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Q8K4S1 (PLCE1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2282 AA.
Sequence statusComplete.
Protein existenceEvidence 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.7 Ref.8 Ref.9 Ref.10

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.11

Subcellular location

Cytoplasmcytosol 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.8 Ref.10

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 but not glial cells. Up-regulated in heart upon induced hypertrophy. Ref.1 Ref.9

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.8 Ref.10

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.

Sequence caution

The sequence BAC29099.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
   DomainRepeat
   Molecular functionGuanine-nucleotide releasing factor
Hydrolase
Transducer
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from sequence or structural similarity. Source: UniProtKB

glomerulus development

Inferred from electronic annotation. Source: Ensembl

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

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

regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium 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

phosphatidylinositol phospholipase C activity

Inferred from sequence or structural similarity. Source: UniProtKB

phospholipase C activity

Inferred from sequence or structural similarity. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 228222821-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
PRO_0000256239

Regions

Domain528 – 781254Ras-GEF
Domain1373 – 1521149PI-PLC X-box
Domain1710 – 1826117PI-PLC Y-box
Domain1836 – 1936101C2
Domain1992 – 2094103Ras-associating 1
Domain2115 – 2218104Ras-associating 2
Region1667 – 174478Required for activation by RHOA, RHOB, GNA12, GNA13 and G-beta gamma By similarity

Sites

Active site13881 By similarity
Active site14331 By similarity

Experimental info

Sequence conflict2951N → S in BAC00906. Ref.1
Sequence conflict2951N → S in AAI38350. Ref.3
Sequence conflict2951N → S in AAI38351. Ref.3
Sequence conflict17981T → A in AAF40208. Ref.6
Sequence conflict18291S → N in AAF40208. Ref.6
Sequence conflict2215 – 22173LKE → VKD in BAC29099. Ref.5
Sequence conflict22331A → G in BAC29099. Ref.5
Sequence conflict22361L → V in BAC29099. Ref.5
Sequence conflict22391L → V in BAC29099. Ref.5
Sequence conflict22751S → T in BAC29099. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8K4S1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: AA288A76304E43ED

FASTA2,282255,047
        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 KTFLNPLEDF 

       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 

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References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, INDUCTION.
Tissue: Embryo.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 919-2282.
Tissue: Brain.
[5]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1166-2282.
Strain: C57BL/6J.
Tissue: Egg and Urinary bladder.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1661-2282.
[7]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[9]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[10]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[11]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IQGAP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB076247 mRNA. Translation: BAC00906.1.
AC111023 Genomic DNA. No translation available.
AC158905 Genomic DNA. No translation available.
BC138349 mRNA. Translation: AAI38350.1.
BC138350 mRNA. Translation: AAI38351.1.
AK122521 mRNA. Translation: BAC65803.1.
AK035546 mRNA. Translation: BAC29099.1. Sequence problems.
AK162236 mRNA. Translation: BAE36807.1.
AF233885 mRNA. Translation: AAF40208.1.
RefSeqNP_062534.2. NM_019588.2.
UniGeneMm.34031.

3D structure databases

ProteinModelPortalQ8K4S1.
SMRQ8K4S1. Positions 1986-2094, 2111-2226.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8K4S1. 2 interactions.
MINTMINT-4117894.

PTM databases

PhosphoSiteQ8K4S1.

Proteomic databases

PaxDbQ8K4S1.
PRIDEQ8K4S1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000169713; ENSMUSP00000130604; ENSMUSG00000024998.
ENSMUST00000182481; ENSMUSP00000138360; ENSMUSG00000024998.
GeneID74055.
KEGGmmu:74055.
UCSCuc008hjp.1. mouse.

Organism-specific databases

CTD51196.
MGIMGI:1921305. Plce1.
RougeSearch...

Phylogenomic databases

eggNOGNOG149692.
GeneTreeENSGT00730000110782.
HOVERGENHBG059220.
InParanoidQ8K4S1.
KOK05860.
OMAVAKCCWN.
OrthoDBEOG7SN8CX.
TreeFamTF314432.

Enzyme and pathway databases

BRENDA3.1.4.11. 3474.

Gene expression databases

BgeeQ8K4S1.
CleanExMM_PLCE1.
GenevestigatorQ8K4S1.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.10.840.10. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 3 hits.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR028398. PLC-epsilon1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000159. Ras-assoc.
IPR023578. Ras_GEF_dom.
IPR001895. RasGRF_CDC25.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF6. PTHR10336:SF6. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. EF-hand_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]
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00314. RA. 1 hit.
SM00147. RasGEF. 1 hit.
[Graphical view]
SUPFAMSSF48366. SSF48366. 2 hits.
SSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 3 hits.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
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NextBio339656.
PROQ8K4S1.
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Entry information

Entry namePLCE1_MOUSE
AccessionPrimary (citable) accession number: Q8K4S1
Secondary accession number(s): B9EHS1 expand/collapse secondary AC list , E9Q5G0, Q3TS68, Q80TC4, Q8BZF3, Q9JKM2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot