Q9Z280
uniprot
Q9Z280
canonical
activity_regulation
ACTIVITY REGULATION: Stimulated by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate, activated by the phosphokinase C-alpha, by the ADP-ribosylation factor-1 (ARF-1), and to a lesser extent by GTP-binding proteins: RHO A, RAC-1 and CDC42. Inhibited by oleate. {ECO:0000250|UniProtKB:Q13393}.
uniprot
proteins
amino_acid_sequence
MSLKSETRVNTSTLQKIAADMSNLIENLDTRELHFEGEEVEYDASPGDPKAQEGCIPFSSIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTSRVPSINLYTIELTHGEFTWQVKRKFKHFQEFHRELLKYKAFIRIPIPTKRHTFRRQNVKEEPREMPSLPRSSENAIQEEQFFGRRKQLEDYLTKILKMPMYRNYHATTEFLDVSQLSFIHDLGPKGLEGMIMKRSGGHRIPGVNCCGHGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRVKVGRKETETKYGLRIDNLSRTLILKCNSYRHARWWGGAIEEFIRKHGADFLKDHRFGSYAALHENTLAKWYVNAKGYFEDIANAMEEASEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYSKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGLSLGSLTAASVESMESLSLKDKHEFHKKEPISKIVDETDMKLKGIGKSRKFSKFSLYRQLHRHHLHNADSISSIDSTSSYFSHCRSHQNLIHGLKPHLKLFHPSSESEQGLTRHSTDTGSIRSVQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIGSVVHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLLPKSQATAHELRYQVPGAVPAKVQLLRSAADWSAGIKHHEESIHAAYIHVIENSKHYIYIENQFFISCADDKVVFNKVGDRIAQRILKAHREGQRYRVYIVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGESSILEQLKPELGNKWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARDLRLECFRLVLGYLSDPSEDLQDPVSDKFFKEIWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPILAKEDALRAEEELRKIRGFLVQFPLYFLSEENLLPSVGTKEAIVPMEVWT
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Pld1 may result in coa which is associated with coat color dilution and white spotting. It is also associated with platelet-storage pool deficiency characterized by decreased levels in serotonin and dense granules.
uniprot
proteins
ec_number
3.1.4.4
uniprot
proteins
function
FUNCTION: Function as phospholipase selectivefor phosphatidylcholine (PubMed:9395408). Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (PubMed:9395408). {ECO:0000269|PubMed:9395408}.
uniprot
proteins
mass_dalton
123969
uniprot
proteins
protein_family
Phospholipase D family
uniprot
proteins
pubmed
9307024
uniprot
proteins
pubmed
9395408
uniprot
proteins
pubmed
9813240
uniprot
proteins
sequence_length
1074
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9395408}. Endoplasmic reticulum membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
uniprot
proteins