NAPE1_CAEEL
ID NAPE1_CAEEL Reviewed; 356 AA.
AC Q965X7;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D 1;
DE Short=NAPE-1 {ECO:0000303|PubMed:25423491};
DE EC=3.1.4.54 {ECO:0000269|PubMed:25423491};
GN Name=nape-1 {ECO:0000312|EMBL:CCD74042.1, ECO:0000312|WormBase:Y37E11AR.4};
GN ORFNames=Y37E11AR.4 {ECO:0000312|WormBase:Y37E11AR.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21562563; DOI=10.1038/nature10007;
RA Lucanic M., Held J.M., Vantipalli M.C., Klang I.M., Graham J.B.,
RA Gibson B.W., Lithgow G.J., Gill M.S.;
RT "N-acylethanolamine signalling mediates the effect of diet on lifespan in
RT Caenorhabditis elegans.";
RL Nature 473:226-229(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25423491; DOI=10.1371/journal.pone.0113007;
RA Harrison N., Lone M.A., Kaul T.K., Reis Rodrigues P., Ogungbe I.V.,
RA Gill M.S.;
RT "Characterization of N-acyl phosphatidylethanolamine-specific
RT phospholipase-D isoforms in the nematode Caenorhabditis elegans.";
RL PLoS ONE 9:e113007-e113007(2014).
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:25423491). NAEs are bioactive lipids that are involved in
CC diverse physiological processes such as growth and lifespan
CC (PubMed:21562563, PubMed:25423491). {ECO:0000269|PubMed:21562563,
CC ECO:0000269|PubMed:25423491}.
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:25423491};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33160;
CC Evidence={ECO:0000305|PubMed:25423491};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(N-hexadecanoyl)-
CC ethanolamine + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phosphate + H(+)
CC + N-hexadecanoylethanolamine; Xref=Rhea:RHEA:51408,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71464,
CC ChEBI:CHEBI:72859, ChEBI:CHEBI:134072;
CC Evidence={ECO:0000269|PubMed:25423491};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51409;
CC Evidence={ECO:0000305|PubMed:25423491};
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:25423491};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45529;
CC Evidence={ECO:0000305|PubMed:25423491};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q6IQ20};
CC Note=Binds 2 zinc divalent cations per subunit.
CC {ECO:0000250|UniProtKB:Q6IQ20};
CC -!- TISSUE SPECIFICITY: Expressed in interneurons that are in close
CC proximity to the primary sensory neurons (PubMed:21562563).
CC Predominantly expressed in the pharynx but can also be found in cell
CC bodies of the dorsal and ventral nerve cords (PubMed:25423491).
CC {ECO:0000269|PubMed:21562563, ECO:0000269|PubMed:25423491}.
CC -!- DISRUPTION PHENOTYPE: No strong phenotype in the nape-1 deletion
CC mutant, however its overexpression alters growth and lifespan when
CC grown at 25 degrees Celsius compared to 15 degrees Celsius.
CC {ECO:0000269|PubMed:25423491}.
CC -!- SIMILARITY: Belongs to the NAPE-PLD family. {ECO:0000305}.
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DR EMBL; BX284604; CCD74042.1; -; Genomic_DNA.
DR RefSeq; NP_500408.1; NM_068007.3.
DR AlphaFoldDB; Q965X7; -.
DR SMR; Q965X7; -.
DR STRING; 6239.Y37E11AR.4; -.
DR SwissLipids; SLP:000001663; -.
DR EPD; Q965X7; -.
DR PaxDb; Q965X7; -.
DR PeptideAtlas; Q965X7; -.
DR EnsemblMetazoa; Y37E11AR.4.1; Y37E11AR.4.1; WBGene00021371.
DR GeneID; 177137; -.
DR KEGG; cel:CELE_Y37E11AR.4; -.
DR UCSC; Y37E11AR.4; c. elegans.
DR CTD; 177137; -.
DR WormBase; Y37E11AR.4; CE21545; WBGene00021371; nape-1.
DR eggNOG; KOG3798; Eukaryota.
DR GeneTree; ENSGT00940000173847; -.
DR HOGENOM; CLU_020884_1_1_1; -.
DR InParanoid; Q965X7; -.
DR OMA; RMAPMHW; -.
DR OrthoDB; 1194556at2759; -.
DR PhylomeDB; Q965X7; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00021371; Expressed in larva and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0102200; F:N-acetylphosphatidylethanolamine-hydrolysing phospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IDA:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; IDA:WormBase.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; IBA:GO_Central.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW.
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 Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Phospholipid degradation; Phospholipid metabolism; Reference proteome;
KW Zinc.
FT CHAIN 1..356
FT /note="N-acyl-phosphatidylethanolamine-hydrolyzing
FT phospholipase D 1"
FT /id="PRO_0000452742"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 147
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000255|PIRSR:PIRSR038896-50"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 286
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000255|PIRSR:PIRSR038896-50"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
SQ SEQUENCE 356 AA; 40319 MW; F3EE650FAEE98103 CRC64;
MSLPTTSSPL TNDQEFAKPV RNGKIFENPK SFTNWGGRPG LTNIFKLVLR ETSHENLPSD
KKVLDSTLPV HNITADDFHS ESGLFATWLG HATVLVDLEG VKFVTDPVWA DRASFTSFAG
PKRYRPPPMK LEDLPDLDFA VVSHDHYDHL DADAVKRITN LNPQIKWFVP LGLKKWMKNQ
GIGADGSNTV TELNWGESSE FVKNGKTITI WCLPAQHSGQ RGLSDHNHRL WSGWAVIGEN
RRFYFPGDTG FCDVEFKKIG EKLGPFDLAA IPIGAYEPRW FMKSHHINPD EAVEVHKLVR
ARNSIGIHWG TYPMGTTEYY LEPRDKLKEL MDAREDLKDT SFVTVDMGEI WEASDR
