Plcd3
entrez
72469
canonical
uniprot
Q8K2J0
canonical
ensembl
ENSMUSG00000020937
resolver
ensp
ENSMUSP00000099366
resolver
ensp
ENSMUSP00000117455
resolver
ensp
ENSMUSP00000264671
resolver
enst
ENSMUST00000103077
resolver
genesymbol
Plcd3
resolver
genesymbol_syn
Kiaa1964
resolver
uniprot
A2AHR0
resolver
uniprot
A2AHR1
resolver
uniprot
Q3UME8
resolver
uniprot
Q69Z55
resolver
uniprot
Q8BL19
resolver
uniprot_entry
PLCD3_MOUSE
resolver
uniprot_sec
A2AHR0
resolver
uniprot_sec
A2AHR1
resolver
uniprot_sec
Q3UME8
resolver
uniprot_sec
Q69Z55
resolver
uniprot_sec
Q8BL19
resolver
activity_regulation
ACTIVITY REGULATION: Strongly activated by phosphatidic acid. Inhibited by phosphatidylethanolamine (PtdEtn), phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine (PtdSer) (By similarity). {ECO:0000250|UniProtKB:Q8N3E9}.
uniprot
proteins
amino_acid_sequence
MLCGGWKRSRRSPEESRVSAQVAAPLAFPPSPASSDSSTKRPGLRALKKMGLTEDEDVQAMLRGSRLLKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAASKHIFFVQHIEAVREGHQSEGLRRFGGAFAPACCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLAKLRARLDAMSQRERLDHWIHSYLHRADSDQDSKMSFKEIKSLLRMVNVDMNDMYAYRLFKECDHSNNERLEGAEIEAFLRRLLKRPELEEIFRRYSGEDRVLSASELLEFLEDQGEDGATLACAQQLIQTYELNETAKQHELMTLDGFMMYLLSPEGAALNVAHTCVFQDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRDHAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPEELPSPEQLKGRILVKGKKLPAARSEDGRILSDREEEEEEEEEAEEALEAAEQRSRAKQISPELSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAGTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLINGQCGYVLKPAYLRQLNTTFDPECPGPPRTTLAIQVLTAQQLPKLNAEKPSSIVDPLVRVEIHGVPEDCAQKETDYVLNNGFNPCWEQTLQFRLRAPELVLVRFVVEDYDTTSPNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLAPATLFVHIRIQNS
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. Regulates neurite outgrowth through the inhibition of RhoA/Rho kinase signaling (PubMed:21187285). {ECO:0000269|PubMed:16314520, ECO:0000269|PubMed:21187285}.
uniprot
proteins
mass_dalton
88607
uniprot
proteins
mutagenesis
MUTAGEN 393; /note="H->A: Loss of phosphatidylinositol 4,5-bisphosphate hydrolyzing activity. In neurons, generates supernumerary protrusions."; /evidence="ECO:0000269|PubMed:21187285
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16314520
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21187285
uniprot
proteins
sequence_length
785
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8N3E9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N3E9}. Cytoplasm {ECO:0000250|UniProtKB:Q8N3E9}. Cleavage furrow {ECO:0000250|UniProtKB:Q8N3E9}. Note=Localizes at the cleavage furrow during cytokinesis. 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). The PS selectivity governs its specific calcium-dependent subcellular targeting to the plasma membrane. {ECO:0000250|UniProtKB:Q8N3E9}.
uniprot
proteins