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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)DescriptionActionsGraphical viewLength
Metal bindingi185Zinc 1Sequence analysis1
Metal bindingi187Zinc 1Sequence analysis1
Metal bindingi189Zinc 2Sequence analysis1
Metal bindingi190Zinc 2Sequence analysis1
Metal bindingi253Zinc 1Sequence analysis1
Metal bindingi343Zinc 2Sequence analysis1

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 databases

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)DescriptionActionsGraphical viewLength
Mutagenesisi147D → N: Abolishes activity. 1 Publication1
Mutagenesisi170C → S: Small decrease in activity. 1 Publication1
Mutagenesisi185H → N: <1% of wild-type activity. 1 Publication1
Mutagenesisi187H → N: <1% of wild-type activity. 1 Publication1
Mutagenesisi189D → N: <1% of wild-type activity. 1 Publication1
Mutagenesisi190H → N: <1% of wild-type activity. 1 Publication1
Mutagenesisi207L → F: <5% of wild-type activity. 1 Publication1
Mutagenesisi222C → S: No effect on activity. 1 Publication1
Mutagenesisi224C → S: Considerable decrease in activity. 1 Publication1
Mutagenesisi237C → S: No effect on activity. 1 Publication1
Mutagenesisi253H → N: Abolishes activity. 1 Publication1
Mutagenesisi255C → S: No effect on activity. 1 Publication1
Mutagenesisi284D → N: Abolishes activity. 1 Publication1
Mutagenesisi288C → S: No effect on activity. 1 Publication1
Mutagenesisi321H → N: Abolishes activity. 1 Publication1
Mutagenesisi331H → N: 4% of wild-type activity. 1 Publication1
Mutagenesisi343H → N: No effect on activity. 1 Publication1
Mutagenesisi353H → N: No effect on activity. 1 Publication1
Mutagenesisi380H → R: <5% of wild-type activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003181621 – 396N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase DAdd BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ769K2.
PRIDEiQ769K2.

PTM databases

iPTMnetiQ769K2.
PhosphoSitePlusiQ769K2.

Expressioni

Gene expression databases

BgeeiENSRNOG00000011363.
ExpressionAtlasiQ769K2. differential.

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.
OMAiDWMQKCG.
OrthoDBiEOG091G0AHO.
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_006235911.3.
XP_008760861.1. XM_008762639.2.
XP_017448006.1. XM_017592517.1.
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_006235911.3.
XP_008760861.1. XM_008762639.2.
XP_017448006.1. XM_017592517.1.
UniGeneiRn.101892.

3D structure databases

ProteinModelPortaliQ769K2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015322.

Chemistry databases

SwissLipidsiSLP:000001131.

PTM databases

iPTMnetiQ769K2.
PhosphoSitePlusiQ769K2.

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.
OMAiDWMQKCG.
OrthoDBiEOG091G0AHO.
PhylomeDBiQ769K2.

Enzyme and pathway databases

BRENDAi3.1.4.54. 5301.

Miscellaneous databases

PROiQ769K2.

Gene expression databases

BgeeiENSRNOG00000011363.
ExpressionAtlasiQ769K2. differential.

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...

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: November 30, 2016
This is version 72 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.