Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D

Gene

NAPEPLD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce N-acylethanolamines (NAEs) and phosphatidic acid. Responsible for the generation of anandamide (N-arachidonoylethanolamine), the ligand of cannabinoid and vanilloid receptors (By similarity).By similarity

Catalytic activityi

An N-acylphosphatidylethanolamine + H2O = an N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate.2 Publications

Cofactori

Zn2+By similarityNote: Binds 1 or 2 zinc ions per subunit.By similarity

Enzyme regulationi

Activity is stimulated by divalent cations.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi185 – 1851Zinc 1Sequence analysis
Metal bindingi187 – 1871Zinc 1Sequence analysis
Metal bindingi189 – 1891Zinc 2Sequence analysis
Metal bindingi190 – 1901Zinc 2Sequence analysis
Metal bindingi253 – 2531Zinc 1Sequence analysis
Metal bindingi343 – 3431Zinc 2Sequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000161048-MONOMER.
BRENDAi3.1.4.54. 2681.
ReactomeiR-HSA-2466712. Biosynthesis of A2E, implicated in retinal degradation.

Chemistry

SwissLipidsiSLP:000001132.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (EC:3.1.4.54)
Short name:
N-acyl phosphatidylethanolamine phospholipase D
Short name:
NAPE-PLD
Short name:
NAPE-hydrolyzing phospholipase D
Gene namesi
Name:NAPEPLD
Synonyms:C7orf18
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:21683. NAPEPLD.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • photoreceptor outer segment membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi152 – 1521S → A: Almost no change in activity. 1 Publication
Mutagenesisi207 – 2071L → F: Loss of activity. 1 Publication
Mutagenesisi380 – 3801H → R: Loss of activity. 1 Publication
Mutagenesisi389 – 3891D → N: Almost no change in activity. 1 Publication

Organism-specific databases

PharmGKBiPA162396960.

Polymorphism and mutation databases

BioMutaiNAPEPLD.
DMDMi167016292.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase DPRO_0000318159Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ6IQ20.
PaxDbiQ6IQ20.
PeptideAtlasiQ6IQ20.
PRIDEiQ6IQ20.

PTM databases

iPTMnetiQ6IQ20.
PhosphoSiteiQ6IQ20.

Expressioni

Gene expression databases

BgeeiQ6IQ20.
CleanExiHS_NAPEPLD.
ExpressionAtlasiQ6IQ20. baseline and differential.
GenevisibleiQ6IQ20. HS.

Organism-specific databases

HPAiHPA019832.
HPA024338.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi128793. 1 interaction.
DIPiDIP-61398N.
STRINGi9606.ENSP00000340093.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi65 – 684Combined sources
Helixi97 – 1037Combined sources
Turni110 – 1134Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi126 – 1294Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi158 – 1614Combined sources
Beta strandi178 – 1825Combined sources
Turni188 – 1903Combined sources
Helixi193 – 20210Combined sources
Beta strandi207 – 2126Combined sources
Helixi216 – 2216Combined sources
Beta strandi226 – 2305Combined sources
Beta strandi235 – 2384Combined sources
Beta strandi241 – 2499Combined sources
Beta strandi257 – 2604Combined sources
Beta strandi269 – 2735Combined sources
Beta strandi278 – 2814Combined sources
Helixi291 – 2977Combined sources
Beta strandi301 – 3077Combined sources
Helixi314 – 3174Combined sources
Turni318 – 3203Combined sources
Helixi324 – 33310Combined sources
Beta strandi339 – 3479Combined sources
Beta strandi350 – 3523Combined sources
Helixi356 – 36813Combined sources
Turni372 – 3743Combined sources
Beta strandi383 – 3853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QN9X-ray2.65A/B1-393[»]
ProteinModelPortaliQ6IQ20.
SMRiQ6IQ20. Positions 57-389.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NAPE-PLD family.Curated

