Pld1
entrez
25096
canonical
uniprot
P70496
canonical
ensembl
ENSRNOG00000028156
resolver
ensp
ENSRNOP00000034466
resolver
ensp
ENSRNOP00000035045
resolver
ensp
ENSRNOP00000106851
resolver
enst
ENSRNOT00000039296
resolver
genesymbol
Pld1
resolver
uniprot
F1LMG4
resolver
uniprot
O08959
resolver
uniprot
O35856
resolver
uniprot
O54765
resolver
uniprot
P70497
resolver
uniprot
Q9QWJ6
resolver
uniprot_entry
F1LMG4_RAT
resolver
uniprot_entry
PLD1_RAT
resolver
uniprot_sec
O08959
resolver
uniprot_sec
O35856
resolver
uniprot_sec
O54765
resolver
uniprot_sec
P70497
resolver
uniprot_sec
Q9QWJ6
resolver
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
MSLRSEARVNTSTLQKIAADMSNLIENLDTRELHFEGEEVEYDASPGDPTAQEACIPFSSIYNTQGFKEPNIQIYLSGCPVKAQVLEVERFTSTSRMPSVNLYTIELTHGEFTWQVKRKFKHFQEFHRELLKYKAFIRIPIPTKRHTFRRQNVKEEPREMPSLPRSSENAIQEEQFFGRRKQLEDYLTKILKMPMYRNYHATTEFLDVSQLSFIHDLGPKGLEGMIMKRSGGHRIPGVNCCGHGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRIKVGKKETETKYGLRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTDFLKDHRFGSYAAVHENILAKWYVNAKGYFEDIANAMEGATEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGQSLGSLTAASVESMESLSLKDKHQSHKNEPVLKSVNDTDMKLKGIGKSRKFSKFSLYRQLHRRNLHNSDSISSVDSASSYFNHYRSHQNLIHGIKPHLKLFRPSSESEQGLTRHSADTGSIRSVQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIGSVVHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLLPKSQATAHELRYQVPGAVHAKAQLLRSAADWSAGIKHHEESIHAAYTHVIENSKHYIYIENQFFISCADDKVVFNKVGNAIAQRILKAHREGQRYRVYIVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGESSILEQLKPELGNKWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFAQGLRLECFRLVLGYLSDPSEDIQDPVSDKFFKEIWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPILAKEDRLRAEEELRKIRGFLVQFPFYFLSEENLLPSVGTKEAIVPMEVWT
uniprot
proteins
ec_number
3.1.4.4
uniprot
proteins
function
FUNCTION: Function as phospholipase selective for phosphatidylcholine (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q13393, ECO:0000250|UniProtKB:Q9Z280}.
uniprot
proteins
mass_dalton
123814
uniprot
proteins
mutagenesis
MUTAGEN 240; /note="C->A: Abolishes palmitoylation and weakens membrane association; when associated with A-241."; /evidence="ECO:0000269|PubMed:11121416"; MUTAGEN 241; /note="C->A: Abolishes palmitoylation and weakens membrane association; when associated with A-240."; /evidence="ECO:0000269|PubMed:11121416
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and threonine residues. {ECO:0000269|PubMed:11121416}.; PTM: It is uncertain whether palmitoylation is on Cys-240 and/or Cys-241. Palmitoylation is required prior to phosphorylation. {ECO:0000269|PubMed:11121416}.
uniprot
proteins
protein_family
Phospholipase D family
uniprot
proteins
pubmed
11121416
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
8753790
uniprot
proteins
pubmed
9361006
uniprot
proteins
pubmed
9445394
uniprot
proteins
pubmed
9533024
uniprot
proteins
sequence_length
1074
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Z280}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}.
uniprot
proteins