NAPEPLD
entrez
222236
canonical
uniprot
Q6IQ20
canonical
ensembl
ENSG00000161048
resolver
ensembl
ENSG00000275723
resolver
ensp
ENSP00000340093
resolver
ensp
ENSP00000392775
resolver
ensp
ENSP00000407112
resolver
ensp
ENSP00000412376
resolver
ensp
ENSP00000419188
resolver
ensp
ENSP00000481285
resolver
ensp
ENSP00000482162
resolver
ensp
ENSP00000487770
resolver
ensp
ENSP00000488504
resolver
ensp
ENSP00000488648
resolver
ensp
ENSP00000543925
resolver
ensp
ENSP00000543927
resolver
ensp
ENSP00000543928
resolver
ensp
ENSP00000543929
resolver
ensp
ENSP00000543931
resolver
ensp
ENSP00000543932
resolver
ensp
ENSP00000543933
resolver
ensp
ENSP00000543934
resolver
ensp
ENSP00000635875
resolver
ensp
ENSP00000635876
resolver
ensp
ENSP00000635877
resolver
ensp
ENSP00000646559
resolver
enst
ENST00000341533
resolver
enst
ENST00000417955
resolver
enst
ENST00000422589
resolver
enst
ENST00000427257
resolver
enst
ENST00000465647
resolver
enst
ENST00000611100
resolver
enst
ENST00000622712
resolver
enst
ENST00000632159
resolver
enst
ENST00000632703
resolver
enst
ENST00000633783
resolver
enst
ENST00000873866
resolver
enst
ENST00000873868
resolver
enst
ENST00000873869
resolver
enst
ENST00000873870
resolver
enst
ENST00000873872
resolver
enst
ENST00000873873
resolver
enst
ENST00000873874
resolver
enst
ENST00000873875
resolver
enst
ENST00000965816
resolver
enst
ENST00000965817
resolver
enst
ENST00000965818
resolver
genesymbol
NAPEPLD
resolver
genesymbol_syn
C7orf18
resolver
hgnc
HGNC:21683
resolver
uniprot
Q5CZ87
resolver
uniprot
Q769K1
resolver
uniprot_entry
NAPEP_HUMAN
resolver
uniprot_sec
Q5CZ87
resolver
uniprot_sec
Q769K1
resolver
activity_regulation
ACTIVITY REGULATION: Activated by divalent cations (PubMed:16527816). Activated by bile acids and their conjugates, except for lithocholic acid which is rather inhibitory. Binding of deoxycholic acid favors the selective release of anandamide and likely other unsatured long FAEs (PubMed:25684574, PubMed:27571266). Inhibited by phosphatidylethanolamines (PubMed:25684574). {ECO:0000269|PubMed:16527816, ECO:0000269|PubMed:25684574, ECO:0000269|PubMed:27571266}.
uniprot
proteins
amino_acid_sequence
MDENESNQSLMTSSQYPKEAVRKRQNSARNSGASDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNPSIPNVLRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGVREAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEHYLEPPVKLNEALERYGLNAEDFFVLKHGESRYLNNDDENF
uniprot
proteins
ec_number
3.1.4.54
uniprot
proteins
function
FUNCTION: D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (PubMed:14634025, PubMed:16527816, PubMed:25684574, PubMed:27571266). Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain (By similarity). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (By similarity). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (By similarity). {ECO:0000250|UniProtKB:Q8BH82, ECO:0000269|PubMed:14634025, ECO:0000269|PubMed:16527816, ECO:0000269|PubMed:25684574, ECO:0000269|PubMed:27571266}.
uniprot
proteins
mass_dalton
45596
uniprot
proteins
mutagenesis
MUTAGEN 158; /note="Q->S: Impairs homodimerization resulting in loss of activity; when associated with S-159."; /evidence="ECO:0000269|PubMed:25684574"; MUTAGEN 159; /note="Y->S: Impairs homodimerization resulting in loss of activity; when associated with S-158."; /evidence="ECO:0000269|PubMed:25684574"; MUTAGEN 207; /note="L->F: Loss of activity."; /evidence="ECO:0000269|PubMed:16527816"; MUTAGEN 257; /note="R->A: Impairs binding to bile acids resulting in loss of activity."; /evidence="ECO:0000269|PubMed:25684574"; MUTAGEN 380; /note="H->R: Loss of activity."; /evidence="ECO:0000269|PubMed:16527816
uniprot
proteins
protein_family
NAPE-PLD family
uniprot
proteins
pubmed
14634025
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15820312
uniprot
proteins
pubmed
16527816
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
25684574
uniprot
proteins
pubmed
27571266
uniprot
proteins
sequence_length
393
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:25684574}; Peripheral membrane protein {ECO:0000305|PubMed:25684574}. Early endosome membrane {ECO:0000269|PubMed:25684574}; Peripheral membrane protein {ECO:0000305|PubMed:25684574}. Nucleus envelope {ECO:0000269|PubMed:25684574}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25684574}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000269|PubMed:25684574}.
uniprot
proteins