Phylogenomic databases

eggNOGiKOG3798. Eukaryota.
COG2220. LUCA.
GeneTreeiENSGT00390000017990.
HOGENOMiHOG000267495.
HOVERGENiHBG054649.
InParanoidiQ6IQ20.
KOiK13985.
OMAiWGSWSVL.
OrthoDBiEOG7Z95MB.
PhylomeDBiQ6IQ20.
TreeFamiTF313520.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Metallo-B-lactamas.
IPR024884. NAPE-PLD.
[Graphical view]
PfamiPF12706. Lactamase_B_2. 1 hit.
[Graphical view]
PIRSFiPIRSF038896. NAPE-PLD. 1 hit.
SUPFAMiSSF56281. SSF56281. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6IQ20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDENESNQSL MTSSQYPKEA VRKRQNSARN SGASDSSRFS RKSFKLDYRL
60 70 80 90 100
EEDVTKSKKG KDGRFVNPWP TWKNPSIPNV LRWLIMEKDH SSVPSSKEEL
110 120 130 140 150
DKELPVLKPY FITNPEEAGV REAGLRVTWL GHATVMVEMD ELIFLTDPIF
160 170 180 190 200
SSRASPSQYM GPKRFRRSPC TISELPPIDA VLISHNHYDH LDYNSVIALN
210 220 230 240 250
ERFGNELRWF VPLGLLDWMQ KCGCENVIEL DWWEENCVPG HDKVTFVFTP
260 270 280 290 300
SQHWCKRTLM DDNKVLWGSW SVLGPWNRFF FAGDTGYCPA FEEIGKRFGP
310 320 330 340 350
FDLAAIPIGA YEPRWFMKYQ HVDPEEAVRI HTDVQTKKSM AIHWGTFALA
360 370 380 390
NEHYLEPPVK LNEALERYGL NAEDFFVLKH GESRYLNNDD ENF
Length:393
Mass (Da):45,596
Last modified:February 5, 2008 - v2
Checksum:i5CE3114CC557B698
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 2811Missing in CAI56779 (PubMed:17974005).Curated
Sequence conflicti371 – 3711N → Y in CAI56779 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti152 – 1521S → A.
Corresponds to variant rs12540583 [ dbSNP | Ensembl ].
VAR_038695
Natural varianti389 – 3891D → N.3 Publications
Corresponds to variant rs3181009 [ dbSNP | Ensembl ].
VAR_038694

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY357337 mRNA. Translation: AAR13673.1.
AB112352 mRNA. Translation: BAD02399.1.
CR936639 mRNA. Translation: CAI56779.1.
CH471070 Genomic DNA. Translation: EAW83314.1.
BC071604 mRNA. Translation: AAH71604.1.
CCDSiCCDS5729.1.
RefSeqiNP_001116310.1. NM_001122838.1.
NP_945341.3. NM_198990.4.
XP_005250271.2. XM_005250214.3.
XP_005250272.1. XM_005250215.1.
XP_005250275.1. XM_005250218.1.
XP_006725115.2. XM_006725052.2.
XP_006725116.2. XM_006725053.2.
XP_006725117.1. XM_006725054.1.
XP_006725119.1. XM_006725056.1.
XP_011514235.1. XM_011515933.1.
UniGeneiHs.324271.

Genome annotation databases

EnsembliENST00000341533; ENSP00000340093; ENSG00000161048.
ENST00000417955; ENSP00000407112; ENSG00000161048.
ENST00000422589; ENSP00000412376; ENSG00000161048.
ENST00000427257; ENSP00000392775; ENSG00000161048.
ENST00000465647; ENSP00000419188; ENSG00000161048.
ENST00000611100; ENSP00000482162; ENSG00000275723.
ENST00000622712; ENSP00000481285; ENSG00000275723.
ENST00000632159; ENSP00000488504; ENSG00000275723.
ENST00000632703; ENSP00000488648; ENSG00000275723.
ENST00000633783; ENSP00000487770; ENSG00000275723.
GeneIDi222236.
KEGGihsa:222236.
UCSCiuc003vbc.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

N-acyl phosphatidylethanolamine-specific phospholipase D entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY357337 mRNA. Translation: AAR13673.1.
AB112352 mRNA. Translation: BAD02399.1.
CR936639 mRNA. Translation: CAI56779.1.
CH471070 Genomic DNA. Translation: EAW83314.1.
BC071604 mRNA. Translation: AAH71604.1.
CCDSiCCDS5729.1.
RefSeqiNP_001116310.1. NM_001122838.1.
NP_945341.3. NM_198990.4.
XP_005250271.2. XM_005250214.3.
XP_005250272.1. XM_005250215.1.
XP_005250275.1. XM_005250218.1.
XP_006725115.2. XM_006725052.2.
XP_006725116.2. XM_006725053.2.
XP_006725117.1. XM_006725054.1.
XP_006725119.1. XM_006725056.1.
XP_011514235.1. XM_011515933.1.
UniGeneiHs.324271.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QN9X-ray2.65A/B1-393[»]
ProteinModelPortaliQ6IQ20.
SMRiQ6IQ20. Positions 57-389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128793. 1 interaction.
DIPiDIP-61398N.
STRINGi9606.ENSP00000340093.

