Gdpd3
entrez
68616
canonical
uniprot
Q99LY2
canonical
ensembl
ENSMUSG00000030703
resolver
ensp
ENSMUSP00000032944
resolver
enst
ENSMUST00000032944
resolver
genesymbol
Gdpd3
resolver
genesymbol_syn
Gde7
resolver
uniprot
Q9D1C0
resolver
uniprot_entry
GDPD3_MOUSE
resolver
uniprot_sec
Q9D1C0
resolver
activity_regulation
ACTIVITY REGULATION: Lysophospholipase D activity is stimulated by calcium. Loss of lysophospholipase D activity in presence of EDTA. {ECO:0000250|UniProtKB:Q7L5L3}.
uniprot
proteins
amino_acid_sequence
MIPLLYFVLPTLGSYVMLSIFFLRRPHLLHTPRAPVFPIRLAAHRGGSGERLENTMEAVENSMAQRADLLEFDCQLTRDGVVVVSHDKNLSRQSGLNKDVNTLDFEELPLYKEELEIYFSPGHFAHGSDRHMISLEDVFQKFPRTPMCLEVKERNEELIHKVANLTRRFDRNEITIWAAEKSSVMKRCRAANPEMPMAFTIWRSFWILLLYYLGLLPFVSIPEKFFFCFLPTIINRTYFPFRCGWMNQLSATITKWIIMRKSLIRHLQDRGVQVLFWCLNEESDFEVAFSLGANGVMTDYPTALRHYLDKQEEETQPPQPEALSCLSLKK
uniprot
proteins
ec_number
3.1.4.-
uniprot
proteins
function
FUNCTION: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines (PubMed:25528375, PubMed:27637550). Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylcholine (lyso-PC) and N-acylethanolamine lysophospholipids (PubMed:25528375). Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine (PubMed:25528375). {ECO:0000269|PubMed:25528375, ECO:0000269|PubMed:27637550}.
uniprot
proteins
mass_dalton
38488
uniprot
proteins
protein_family
Glycerophosphoryl diester phosphodiesterase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
25528375
uniprot
proteins
pubmed
27637550
uniprot
proteins
sequence_length
330
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25528375}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25528375}; Multi-pass membrane protein {ECO:0000305}. Note=Partially colocalized with CANX (PubMed:25528375). {ECO:0000269|PubMed:25528375}.
uniprot
proteins
transmembrane_region
TRANSMEM 2..22; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 201..221; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins