Reviewed, UniProtKB/Swiss-Prot Q8K4S1 (PLCE1_MOUSE)

Names and origin

Protein names

Recommended name:
    1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
    EC=3.1.4.11
Alternative name(s):
    Phosphoinositide phospholipase C-epsilon-1
    Phospholipase C-epsilon-1
      Short name=PLC-epsilon-1

Gene names

Name:	Plce1
Synonyms:	Kiaa1516, Plce

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	2282 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine-exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation. Ref.6 Ref.7 Ref.8 Ref.9
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. Ref.1
Cofactor	Calcium By similarity.
Enzyme regulation	Activated by the heterotrimeric G-protein subunits GNA12, GNA13 and GNB1-GNG2. Activated by HRAS, RAP1A, RHOA, RHOB, RHOC, RRAS and RRAS2. Activated by the G(s)-coupled GPCRs ADRB2, PTGER1 and CHRM3 through cyclic-AMP formation and RAP2B activation. Inhibited by G(i)-coupled GPCRs By similarity.
Subunit structure	Interacts with GTP-bound HRAS, RAP1A, RAP2A, RAP2B and RHOA By similarity. Interacts with IQGAP1. Ref.10
Subcellular location	Cytoplasm › cytosol By similarity. Cell membrane By similarity. Golgi apparatus membrane By similarity. Note: Recruited to plasma membrane by activated HRAS and RAP2. Recruited to perinuclear membrane by activated RAP1A. Associates with Golgi membranes By similarity.
Tissue specificity	Highly expressed in neurons and to a lower extent in skin, skeletal muscle and heart (at protein level). Expressed in the epidermis. Ref.7 Ref.9
Developmental stage	Specifically expressed in cells committed to the neuronal lineage (at protein level). Weakly expressed at E7, expression strongly increases at later embryonic stages. Expressed abundantly in almost all neural tissues at E12.5 and also detected in tongue muscles, genital tubercle and hand plate. At E15.5 a strong expression in skeletal muscles is detected together with the strong expression in neural tissues. Ref.1
Induction	Up-regulated during the differentiation of neural precursor cells into neurons and not glial cells. Up-regulated in heart upon induced hypertrophy. Ref.8 Ref.1
Domain	The Ras-associating domain 1 is degenerated and may not bind HRAS. The Ras-associating domain 2 mediates interaction with GTP-bound HRAS, RAP1A, RAP2A and RAP2B and recruitment of HRAS to the cell membrane By similarity. The Ras-GEF domain has a GEF activity towards HRAS and RAP1A. Mediates activation of the mitogen-activated protein kinase pathway By similarity.
Disruption phenotype	Mice exhibit delayed onset and markedly reduced incidence of chemically induced skin squamous tumors. They also display cardiac malformations which mainly affects aortic and pulmonary valves and enhanced susceptibility to cardiac hypertrophy and fibrosis in response to chronic stress. Ref.7 Ref.9
Sequence similarities	Contains 1 C2 domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain. Contains 2 Ras-associating domains. Contains 1 Ras-GEF domain.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cell membrane Cytoplasm Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Guanine-nucleotide releasing factor Hydrolase Transducer
Gene Ontology (GO)
Biological process	activation of MAPK activity Inferred from sequence or structural similarity. Source: UniProtKB activation of phospholipase C activity by G-protein coupled receptor protein signaling pathway coupled to IP3 second messenger Inferred from sequence or structural similarity. Source: UniProtKB lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of G-protein coupled receptor protein signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB regulation of Ras protein signal transduction Inferred from sequence or structural similarity. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from sequence or structural similarity. Source: UniProtKB membrane fraction Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro enzyme binding Inferred from sequence or structural similarity. Source: UniProtKB guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide phospholipase C activity Inferred from sequence or structural similarity. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8K4S1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8K4S1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1150: Missing.
     1151-1165: TAGSPNLATGMSSPI → MAWGLHLPVTAMFLC

