NAPEP_RAT
ID NAPEP_RAT Reviewed; 396 AA.
AC Q769K2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D;
DE Short=N-acyl phosphatidylethanolamine phospholipase D;
DE Short=NAPE-PLD {ECO:0000303|PubMed:16527816};
DE Short=NAPE-hydrolyzing phospholipase D;
DE EC=3.1.4.54 {ECO:0000269|PubMed:16527816};
GN Name=Napepld;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 103-114 AND 368-379,
RP SUBCELLULAR LOCATION, SUBUNIT, AND FUNCTION.
RX PubMed=14634025; DOI=10.1074/jbc.m306642200;
RA Okamoto Y., Morishita J., Tsuboi K., Tonai T., Ueda N.;
RT "Molecular characterization of a phospholipase D generating anandamide and
RT its congeners.";
RL J. Biol. Chem. 279:5298-5305(2004).
RN [2]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBUNIT, POTENTIAL ZINC-BINDING
RP SITES, AND MUTAGENESIS OF ASP-147; CYS-170; HIS-185; HIS-187; ASP-189;
RP HIS-190; LEU-207; CYS-222; CYS-224; CYS-237; HIS-253; CYS-255; ASP-284;
RP CYS-288; HIS-321; HIS-331; HIS-343; HIS-353 AND HIS-380.
RX PubMed=16527816; DOI=10.1074/jbc.m512359200;
RA Wang J., Okamoto Y., Morishita J., Tsuboi K., Miyatake A., Ueda N.;
RT "Functional analysis of the purified anandamide-generating phospholipase D
RT as a member of the metallo-beta-lactamase family.";
RL J. Biol. Chem. 281:12325-12335(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=17655883; DOI=10.1016/j.neuropharm.2007.06.001;
RA Wang J., Okamoto Y., Tsuboi K., Ueda N.;
RT "The stimulatory effect of phosphatidylethanolamine on N-
RT acylphosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD).";
RL Neuropharmacology 54:8-15(2008).
CC -!- FUNCTION: D-type phospholipase that hydrolyzes N-acyl-
CC phosphatidylethanolamines (NAPEs) to produce bioactive N-
CC acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic
CC acid (PubMed:14634025, PubMed:16527816, PubMed:17655883). Cleaves the
CC terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs,
CC primarily playing a role in the generation of long-chain saturated and
CC monounsaturated NAEs in the brain (By similarity). May control NAPE
CC homeostasis in dopaminergic neuron membranes and regulate neuron
CC survival, partly through RAC1 activation (By similarity). As a
CC regulator of lipid metabolism in the adipose tissue, mediates the
CC crosstalk between adipocytes, gut microbiota and immune cells to
CC control body temperature and weight. In particular, regulates energy
CC homeostasis by promoting cold-induced brown or beige adipocyte
CC differentiation program to generate heat from fatty acids and glucose.
CC Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (By
CC similarity). {ECO:0000250|UniProtKB:Q8BH82,
CC ECO:0000269|PubMed:14634025, ECO:0000269|PubMed:16527816,
CC ECO:0000269|PubMed:17655883}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a
CC 1,2-diacyl-sn-glycero-3-phosphate + an N-acylethanolamine + H(+);
CC Xref=Rhea:RHEA:33159, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52640, ChEBI:CHEBI:58608, ChEBI:CHEBI:62537; EC=3.1.4.54;
CC Evidence={ECO:0000269|PubMed:16527816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33160;
CC Evidence={ECO:0000305|PubMed:16527816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-butanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-butanoyl
CC ethanolamine; Xref=Rhea:RHEA:45620, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85298,
CC ChEBI:CHEBI:85304; Evidence={ECO:0000269|PubMed:16527816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45621;
CC Evidence={ECO:0000305|PubMed:16527816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-hexanoyl
CC ethanolamine; Xref=Rhea:RHEA:45616, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85297,
CC ChEBI:CHEBI:85303; Evidence={ECO:0000269|PubMed:16527816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45617;
CC Evidence={ECO:0000305|PubMed:16527816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-octanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-octanoyl
CC ethanolamine; Xref=Rhea:RHEA:45612, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85296,
CC ChEBI:CHEBI:85302; Evidence={ECO:0000269|PubMed:16527816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45613;
CC Evidence={ECO:0000305|PubMed:16527816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-decanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-decanoyl
CC ethanolamine; Xref=Rhea:RHEA:45608, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85295,
CC ChEBI:CHEBI:85301; Evidence={ECO:0000269|PubMed:16527816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45609;
CC Evidence={ECO:0000305|PubMed:16527816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-dodecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC + H(+) + N-dodecanoylethanolamine; Xref=Rhea:RHEA:45556,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546,
CC ChEBI:CHEBI:85263, ChEBI:CHEBI:85294;
CC Evidence={ECO:0000269|PubMed:16527816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45557;
CC Evidence={ECO:0000305|PubMed:16527816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-tetradecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC + H(+) + N-tetradecanoylethanolamine; Xref=Rhea:RHEA:45552,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546,