Chemistry

SwissLipidsiSLP:000001132.

PTM databases

iPTMnetiQ6IQ20.
PhosphoSiteiQ6IQ20.

Polymorphism and mutation databases

BioMutaiNAPEPLD.
DMDMi167016292.

Proteomic databases

MaxQBiQ6IQ20.
PaxDbiQ6IQ20.
PeptideAtlasiQ6IQ20.
PRIDEiQ6IQ20.

Protocols and materials databases

DNASUi222236.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341533; ENSP00000340093; ENSG00000161048.
ENST00000417955; ENSP00000407112; ENSG00000161048.
ENST00000422589; ENSP00000412376; ENSG00000161048.
ENST00000427257; ENSP00000392775; ENSG00000161048.
ENST00000465647; ENSP00000419188; ENSG00000161048.
ENST00000611100; ENSP00000482162; ENSG00000275723.
ENST00000622712; ENSP00000481285; ENSG00000275723.
ENST00000632159; ENSP00000488504; ENSG00000275723.
ENST00000632703; ENSP00000488648; ENSG00000275723.
ENST00000633783; ENSP00000487770; ENSG00000275723.
GeneIDi222236.
KEGGihsa:222236.
UCSCiuc003vbc.3. human.

Organism-specific databases

CTDi222236.
GeneCardsiNAPEPLD.
HGNCiHGNC:21683. NAPEPLD.
HPAiHPA019832.
HPA024338.
MIMi612334. gene.
neXtProtiNX_Q6IQ20.
PharmGKBiPA162396960.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3798. Eukaryota.
COG2220. LUCA.
GeneTreeiENSGT00390000017990.
HOGENOMiHOG000267495.
HOVERGENiHBG054649.
InParanoidiQ6IQ20.
KOiK13985.
OMAiWGSWSVL.
OrthoDBiEOG7Z95MB.
PhylomeDBiQ6IQ20.
TreeFamiTF313520.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000161048-MONOMER.
BRENDAi3.1.4.54. 2681.
ReactomeiR-HSA-2466712. Biosynthesis of A2E, implicated in retinal degradation.

Miscellaneous databases

ChiTaRSiNAPEPLD. human.
GenomeRNAii222236.
PROiQ6IQ20.
SOURCEiSearch...

Gene expression databases

BgeeiQ6IQ20.
CleanExiHS_NAPEPLD.
ExpressionAtlasiQ6IQ20. baseline and differential.
GenevisibleiQ6IQ20. HS.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Metallo-B-lactamas.
IPR024884. NAPE-PLD.
[Graphical view]
PfamiPF12706. Lactamase_B_2. 1 hit.
[Graphical view]
PIRSFiPIRSF038896. NAPE-PLD. 1 hit.
SUPFAMiSSF56281. SSF56281. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of a phospholipase D generating anandamide and its congeners."
    Okamoto Y., Morishita J., Tsuboi K., Tonai T., Ueda N.
    J. Biol. Chem. 279:5298-5305(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
  2. "Isolation and analysis of candidate myeloid tumor suppressor genes from a commonly deleted segment of 7q22."
    Curtiss N.P., Bonifas J.M., Lauchle J.O., Balkman J.D., Kratz C.P., Emerling B.M., Green E.D., Le Beau M.M., Shannon K.M.
    Genomics 85:600-607(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-389.
    Tissue: Colon carcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-389.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-389.
    Tissue: Brain.
  6. "Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-beta-lactamase family."
    Wang J., Okamoto Y., Morishita J., Tsuboi K., Miyatake A., Ueda N.
    J. Biol. Chem. 281:12325-12335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF SER-152; LEU-207; HIS-380 AND ASP-389.
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNAPEP_HUMAN
AccessioniPrimary (citable) accession number: Q6IQ20
Secondary accession number(s): Q5CZ87, Q769K1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: June 8, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.