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2282	2282	1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1		PRO_0000256239
Regions
	Domain	528 – 781	254	Ras-GEF
	Domain	1373 – 1521	149	PI-PLC X-box
	Domain	1710 – 1826	117	PI-PLC Y-box
	Domain	1836 – 1936	101	C2
	Domain	1992 – 2094	103	Ras-associating 1
	Domain	2115 – 2218	104	Ras-associating 2
	Region	1667 – 1744	78	Required for activation by RHOA, RHOB, GNA12, GNA13 and G-beta gamma By similarity
Sites
	Active site	1388	1	By similarity
	Active site	1433	1	By similarity
Natural variations
	Alternative sequence	1 – 1150	1150	Missing in isoform 2.		VSP_021337
	Alternative sequence	1151 – 1165	15	TAGSP…MSSPI → MAWGLHLPVTAMFLC in isoform 2.		VSP_021338
Experimental info
	Sequence conflict	1798	1	T → A in AAF40208. Ref.4
	Sequence conflict	1829	1	S → N in AAF40208. Ref.4
	Sequence conflict	2215 – 2217	3	LKE → VKD in BAC29099. Ref.2
	Sequence conflict	2233	1	A → G in BAC29099. Ref.2
	Sequence conflict	2236	1	L → V in BAC29099. Ref.2
	Sequence conflict	2239	1	L → V in BAC29099. Ref.2
	Sequence conflict	2275	1	S → T in BAC29099. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 1E694A07ADADFFB3	FASTA	2,282	255,020
	10 20 30 40 50 60 MTSEEMAASV LIPVTQRKVA SAQSVAEERS VKVSDAGIPR ARAGRQGALI PPTISQWNKH 70 80 90 100 110 120 KEESSRSDLS KVFSIARGEL VCDENSNEEG WEENAPDSPE NHAMNGNSLV QSHQHQFPRS 130 140 150 160 170 180 QLCEARDSVT EDPCLQPGIP SPLERKVLPG IQLEMEDSPM DVSPAGSQPR IMESSGPHSD 190 200 210 220 230 240 RNTAVFHFHY EADRTMSDAF HTLSENLILD DCANCVTLPG GQQNKNCMAY ACKLVELTRT 250 260 270 280 290 300 CGSKNGQVQC EHCTSLRDEY LCFESSCSKA DEVCSGGGFC EDGFAHGPAA KTFLSPLEDF 310 320 330 340 350 360 SDNCEDVDDF FKSKKERSTL LVRRFCKNDR EVKKSVYTGT RAIMRTLPSG CIGPAAWNYV 370 380 390 400 410 420 DQKKAGLLWP CGNVMGTLSA MDIRQSGSQR LSEAQWCLIY SAVRRGEEIE DTVGSLLHCS 430 440 450 460 470 480 TQLPNSETAH GRIEDGPCLK QCVRDTECEF RATLQRTSIA QYITGSLLEA TTSLGARSGL 490 500 510 520 530 540 LSSFGGSTGR IMLKERQLGT SMANSNPVPS SSAGISKELI DLQPLIQFPE EVASILTEQE 550 560 570 580 590 600 QNIYRRVLPM DYLCFLTRDL SSPECQRSLP RLKASISESI LTSQSGEHNA LEDLVMRFNE 610 620 630 640 650 660 VSSWVTWLIL TAGSMEEKRE VFSYLVHVAK CCWNMGNYNA VMEFLAGLRS RKVLKMWQFM 670 680 690 700 710 720 DQSDIETMRS LKDAMAQHES SVEYKKVVTR ALHIPGCKVV PFCGVFLKEL CEVLDGASGL 730 740 750 760 770 780 LKLCPRYSSQ EEALEFVADY SGQDNFLQRV GQNGLKNSEK ELTVNSIFQV IRSCSRSLEM 790 800 810 820 830 840 EEEDSASEGS GSRKNSLKDK ARWQFIIGDL LDSENDIFEK SKECDPHGSE ESQKAFDHGT 850 860 870 880 890 900 ELIPWYVLSI QADVHQFLLQ GATVIHYDQD THLSARCFLQ LQPDNSTLTW MKPPTASPAG 910 920 930 940 950 960 ARPKLGVLSN MAEPGKFPSP GNAGVSGLAE GILDLFSVKA VYMGHPGIDI HTVCVQNKLS 970 980 990 1000 1010 1020 SMLLSETGVT LLYGLQTTDN RLLHFVAPKH TAEMLFSGLL ELTTAVRKIR RFPDQRQQWL 1030 1040 1050 1060 1070 1080 RKQYVSLYQE DGRYEGPTLA HAVELFGGRR WSTRNPSPGM SAKNAEKPNM QRNNTLGIST 1090 1100 1110 1120 1130 1140 TKKKKKMLMR GESGEVTDDE MATRKAKMYR ECRSRSGSDP QDVNEQEESE ANVITNPPNP 1150 1160 1170 1180 1190 1200 LHSRRAYSLT TAGSPNLATG MSSPISAWSS SSWHGRIRGG MQGFQSFMVS DSNMSFVEFV 