PLCE1
entrez
51196
canonical
uniprot
Q9P212
canonical
ensembl
ENSG00000138193
resolver
ensp
ENSP00000360426
resolver
ensp
ENSP00000360431
resolver
ensp
ENSP00000501910
resolver
ensp
ENSP00000508416
resolver
ensp
ENSP00000508605
resolver
ensp
ENSP00000509140
resolver
ensp
ENSP00000509490
resolver
ensp
ENSP00000545511
resolver
enst
ENST00000688810
resolver
enst
ENST00000692396
resolver
genesymbol
PLCE1
resolver
genesymbol_syn
KIAA1516
resolver
genesymbol_syn
PLCE
resolver
genesymbol_syn
PPLC
resolver
hgnc
HGNC:17175
resolver
uniprot
A0A8I5KXT2
resolver
uniprot
A0A8I5QKK3
resolver
uniprot
A6NGW0
resolver
uniprot
A6NLA1
resolver
uniprot
A7MBN7
resolver
uniprot
A8K1D7
resolver
uniprot
B7ZM61
resolver
uniprot
B9EIJ6
resolver
uniprot
Q1X6H8
resolver
uniprot
Q5VWL4
resolver
uniprot
Q5VWL5
resolver
uniprot
Q9H9X8
resolver
uniprot
Q9HBX6
resolver
uniprot
Q9HC53
resolver
uniprot
Q9UHV3
resolver
uniprot_entry
A0A8I5KXT2_HUMAN
resolver
uniprot_entry
A0A8I5QKK3_HUMAN
resolver
uniprot_entry
B7ZM61_HUMAN
resolver
uniprot_entry
PLCE1_HUMAN
resolver
uniprot_sec
A6NGW0
resolver
uniprot_sec
A6NLA1
resolver
uniprot_sec
A7MBN7
resolver
uniprot_sec
A8K1D7
resolver
uniprot_sec
B9EIJ6
resolver
uniprot_sec
Q1X6H8
resolver
uniprot_sec
Q5VWL4
resolver
uniprot_sec
Q5VWL5
resolver
uniprot_sec
Q9H9X8
resolver
uniprot_sec
Q9HBX6
resolver
uniprot_sec
Q9HC53
resolver
uniprot_sec
Q9UHV3
resolver
activity_regulation
ACTIVITY 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. {ECO:0000269|PubMed:11022047, ECO:0000269|PubMed:11022048, ECO:0000269|PubMed:11715024, ECO:0000269|PubMed:11877431, ECO:0000269|PubMed:15157671, ECO:0000269|PubMed:16537651}.
uniprot
proteins
amino_acid_sequence
MTSEEMTASVLIPVTQRKVVSAQSAADESSEKVSDINISKAHTVRRSGETSHTISQLNKLKEEPSGSNLPKILSIAREKIVSDENSNEKCWEKIMPDSAKNLNINCNNILRNHQHGLPQRQFYEMYNSVAEEDLCLETGIPSPLERKVFPGIQLELDRPSMGISPLGNQSVIIETGRAHPDSRRAVFHFHYEVDRRMSDTFCTLSENLILDDCGNCVPLPGGEEKQKKNYVAYTCKLMELAKNCDNKNEQLQCDHCDTLNDKYFCFEGSCEKVDMVYSGDSFCRKDFTDSQAAKTFLSHFEDFPDNCDDVEEDAFKSKKERSTLLVRRFCKNDREVKKSVYTGTRAIVRTLPSGHIGLTAWSYIDQKRNGPLLPCGRVMEPPSTVEIRQDGSQRLSEAQWYPIYNAVRREETENTVGSLLHFLTKLPASETAHGRISVGPCLKQCVRDTVCEYRATLQRTSISQYITGSLLEATTSLGARSGLLSTFGGSTGRMMLKERQPGPSVANSNALPSSSAGISKELIDLQPLIQFPEEVASILMEQEQTIYRRVLPVDYLCFLTRDLGTPECQSSLPCLKASISASILTTQNGEHNALEDLVMRFNEVSSWVTWLILTAGSMEEKREVFSYLVHVAKCCWNMGNYNAVMEFLAGLRSRKVLKMWQFMDQSDIETMRSLKDAMAQHESSCEYRKVVTRALHIPGCKVVPFCGVFLKELCEVLDGASGLMKLCPRYNSQEETLEFVADYSGQDNFLQRVGQNGLKNSEKESTVNSIFQVIRSCNRSLETDEEDSPSEGNSSRKSSLKDKSRWQFIIGDLLDSDNDIFEQSKEYDSHGSEDSQKAFDHGTELIPWYVLSIQADVHQFLLQGATVIHYDQDTHLSARCFLQLQPDNSTLTWVKPTTASPASSKAKLGVLNNTAEPGKFPLLGNAGLSSLTEGVLDLFAVKAVYMGHPGIDIHTVCVQNKLGSMFLSETGVTLLYGLQTTDNRLLHFVAPKHTAKMLFSGLLELTRAVRKMRKFPDQRQQWLRKQYVSLYQEDGRYEGPTLAHAVELFGGRRWSARNPSPGTSAKNAEKPNMQRNNTLGISTTKKKKKILMRGESGEVTDDEMATRKAKMHKECRSRSGSDPQDINEQEESEVNAIANPPNPLPSRRAHSLTTAGSPNLAAGTSSPIRPVSSPVLSSSNKSPSSAWSSSSWHGRIKGGMKGFQSFMVSDSNMSFVEFVELFKSFSVRSRKDLKDLFDVYAVPCNRSGSESAPLYTNLTIDENTSDLQPDLDLLTRNVSDLGLFIKSKQQLSDNQRQISDAIAAASIVTNGTGIESTSLGIFGVGILQLNDFLVNCQGEHCTYDEILSIIQKFEPSISMCHQGLMSFEGFARFLMDKENFASKNDESQENIKELQLPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLQGCRSVELDCWDGDDGMPIIYHGHTLTTKIPFKEVVEAIDRSAFINSDLPIIISIENHCSLPQQRKMAEIFKTVFGEKLVTKFLFETDFSDDPMLPSPDQLRKKVLLKNKKLKAHQTPVDILKQKAHQLASMQVQAYNGGNANPRPANNEEEEDEEDEYDYDYESLSDDNILEDRPENKSCNDKLQFEYNEEIPKRIKKADNSACNKGKVYDMELGEEFYLDQNKKESRQIAPELSDLVIYCQAVKFPGLSTLNASGSSRGKERKSRKSIFGNNPGRMSPGETASFNKTSGKSSCEGIRQTWEESSSPLNPTTSLSAIIRTPKCYHISSLNENAAKRLCRRYSQKLTQHTACQLLRTYPAATRIDSSNPNPLMFWLHGIQLVALNYQTDDLPLHLNAAMFEANGGCGYVLKPPVLWDKNCPMYQKFSPLERDLDSMDPAVYSLTIVSGQNVCPSNSMGSPCIEVDVLGMPLDSCHFRTKPIHRNTLNPMWNEQFLFHVHFEDLVFLRFAVVENNSSAVTAQRIIPLKALKRGYRHLQLRNLHNEVLEISSLFINSRRMEENSSGNTMSASSMFNTEERKCLQTHRVTVHGVPGPEPFTVFTINGGTKAKQLLQQILTNEQDIKPVTTDYFLMEEKYFISKEKNECRKQPFQRAIGPEEEIMQILSSWFPEEGYMGRIVLKTQQENLEEKNIVQDDKEVILSSEEESFFVQVHDVSPEQPRTVIKAPRVSTAQDVIQQTLCKAKYSYSILSNPNPSDYVLLEEVVKDTTNKKTTTPKSSQRVLLDQECVFQAQSKWKGAGKFILKLKEQVQASREDKKKGISFASELKKLTKSTKQPRGLTSPSQLLTSESIQTKEEKPVGGLSSSDTMDYRQ
