PLCD3
entrez
113026
canonical
uniprot
Q8N3E9
canonical
ensembl
ENSG00000161714
resolver
ensp
ENSP00000479636
resolver
ensp
ENSP00000535015
resolver
enst
ENST00000619929
resolver
genesymbol
PLCD3
resolver
genesymbol_syn
KIAA1964
resolver
hgnc
HGNC:9061
resolver
uniprot
Q8TEC1
resolver
uniprot
Q8TF37
resolver
uniprot
Q96FL6
resolver
uniprot_entry
PLCD3_HUMAN
resolver
uniprot_sec
Q8TEC1
resolver
uniprot_sec
Q8TF37
resolver
uniprot_sec
Q96FL6
resolver
activity_regulation
ACTIVITY REGULATION: Strongly activated by phosphatidic acid. Inhibited by phosphatidylethanolamine (PtdEtn), phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine (PtdSer). {ECO:0000269|PubMed:10336610, ECO:0000269|PubMed:9799116}.
uniprot
proteins
amino_acid_sequence
MLCGRWRRCRRPPEEPPVAAQVAAQVAAPVALPSPPTPSDGGTKRPGLRALKKMGLTEDEDVRAMLRGSRLRKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAPSQHIFFVQHIEAVREGHQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLTKLRARLDAMSQRERLDHWIHSYLHRADSNQDSKMSFKEIKSLLRMVNVDMNDMYAYLLFKECDHSNNDRLEGAEIEEFLRRLLKRPELEEIFHQYSGEDRVLSAPELLEFLEDQGEEGATLARAQQLIQTYELNETAKQHELMTLDGFMMYLLSPEGAALDNTHTCVFQDMNQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVVQAVRDHAFTLSPYPVILSLENHCGLEQQAAMARHLCTILGDMLVTQALDSPNPEELPSPEQLKGRVLVKGKKLPAARSEDGRALSDREEEEEDDEEEEEEVEAAAQRRLAKQISPELSALAVYCHATRLRTLHPAPNAPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVNGQCGYVLKPACLRQPDSTFDPEYPGPPRTTLSIQVLTAQQLPKLNAEKPHSIVDPLVRIEIHGVPADCARQETDYVLNNGFNPRWGQTLQFQLRAPELALVRFVVEDYDATSPNDFVGQFTLPLSSLKQGYRHIHLLSKDGASLSPATLFIQIRIQRS
uniprot
proteins
ec_number
3.1.4.11
uniprot
proteins
function
FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow (PubMed:10336610). Regulates neurite outgrowth through the inhibition of RhoA/Rho kinase signaling (By similarity). {ECO:0000250|UniProtKB:Q8K2J0, ECO:0000269|PubMed:10336610}.
uniprot
proteins
mass_dalton
89258
uniprot
proteins
pubmed
10336610
uniprot
proteins
pubmed
10702670
uniprot
proteins
pubmed
11500033
uniprot
proteins
pubmed
11706040
uniprot
proteins
pubmed
11853319
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15505048
uniprot
proteins
pubmed
17041247
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
9056492
uniprot
proteins
pubmed
9360711
uniprot
proteins
pubmed
9799116
uniprot
proteins
sequence_length
789
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11706040}; Peripheral membrane protein {ECO:0000269|PubMed:11706040}. Cytoplasm {ECO:0000269|PubMed:11706040}. Cleavage furrow {ECO:0000269|PubMed:17041247}. Note=Localizes at the cleavage furrow during cytokinesis (PubMed:17041247). The membrane binding is driven by the C2 domain and involves non-specific electrostatic interactions between the calcium-induced cationic surface of protein and the anionic membrane and specific interactions involving calcium and phosphatidylserine (PS) (PubMed:11706040). The PS selectivity governs its specific calcium-dependent subcellular targeting to the plasma membrane (PubMed:11706040). {ECO:0000269|PubMed:11706040, ECO:0000269|PubMed:17041247}.
uniprot
proteins