CC ChEBI:CHEBI:85262, ChEBI:CHEBI:85293;
CC Evidence={ECO:0000269|PubMed:16527816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45553;
CC Evidence={ECO:0000305|PubMed:16527816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC + H(+) + N-hexadecanoylethanolamine; Xref=Rhea:RHEA:45540,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71464,
CC ChEBI:CHEBI:74546, ChEBI:CHEBI:78097;
CC Evidence={ECO:0000269|PubMed:16527816, ECO:0000269|PubMed:17655883};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45541;
CC Evidence={ECO:0000305|PubMed:16527816, ECO:0000305|PubMed:17655883};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-
CC hexadecanoylethanolamine; Xref=Rhea:RHEA:45596, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:71464, ChEBI:CHEBI:72860,
CC ChEBI:CHEBI:85334; Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45597;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-octadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC + H(+) + N-octadecanoyl ethanolamine; Xref=Rhea:RHEA:45536,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546,
CC ChEBI:CHEBI:85292, ChEBI:CHEBI:85299;
CC Evidence={ECO:0000269|PubMed:16527816, ECO:0000269|PubMed:17655883};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45537;
CC Evidence={ECO:0000305|PubMed:16527816, ECO:0000305|PubMed:17655883};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1,2-tri-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC + H(+) + N-(9Z-octadecenoyl) ethanolamine; Xref=Rhea:RHEA:45532,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71466,
CC ChEBI:CHEBI:74546, ChEBI:CHEBI:85291;
CC Evidence={ECO:0000269|PubMed:16527816, ECO:0000269|PubMed:17655883};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45533;
CC Evidence={ECO:0000305|PubMed:16527816, ECO:0000305|PubMed:17655883};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-diacyl-sn-
CC glycero-3-phosphoethanolamine = a 1,2-diacyl-sn-glycero-3-phosphate +
CC H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine;
CC Xref=Rhea:RHEA:56548, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58608, ChEBI:CHEBI:140532;
CC Evidence={ECO:0000250|UniProtKB:Q6IQ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56549;
CC Evidence={ECO:0000250|UniProtKB:Q6IQ20};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-ethanolamine; Xref=Rhea:RHEA:45528,
CC ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:74546, ChEBI:CHEBI:85277;
CC Evidence={ECO:0000269|PubMed:16527816, ECO:0000269|PubMed:17655883};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45529;
CC Evidence={ECO:0000305|PubMed:16527816, ECO:0000305|PubMed:17655883};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC N-hexadecanoyl-ethanolamine + H2O = 1-O-(1Z-octadecenoyl)-2-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-
CC hexadecanoylethanolamine; Xref=Rhea:RHEA:56464, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:71464, ChEBI:CHEBI:138663,
CC ChEBI:CHEBI:140452; Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56465;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-
CC sn-glycero-3-phosphate + an N-acylethanolamine + H(+);
CC Xref=Rhea:RHEA:53164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52640, ChEBI:CHEBI:57970, ChEBI:CHEBI:85216;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53165;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine = 1-
CC hexadecanoyl-sn-glycero-3-phosphate + H(+) + N-
CC hexadecanoylethanolamine; Xref=Rhea:RHEA:45592, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:71464,
CC ChEBI:CHEBI:85335; Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45593;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-
CC sn-glycero-3-phosphoethanolamine = 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine;
CC Xref=Rhea:RHEA:45544, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:74544, ChEBI:CHEBI:85223;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45545;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:16527816};
CC Note=Binds 2 zinc divalent cations per subunit.
CC {ECO:0000250|UniProtKB:Q6IQ20};
CC -!- ACTIVITY REGULATION: Activated by divalent cations (PubMed:17655883).
CC Activated by bile acids (By similarity). Activated by membrane
CC phospholipids such as phosphatidylethanolamines. Inhibited by
CC cardiolipins (PubMed:17655883). {ECO:0000250|UniProtKB:Q6IQ20,
CC ECO:0000269|PubMed:17655883}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 uM for N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine (in the presence of calcium ions)
CC {ECO:0000269|PubMed:17655883};
CC KM=1.7 uM for N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine (in the presence of calcium ions and
CC phosphatidylethanolamine) {ECO:0000269|PubMed:17655883};
CC Vmax=790.6 nmol/min/mg enzyme toward N-hexadecanoyl-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine (in the presence of
CC calcium ions) {ECO:0000269|PubMed:17655883};
CC Vmax=1263 nmol/min/mg enzyme toward N-hexadecanoyl-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine (in the presence of
CC calcium ions and phosphatidylethanolamine)
CC {ECO:0000269|PubMed:17655883};
CC -!- SUBUNIT: Homodimer. Bile acids promote the assembly of inactive
CC monomers into an active dimer and enable catalysis.
