"
FT /evidence="ECO:0000305"
FT CONFLICT 2233
FT /note="A -> G (in Ref. 5; BAC29099)"
FT /evidence="ECO:0000305"
FT CONFLICT 2236
FT /note="L -> V (in Ref. 5; BAC29099)"
FT /evidence="ECO:0000305"
FT CONFLICT 2239
FT /note="L -> V (in Ref. 5; BAC29099)"
FT /evidence="ECO:0000305"
FT CONFLICT 2275
FT /note="S -> T (in Ref. 5; BAC29099)"
FT /evidence="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
