NAPE2_CAEEL
ID NAPE2_CAEEL Reviewed; 355 AA.
AC Q965X9; Q8MXT4; Q965X8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D 2;
DE Short=NAPE-2 {ECO:0000303|PubMed:25423491};
DE EC=3.1.4.54 {ECO:0000269|PubMed:25423491};
GN Name=nape-2 {ECO:0000312|EMBL:CCD74039.1,
GN ECO:0000312|WormBase:Y37E11AR.3a};
GN ORFNames=Y37E11AR.3 {ECO:0000312|WormBase:Y37E11AR.3a};
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, 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. NAEs are bioactive lipids that are involved in diverse
CC physiological processes such as growth and lifespan.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=a;
CC IsoId=Q965X9-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q965X9-2; Sequence=VSP_061049;
CC Name=c;
CC IsoId=Q965X9-3; Sequence=VSP_061050;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the pharynx, also highly
CC expressed in the dorsal and ventral nerve cords, as well as in the
CC vulval muscles of hermaphrodites. {ECO:0000269|PubMed:25423491}.
CC -!- DISRUPTION PHENOTYPE: No strong phenotype in the nape-2 deletion
CC mutant, however its overexpression alters growth and lifespan when
CC grown at 15 degrees Celsius compared to 25 degrees Celsius.
CC {ECO:0000269|PubMed:25423491}.
CC -!- SIMILARITY: Belongs to the NAPE-PLD family. {ECO:0000305}.
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DR EMBL; BX284604; CCD74039.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD74040.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD74041.1; -; Genomic_DNA.
DR RefSeq; NP_500406.1; NM_068005.3.
DR RefSeq; NP_500407.1; NM_068006.4.
DR RefSeq; NP_741361.1; NM_171307.3. [Q965X9-3]
DR AlphaFoldDB; Q965X9; -.
DR SMR; Q965X9; -.
DR STRING; 6239.Y37E11AR.3b; -.
DR SwissLipids; SLP:000001664; -.
DR EPD; Q965X9; -.
DR PeptideAtlas; Q965X9; -.
DR EnsemblMetazoa; Y37E11AR.3a.1; Y37E11AR.3a.1; WBGene00021370. [Q965X9-1]
DR EnsemblMetazoa; Y37E11AR.3a.2; Y37E11AR.3a.2; WBGene00021370. [Q965X9-1]
DR EnsemblMetazoa; Y37E11AR.3a.3; Y37E11AR.3a.3; WBGene00021370. [Q965X9-1]
DR EnsemblMetazoa; Y37E11AR.3a.4; Y37E11AR.3a.4; WBGene00021370. [Q965X9-1]
DR EnsemblMetazoa; Y37E11AR.3b.1; Y37E11AR.3b.1; WBGene00021370. [Q965X9-2]
DR EnsemblMetazoa; Y37E11AR.3c.1; Y37E11AR.3c.1; WBGene00021370. [Q965X9-3]
DR GeneID; 177136; -.
DR UCSC; Y37E11AR.3b; c. elegans.
DR CTD; 177136; -.
DR WormBase; Y37E11AR.3a; CE27604; WBGene00021370; nape-2.
DR WormBase; Y37E11AR.3b; CE28519; WBGene00021370; nape-2.
DR WormBase; Y37E11AR.3c; CE31637; WBGene00021370; nape-2.
DR eggNOG; KOG3798; Eukaryota.
DR GeneTree; ENSGT00940000173847; -.
DR HOGENOM; CLU_020884_2_1_1; -.
DR OMA; HQPPISL; -.
DR OrthoDB; 1194556at2759; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00021370; Expressed in adult organism and 3 other tissues.
DR ExpressionAtlas; Q965X9; baseline and differential.
DR GO; GO:0043005; C:neuron projection; 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: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 Alternative initiation; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Phospholipid degradation; Phospholipid metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..355
FT /note="N-acyl-phosphatidylethanolamine-hydrolyzing
FT phospholipase D 2"
FT /id="PRO_0000452743"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
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 145
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 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 285
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 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT VAR_SEQ 1
FT /note="M -> MRTSFRKRFYRLVACAAGGVVM (in isoform b)"
FT /id="VSP_061049"
FT VAR_SEQ 1
FT /note="M -> MFVPVVMTIVLLLYATSDSVVM (in isoform c)"
FT /id="VSP_061050"
SQ SEQUENCE 355 AA; 40265 MW; 41E96A9ACB8061A7 CRC64;
MSAPTTSSST DEDFAKPVKN GKTFANPKSF TNWGGIPGIS DGFKFAFTET NHENVPCDKK
ILDVEIPVHN ITADDFHSES DLFATWLGHA TVLVDLEGVK FVTDPVWADR ASFTSFAGPK
RYRPPPMKLE DLPDLDFAVV SHDHYDHLDA DAVKKITDRN PQIKWFVPLG MKKWMEGQGI
GVDGSSTAVT ELNWGESSEF VKNGKTYTIW CLPAQHWGQR GLFDRNHRLW SGWAVIGENR
RFYYSGDTGH CDGEFKKFGE KLGPFDLAAI PIGAYEPRWF MKSQHINPEE AIEVHKLIRA
KNSIGIHWGT YHMGSTEYYL EPRDKLKELM DAREDLKNTS FVTIEMGRIW EASDQ