CC {ECO:0000250|UniProtKB:Q6IQ20}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the
CC cellular membranes likely through interaction with membrane
CC phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in brain,
CC kidney and testis (at protein level). Expressed in adipose tissue (at
CC protein level). {ECO:0000250|UniProtKB:Q8BH82}.
CC -!- SIMILARITY: Belongs to the NAPE-PLD family. {ECO:0000305}.
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DR EMBL; AB112351; BAD02398.1; -; mRNA.
DR RefSeq; NP_955413.1; NM_199381.1.
DR RefSeq; XP_006235973.1; XM_006235911.3.
DR RefSeq; XP_008760861.1; XM_008762639.2.
DR RefSeq; XP_017448006.1; XM_017592517.1.
DR AlphaFoldDB; Q769K2; -.
DR SMR; Q769K2; -.
DR STRING; 10116.ENSRNOP00000015322; -.
DR SwissLipids; SLP:000001131; -.
DR iPTMnet; Q769K2; -.
DR PhosphoSitePlus; Q769K2; -.
DR PaxDb; Q769K2; -.
DR PRIDE; Q769K2; -.
DR Ensembl; ENSRNOT00000116230; ENSRNOP00000082705; ENSRNOG00000011363.
DR GeneID; 296757; -.
DR KEGG; rno:296757; -.
DR CTD; 222236; -.
DR RGD; 735197; Napepld.
DR eggNOG; KOG3798; Eukaryota.
DR GeneTree; ENSGT00390000017990; -.
DR InParanoid; Q769K2; -.
DR OMA; QHWTRRT; -.
DR OrthoDB; 1194556at2759; -.
DR PhylomeDB; Q769K2; -.
DR BRENDA; 3.1.4.54; 5301.
DR PRO; PR:Q769K2; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000011363; Expressed in heart and 18 other tissues.
DR ExpressionAtlas; Q769K2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0032052; F:bile acid binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0102200; F:N-acetylphosphatidylethanolamine-hydrolysing phospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0048874; P:host-mediated regulation of intestinal microbiota composition; ISS:UniProtKB.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; ISO:RGD.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:1903999; P:negative regulation of eating behavior; IMP:RGD.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:RGD.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0035900; P:response to isolation stress; IEP:RGD.
DR GO; GO:0001659; P:temperature homeostasis; ISS:UniProtKB.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR024884; NAPE-PLD.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR PIRSF; PIRSF038896; NAPE-PLD; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endosome; Golgi apparatus;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW Nucleus; Phospholipid degradation; Phospholipid metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..396
FT /note="N-acyl-phosphatidylethanolamine-hydrolyzing
FT phospholipase D"
FT /id="PRO_0000318162"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 188
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 256
FT /ligand="deoxycholate"
FT /ligand_id="ChEBI:CHEBI:23614"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 321
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 348
FT /ligand="deoxycholate"
FT /ligand_id="ChEBI:CHEBI:23614"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT MUTAGEN 147
FT /note="D->N: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 170
FT /note="C->S: Small decrease in activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 185
FT /note="H->N: <1% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 187
FT /note="H->N: <1% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 189
FT /note="D->N: <1% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 190
FT /note="H->N: <1% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 207
FT /note="L->F: <5% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 222
FT /note="C->S: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 224
FT /note="C->S: Considerable decrease in activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 237
FT /note="C->S: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 253
FT /note="H->N: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 255
FT /note="C->S: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 284
FT /note="D->N: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 288
FT /note="C->S: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 321
FT /note="H->N: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 331
FT /note="H->N: 4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 343
FT /note="H->N: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 353
FT /note="H->N: No effect on activity."
FT /evidence="ECO:0000269|PubMed:16527816"
FT MUTAGEN 380
FT /note="H->R: <5% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16527816"
SQ SEQUENCE 396 AA; 45723 MW; 57AD6EC8B2C7363F CRC64;
MDENENSQSP APSHQYPKET LRKRQNSVQN SGGSESSRLS RKSFKLDYRL EEDVTKSKKG
KDGRFVNPWP TWKNVSIPNV LRWLIMEKDH SSVPGSKEEL DKELPVLKPY FISDPEEAGV
REAGLRVTWL GHATLMVEMD ELILLTDPMF SSRASPSQYM GPKRFRRPPC TISELPPIDA
VLISHNHYDH LDYGSVLALN ERFGSELRWF VPLGLLDWMQ KCGCENVIEL DWWEENCVPG
HDKVTFVFTP SQHWCKRTLL DDNKVLWGSW SVLGPWNRFF FAGDTGYCPA FEEIGKRFGP
FDLAAIPIGA YEPRWFMKYQ HADPEDAVRI HIDVQAKRSV AIHWGTFALA NEHYLEPPVK
LNEALERYGL KSEDFFILKH GESRYLNTDD KAFEET