uniprot
proteins
disease_involvement
DISEASE: Nephrotic syndrome 3 (NPHS3) [MIM:610725]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. Most patients with NPHS3 show diffuse mesangial sclerosis on renal biopsy, which is a pathologic entity characterized by mesangial matrix expansion with no mesangial hypercellularity, hypertrophy of the podocytes, vacuolized podocytes, thickened basement membranes, and diminished patency of the capillary lumen. {ECO:0000269|PubMed:17086182, ECO:0000269|PubMed:23595123}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.4.11
uniprot
proteins
function
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. In podocytes, is involved in the regulation of lamellipodia formation. Acts downstream of AVIL to allow ARP2/3 complex assembly (PubMed:29058690). {ECO:0000269|PubMed:11022047, ECO:0000269|PubMed:11395506, ECO:0000269|PubMed:11715024, ECO:0000269|PubMed:11877431, ECO:0000269|PubMed:12721365, ECO:0000269|PubMed:16537651, ECO:0000269|PubMed:17086182, ECO:0000269|PubMed:29058690}.
uniprot
proteins
mass_dalton
258715
uniprot
proteins
mutagenesis
MUTAGEN 1452; /note="H->L: Loss of the phospholipase C enzymatic activity. Still activates HRAS and the MAP kinase pathway."; /evidence="ECO:0000269|PubMed:11022047"; MUTAGEN 2140; /note="Q->E: Increases 2.8-fold the affinity for HRAS."; /evidence="ECO:0000269|PubMed:16483931"; MUTAGEN 2148; /note="Q->E: Decreases 17.5-fold the affinity for HRAS."; /evidence="ECO:0000269|PubMed:16483931"; MUTAGEN 2148; /note="Q->K: Increases 1.4-fold the affinity for HRAS."; /evidence="ECO:0000269|PubMed:16483931"; MUTAGEN 2150; /note="R->L: Abolishes interaction with HRAS."; /evidence="ECO:0000269|PubMed:16483931"; MUTAGEN 2171; /note="K->L: No effect on HRAS-binding."; /evidence="ECO:0000269|PubMed:16483931"; MUTAGEN 2174; /note="Y->L: Reduces HRAS-binding."; /evidence="ECO:0000269|PubMed:16483931
uniprot
proteins
pubmed
10819331
uniprot
proteins
pubmed
11022047
uniprot
proteins
pubmed
11022048
uniprot
proteins
pubmed
11395506
uniprot
proteins
pubmed
11715024
uniprot
proteins
pubmed
11877431
uniprot
proteins
pubmed
12444546
uniprot
proteins
pubmed
12721365
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15157671
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15558028
uniprot
proteins
pubmed
16293787
uniprot
proteins
pubmed
16483931
uniprot
proteins
pubmed
16537651
uniprot
proteins
pubmed
17086182
uniprot
proteins
pubmed
23595123
uniprot
proteins
pubmed
29058690
uniprot
proteins
sequence_length
2302
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11022048}. Cell membrane {ECO:0000269|PubMed:11022048}; Peripheral membrane protein {ECO:0000305|PubMed:11022048}; Cytoplasmic side {ECO:0000305|PubMed:11022048}. Golgi apparatus membrane. Cell projection, lamellipodium {ECO:0000269|PubMed:29058690}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11022048}. Note=Recruited to plasma membrane by activated HRAS and RAP2 (PubMed:11022048). Recruited to perinuclear region by activated RAP1A (PubMed:11022048). Isoform 1 and isoform 2 associates with Golgi membranes. {ECO:0000269|PubMed:11022048}.
uniprot
proteins