1210 1220 1230 1240 1250 1260 ELFKSFSIRS RKDLKDIFDI YSVPCNRSAS ESAPLYTNLT IEENTSDLQP DLDLLTRNVS 1270 1280 1290 1300 1310 1320 DLGLFIKSKQ QLSDNQRQIS DAIAAASIVT NGTGIESTSL GIFGVGILQL NDFLVNCQGE 1330 1340 1350 1360 1370 1380 HCTYDEILSI IQKFEPSVSM CHQGLLSFEG FARFLMDKDN FASKNDESRE NKKELQLPLS 1390 1400 1410 1420 1430 1440 YYYIESSHNT YLTGHQLKGE SSVELYSQVL LQGCRSIELD CWDGDDGMPI IYHGHTLTTK 1450 1460 1470 1480 1490 1500 IPFKEVVEAI DRSAFITSDL PIIISIENHC SLPQQRKMAE IFKSVFGEKL VAKFLFETDF 1510 1520 1530 1540 1550 1560 SDDPMLPSPD QLRRKVLLKN KKLKAHQTPV DILKQKAHQL ASMQAQAFTG GNANPPPASN 1570 1580 1590 1600 1610 1620 EEEEDEEDEY DYDYESLSDD NILEDRPENK SCADKLQFEY NEEVPKRIKK ADNSSGNKGK 1630 1640 1650 1660 1670 1680 VYDMELGEEF YLPQNKKESR QIAPELSDLV IYCQAVKFPG LSTLNSSGSS RGKERKSRKS 1690 1700 1710 1720 1730 1740 IFGNNPGRMS PGETAPFNRT SGKGSCEGMR HTWEESSPLS PSTSLSAIIR TPKCYHISSL 1750 1760 1770 1780 1790 1800 NENAAKRLCR RGSQKLIQHT AYQLLRTYPA ATRIDSSNPN PIMFWLHGIQ LVALNYQTDD 1810 1820 1830 1840 1850 1860 LPLHLNAAMF EANGGCGYVL KPPVLWDKSC PMYQKFSPLE RDLDNLDPAI YSLTIISGQN 1870 1880 1890 1900 1910 1920 VCPSNSTGSP CIEVDVLGMP LDSCHFRTKP IHRNTLNPMW NEQFLFRVHF EDLVFLRFAV 1930 1940 1950 1960 1970 1980 VENNSSAITA QRIIPLRALK RGYRHLQLRN LHNEILEISS LFINSRRMEE NPSGSSMPAS 1990 2000 2010 2020 2030 2040 LMFNTEERKC SQTHKVTVHG VPGPEPFAVF TINEGTKAKQ LLQQVLAVDQ DTKCTATDYF 2050 2060 2070 2080 2090 2100 LMEEKHFISK EKNECRKQPF QRAVGPEEDI VQILNSWFPE EGYVGRIVLK PQQETLEEKS 2110 2120 2130 2140 2150 2160 IVFDDKEVIL SSEEESFFVQ VHDVSPEQPR TVIKAPRVST AQDVIQQTLC KAKYSYSILN 2170 2180 2190 2200 2210 2220 NPNPCDYVLL EEVLKDAANK KSSTPKSSQR ILLDQECVFQ AQSKWKGAGK FILKLKEQVQ 2230 2240 2250 2260 2270 2280 ASREDKRRGI SFASELKKLT KSTKQSRGLP SPPQLVASES VQSKEEKPVG ALSSSDTVGY QQ
	Isoform 2. Checksum: B0647BF909EAD5BE	FASTA	1,132	127,581
	10 20 30 40 50 60 MAWGLHLPVT AMFLCSAWSS SSWHGRIRGG MQGFQSFMVS DSNMSFVEFV ELFKSFSIRS 70 80 90 100 110 120 RKDLKDIFDI YSVPCNRSAS ESAPLYTNLT IEENTSDLQP DLDLLTRNVS DLGLFIKSKQ 130 140 150 160 170 180 QLSDNQRQIS DAIAAASIVT NGTGIESTSL GIFGVGILQL NDFLVNCQGE HCTYDEILSI 190 200 210 220 230 240 IQKFEPSVSM CHQGLLSFEG FARFLMDKDN FASKNDESRE NKKELQLPLS YYYIESSHNT 250 260 270 280 290 300 YLTGHQLKGE SSVELYSQVL LQGCRSIELD CWDGDDGMPI IYHGHTLTTK IPFKEVVEAI 310 320 330 340 350 360 DRSAFITSDL PIIISIENHC SLPQQRKMAE IFKSVFGEKL VAKFLFETDF SDDPMLPSPD 370 380 390 400 410 420 QLRRKVLLKN KKLKAHQTPV DILKQKAHQL ASMQAQAFTG GNANPPPASN EEEEDEEDEY 430 440 450 460 470 480 DYDYESLSDD NILEDRPENK SCADKLQFEY NEEVPKRIKK ADNSSGNKGK VYDMELGEEF 490 500 510 520 530 540 YLPQNKKESR QIAPELSDLV IYCQAVKFPG LSTLNSSGSS RGKERKSRKS IFGNNPGRMS 550 560 570 580 590 600 PGETAPFNRT SGKGSCEGMR HTWEESSPLS PSTSLSAIIR TPKCYHISSL NENAAKRLCR 610 620 630 640 650 660 RGSQKLIQHT AYQLLRTYPA ATRIDSSNPN PIMFWLHGIQ LVALNYQTDD LPLHLNAAMF 670 680 690 700 710 720 EANGGCGYVL KPPVLWDKSC PMYQKFSPLE RDLDNLDPAI YSLTIISGQN VCPSNSTGSP 730 740 750 760 770 780 CIEVDVLGMP LDSCHFRTKP IHRNTLNPMW NEQFLFRVHF EDLVFLRFAV VENNSSAITA 790 800 810 820 830 840 QRIIPLRALK RGYRHLQLRN LHNEILEISS LFINSRRMEE NPSGSSMPAS LMFNTEERKC 850 860 870 880 890 900 SQTHKVTVHG VPGPEPFAVF TINEGTKAKQ LLQQVLAVDQ DTKCTATDYF LMEEKHFISK 910 920 930 940 950 960 EKNECRKQPF QRAVGPEEDI VQILNSWFPE EGYVGRIVLK PQQETLEEKS IVFDDKEVIL 970 980 990 1000 1010 1020 SSEEESFFVQ VHDVSPEQPR TVIKAPRVST AQDVIQQTLC KAKYSYSILN NPNPCDYVLL 1030 1040 1050 1060 1070 1080 EEVLKDAANK KSSTPKSSQR ILLDQECVFQ AQSKWKGAGK FILKLKEQVQ ASREDKRRGI 1090 1100 1110 1120 1130 SFASELKKLT KSTKQSRGLP SPPQLVASES VQSKEEKPVG ALSSSDTVGY QQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Neuronal lineage-specific induction of phospholipase Cepsilon expression in the developing mouse brain." Wu D., Tadano M., Edamatsu H., Masago-Toda M., Yamawaki-Kataoka Y., Terashima T., Mizoguchi A., Minami Y., Satoh T., Kataoka T. Eur. J. Neurosci. 17:1571-1580(2003) [PubMed: 12752375] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, INDUCTION. Tissue: Embryo.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Egg and Urinary bladder.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[4]	"A novel transgenic marker for migrating limb muscle precursors and for vascular smooth muscle cells." Tidhar A., Reichenstein M., Cohen D., Faerman A., Copeland N.G., Gilbert D.J., Jenkins N.A., Shani M. Dev. Dyn. 220:60-73(2001) [PubMed: 11146508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 919-2282 (ISOFORMS 1/2).
[5]	"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H. DNA Res. 10:35-48(2003) [PubMed: 12693553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 919-2282 (ISOFORMS 1/2). Tissue: Brain.
[6]	"Activation of CD4 T cells by Raf-independent effectors of Ras." Czyzyk J., Brogdon J.L., Badou A., Henegariu O., Preston Hurlburt P., Flavell R., Bottomly K. Proc. Natl. Acad. Sci. U.S.A. 100:6003-6008(2003) [PubMed: 12721365] [Abstract] Cited for: FUNCTION.
[7]	"Crucial role of phospholipase Cepsilon in chemical carcinogen-induced skin tumor development." Bai Y., Edamatsu H., Maeda S., Saito H., Suzuki N., Satoh T., Kataoka T. Cancer Res. 64:8808-8810(2004) [PubMed: 15604236] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[8]	"Phospholipase C epsilon modulates beta-adrenergic receptor-dependent cardiac contraction and inhibits cardiac hypertrophy." Wang H., Oestreich E.A., Maekawa N., Bullard T.A., Vikstrom K.L., Dirksen R.T., Kelley G.G., Blaxall B.C., Smrcka A.V. Circ. Res. 97:1305-1313(2005) [PubMed: 16293787] [Abstract] Cited for: FUNCTION, INDUCTION.
[9]	"Congenital semilunar valvulogenesis defect in mice deficient in phospholipase C epsilon." Tadano M., Edamatsu H., Minamisawa S., Yokoyama U., Ishikawa Y., Suzuki N., Saito H., Wu D., Masago-Toda M., Yamawaki-Kataoka Y., Setsu T., Terashima T., Maeda S., Satoh T., Kataoka T. Mol. Cell. Biol. 25:2191-2199(2005) [PubMed: 15743817] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[10]	"Positional cloning uncovers mutations in PLCE1 responsible for a nephrotic syndrome variant that may be reversible." Hinkes B., Wiggins R.C., Gbadegesin