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Protein

N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D

Gene

Napepld

Organism
Rattus norvegicus (Rat)
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.2 Publications

Catalytic activityi

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

Cofactori

Zn2+1 PublicationNote: Binds 1 or 2 zinc ions per subunit.1 Publication

Enzyme regulationi

Activity is stimulated by divalent cations.1 Publication

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

  • aging Source: RGD
  • negative regulation of eating behavior Source: RGD
  • phospholipid catabolic process Source: UniProtKB-KW
  • phospholipid metabolic process Source: RGD
  • response to isolation stress Source: RGD
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

BRENDAi3.1.4.54. 5301.

Chemistry

SwissLipidsiSLP:000001131.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi735197. Napepld.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • extracellular exosome Source: Ensembl
  • membrane Source: UniProtKB-SubCell
  • membrane-bounded organelle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi147 – 1471D → N: Abolishes activity. 1 Publication
Mutagenesisi170 – 1701C → S: Small decrease in activity. 1 Publication
Mutagenesisi185 – 1851H → N: <1% of wild-type activity. 1 Publication
Mutagenesisi187 – 1871H → N: <1% of wild-type activity. 1 Publication
Mutagenesisi189 – 1891D → N: <1% of wild-type activity. 1 Publication
Mutagenesisi190 – 1901H → N: <1% of wild-type activity. 1 Publication
Mutagenesisi207 – 2071L → F: <5% of wild-type activity. 1 Publication
Mutagenesisi222 – 2221C → S: No effect on activity. 1 Publication
Mutagenesisi224 – 2241C → S: Considerable decrease in activity. 1 Publication
Mutagenesisi237 – 2371C → S: No effect on activity. 1 Publication
Mutagenesisi253 – 2531H → N: Abolishes activity. 1 Publication
Mutagenesisi255 – 2551C → S: No effect on activity. 1 Publication
Mutagenesisi284 – 2841D → N: Abolishes activity. 1 Publication
Mutagenesisi288 – 2881C → S: No effect on activity. 1 Publication
Mutagenesisi321 – 3211H → N: Abolishes activity. 1 Publication
Mutagenesisi331 – 3311H → N: 4% of wild-type activity. 1 Publication
Mutagenesisi343 – 3431H → N: No effect on activity. 1 Publication
Mutagenesisi353 – 3531H → N: No effect on activity. 1 Publication
Mutagenesisi380 – 3801H → R: <5% of wild-type activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase DPRO_0000318162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ769K2.
PRIDEiQ769K2.

PTM databases

iPTMnetiQ769K2.
PhosphoSiteiQ769K2.

Expressioni

Gene expression databases

ExpressionAtlasiQ769K2. baseline.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015322.

Structurei

3D structure databases

ProteinModelPortaliQ769K2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NAPE-PLD family.Curated

Phylogenomic databases

eggNOGiKOG3798. Eukaryota.
COG2220. LUCA.
GeneTreeiENSGT00390000017990.
HOGENOMiHOG000267495.
HOVERGENiHBG054649.
InParanoidiQ769K2.
KOiK13985.
OMAiWGSWSVL.
OrthoDBiEOG7Z95MB.
PhylomeDBiQ769K2.

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.

Q769K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDENENSQSP APSHQYPKET LRKRQNSVQN SGGSESSRLS RKSFKLDYRL
60 70 80 90 100
EEDVTKSKKG KDGRFVNPWP TWKNVSIPNV LRWLIMEKDH SSVPGSKEEL
110 120 130 140 150
DKELPVLKPY FISDPEEAGV REAGLRVTWL GHATLMVEMD ELILLTDPMF
160 170 180 190 200
SSRASPSQYM GPKRFRRPPC TISELPPIDA VLISHNHYDH LDYGSVLALN
210 220 230 240 250
ERFGSELRWF VPLGLLDWMQ KCGCENVIEL DWWEENCVPG HDKVTFVFTP
260 270 280 290 300
SQHWCKRTLL DDNKVLWGSW SVLGPWNRFF FAGDTGYCPA FEEIGKRFGP
310 320 330 340 350
FDLAAIPIGA YEPRWFMKYQ HADPEDAVRI HIDVQAKRSV AIHWGTFALA
360 370 380 390
NEHYLEPPVK LNEALERYGL KSEDFFILKH GESRYLNTDD KAFEET
Length:396
Mass (Da):45,723
Last modified:July 5, 2004 - v1
Checksum:i57AD6EC8B2C7363F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB112351 mRNA. Translation: BAD02398.1.
RefSeqiNP_955413.1. NM_199381.1.
XP_006235973.1. XM_006235911.2.
XP_008760861.1. XM_008762639.1.
UniGeneiRn.101892.

Genome annotation databases

EnsembliENSRNOT00000015322; ENSRNOP00000015322; ENSRNOG00000011363.
GeneIDi296757.
KEGGirno:296757.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB112351 mRNA. Translation: BAD02398.1.
RefSeqiNP_955413.1. NM_199381.1.
XP_006235973.1. XM_006235911.2.
XP_008760861.1. XM_008762639.1.
UniGeneiRn.101892.

3D structure databases

ProteinModelPortaliQ769K2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015322.

Chemistry

SwissLipidsiSLP:000001131.

PTM databases

iPTMnetiQ769K2.
PhosphoSiteiQ769K2.

Proteomic databases

PaxDbiQ769K2.
PRIDEiQ769K2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015322; ENSRNOP00000015322; ENSRNOG00000011363.
GeneIDi296757.
KEGGirno:296757.

Organism-specific databases

CTDi222236.
RGDi735197. Napepld.

Phylogenomic databases

eggNOGiKOG3798. Eukaryota.
COG2220. LUCA.
GeneTreeiENSGT00390000017990.
HOGENOMiHOG000267495.
HOVERGENiHBG054649.
InParanoidiQ769K2.
KOiK13985.
OMAiWGSWSVL.
OrthoDBiEOG7Z95MB.
PhylomeDBiQ769K2.

Enzyme and pathway databases

BRENDAi3.1.4.54. 5301.

Miscellaneous databases

NextBioi641757.
PROiQ769K2.

Gene expression databases

ExpressionAtlasiQ769K2. baseline.

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

  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], PROTEIN SEQUENCE OF 103-114 AND 368-379, SUBCELLULAR LOCATION, SUBUNIT, FUNCTION.
  2. "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: FUNCTION, COFACTOR, ENZYME REGULATION, SUBUNIT, POTENTIAL ZINC-BINDING SITES, MUTAGENESIS OF ASP-147; CYS-170; HIS-185; HIS-187; ASP-189; HIS-190; LEU-207; CYS-222; CYS-224; CYS-237; HIS-253; CYS-255; ASP-284; CYS-288; HIS-321; HIS-331; HIS-343; HIS-353 AND HIS-380.

Entry informationi

Entry nameiNAPEP_RAT
AccessioniPrimary (citable) accession number: Q769K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.