R., Vlangos C.N., Seelow D., Nuernberg G., Garg P., Verma R., Chaib H., Hoskins B.E., Ashraf S., Becker C., Hennies H.C., Goyal M., Wharram B.L., Schachter A.D., Mudumana S., Drummond I. , Kerjaschki D., Waldherr R., Dietrich A., Ozaltin F., Bakkaloglu A., Cleper R., Basel-Vanagaite L., Pohl M., Griebel M., Tsygin A.N., Soylu A., Mueller D., Sorli C.S., Bunney T.D., Katan M., Liu J., Attanasio M., O'toole J.F., Hasselbacher K., Mucha B., Otto E.A., Airik R., Kispert A., Kelley G.G., Smrcka A.V., Gudermann T., Holzman L.B., Nuernberg P., Hildebrandt F. Nat. Genet. 38:1397-1405(2006) [PubMed: 17086182] [Abstract] Cited for: INTERACTION WITH IQGAP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB076247 mRNA. Translation: BAC00906.1. AK035546 mRNA. Translation: BAC29099.1. AK162236 mRNA. Translation: BAE36807.1. BC138349 mRNA. Translation: AAI38350.1. BC138350 mRNA. Translation: AAI38351.1. AF233885 mRNA. Translation: AAF40208.1. Different initiation. AK122521 mRNA. Translation: BAC65803.1.
IPI	IPI00170268. IPI00798586.
RefSeq	NP_062534.2.
UniGene	Mm.34031
3D structure databases
HSSP	HSSP built from PDB template 2C5L based on UniProtKB Q9UHV3.
SMR	Q8K4S1. Positions 528-827, 1309-1966, 1986-2094, 2111-2226.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8K4S1.
PTM databases
PhosphoSite	Q8K4S1.
Proteomic databases
PRIDE	Q8K4S1.
Genome annotation databases
Ensembl	ENSMUST00000025962; ENSMUSP00000025962; ENSMUSG00000024998; Mus musculus. [Genome view]
GeneID	74055.
KEGG	mmu:74055.
UCSC	uc008hjp.1. mouse. uc008hjq.1. mouse.
Organism-specific databases
CTD	74055.
MGI	MGI:1921305. Plce1.
Rouge	Search...
Phylogenomic databases
eggNOG	roNOG11704.
HOVERGEN	Q8K4S1.
InParanoid	Q8K4S1.
PhylomeDB	Q8K4S1.
Enzyme and pathway databases
BRENDA	3.1.4.11. 244.
Gene expression databases
ArrayExpress	Q8K4S1.
Bgee	Q8K4S1.
CleanEx	MM_PLCE1.
Genevestigator	Q8K4S1.
GermOnline	ENSMUSG00000024998. Mus musculus.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR000909. PLipase_C_PInositol-sp_X_dom. IPR000159. Ras-assoc. IPR008937. Ras_GEF. IPR001895. RasGRF_CDC25. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 2 hits. G3DSA:1.10.840.10. RasGRF_CDC25. 1 hit.
Pfam	PF00168. C2. 1 hit. PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. PF00788. RA. 1 hit. PF00617. RasGEF. 1 hit. [Graphical view]
PRINTS	PR00390. PHPHLIPASEC.
SMART	SM00239. C2. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. SM00314. RA. 1 hit. SM00147. RasGEF. 1 hit. [Graphical view]
PROSITE	PS50004. C2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. PS50200. RA. 1 hit. PS00720. RASGEF. False negative. PS50009. RASGEF_CAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	339656.
SOURCE	Search...

Entry information

Entry name

PLCE1_MOUSE

Accession

Primary (citable) accession number: Q8K4S1
Secondary accession number(s): B9EHS1 , Q3TS68, Q80TC4, Q8BZF3, Q9JKM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	February 9, 2010
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)