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Entry version 142 (07 Apr 2021)
Sequence version 2 (05 Feb 2008)
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Protein

N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D

Gene

NAPEPLD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (PubMed:14634025, PubMed:16527816, PubMed:27571266, PubMed:25684574). Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain (By similarity). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (By similarity). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (By similarity).By similarity4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+1 PublicationNote: Binds 2 zinc divalent cations per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by divalent cations (PubMed:16527816). Activated by bile acids and their conjugates, except for lithocholic acid which is rather inhibitory. Binding of deoxycholic acid favors the selective release of anandamide and likely other unsatured long FAEs (PubMed:27571266, PubMed:25684574). Inhibited by phosphatidylethanolamines (PubMed:25684574).3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=9 µM for N-hexadecanoyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (in the presence of deoxycholic acid)1 Publication
  2. KM=9 µM for N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-diacyl-sn-glycero-3-phosphoethanolamine (in the presence of deoxycholic acid)1 Publication
  1. Vmax=156 nmol/min/mg enzyme toward N-hexadecanoyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (in the presence of deoxycholic acid)1 Publication
  2. Vmax=1131 nmol/min/mg enzyme toward N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-diacyl-sn-glycero-3-phosphoethanolamine (in the presence of deoxycholic acid)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi185Zinc 1; via tele nitrogen1 Publication1
Metal bindingi187Zinc 1; via pros nitrogen1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei188N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine1 Publication1
Metal bindingi189Zinc 21 Publication1
Metal bindingi190Zinc 2; via tele nitrogen1 Publication1
Metal bindingi253Zinc 1; via tele nitrogen1 Publication1
Binding sitei256deoxycholic acidCombined sources1 Publication1
Binding sitei260deoxycholic acid; via amide nitrogenCombined sources1 Publication1
Metal bindingi284Zinc 11 Publication1
Metal bindingi284Zinc 21 Publication1
Binding sitei321N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine1 Publication1
Metal bindingi343Zinc 2; via tele nitrogen1 Publication1
Binding sitei348deoxycholic acid; via carbonyl oxygenCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processLipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:ENSG00000161048-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.4.54, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
Q6IQ20

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2466712, Biosynthesis of A2E, implicated in retinal degradation

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001132

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D1 Publication (EC:3.1.4.543 Publications)
Short name:
N-acyl phosphatidylethanolamine phospholipase D
Short name:
NAPE-PLD1 Publication
Short name:
NAPE-hydrolyzing phospholipase D
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NAPEPLD
Synonyms:C7orf18
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:21683, NAPEPLD

Online Mendelian Inheritance in Man (OMIM)

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MIMi
612334, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q6IQ20

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000161048.11

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Endosome, Golgi apparatus, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi158Q → S: Impairs homodimerization resulting in loss of activity; when associated with S-159. 1 Publication1
Mutagenesisi159Y → S: Impairs homodimerization resulting in loss of activity; when associated with S-158. 1 Publication1
Mutagenesisi207L → F: Loss of activity. 1 Publication1
Mutagenesisi257R → A: Impairs binding to bile acids resulting in loss of activity. 1 Publication1
Mutagenesisi380H → R: Loss of activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
222236

Open Targets

More...
OpenTargetsi
ENSG00000161048

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA162396960

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q6IQ20, Tbio

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB14009, Medical Cannabis

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1398

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
NAPEPLD

Domain mapping of disease mutations (DMDM)

More...
DMDMi
167016292

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003181591 – 393N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase DAdd BLAST393

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q6IQ20

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q6IQ20

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q6IQ20

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q6IQ20

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q6IQ20

PeptideAtlas

More...
PeptideAtlasi
Q6IQ20

PRoteomics IDEntifications database

More...
PRIDEi
Q6IQ20

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
66476

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6IQ20

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q6IQ20

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed. Highest expression in brain, kidney and testis (at protein level). Expressed in adipose tissue (at protein level).By similarity

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000161048, Expressed in dorsal plus ventral thalamus and 219 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q6IQ20, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q6IQ20, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000161048, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Bile acids promote the assembly of inactive monomers into an active dimer and enable catalysis.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Q6IQ20
With#Exp.IntAct
itself3EBI-16143143,EBI-16143143

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
128793, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-61398N

Protein interaction database and analysis system

More...
IntActi
Q6IQ20, 1 interactor

STRING: functional protein association networks

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STRINGi
9606.ENSP00000407112

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q6IQ20, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q6IQ20

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NAPE-PLD family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3798, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00390000017990

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_020884_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6IQ20

Identification of Orthologs from Complete Genome Data

More...
OMAi
QHWTRRT

Database of Orthologous Groups

More...
OrthoDBi
1194556at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6IQ20

TreeFam database of animal gene trees

More...
TreeFami
TF313520

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.15.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001279, Metallo-B-lactamas
IPR024884, NAPE-PLD
IPR036866, RibonucZ/Hydroxyglut_hydro

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12706, Lactamase_B_2, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF038896, NAPE-PLD, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56281, SSF56281, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5CE3114CC557B698
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JGB1C9JGB1_HUMAN
N-acyl-phosphatidylethanolamine-hyd...
NAPEPLD
124Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y4Y2H0Y4Y2_HUMAN
N-acyl-phosphatidylethanolamine-hyd...
NAPEPLD
143Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti281Missing in CAI56779 (PubMed:17974005).Curated1
Sequence conflicti371N → Y in CAI56779 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_038695152S → A Almost no change in activity. 1 PublicationCorresponds to variant dbSNP:rs12540583Ensembl.1
Natural variantiVAR_038694389D → N Almost no change in activity. 4 PublicationsCorresponds to variant dbSNP:rs3181009Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS5729.1

NCBI Reference Sequences

More...
RefSeqi
NP_001116310.1, NM_001122838.1
NP_945341.3, NM_198990.4
XP_005250271.2, XM_005250214.4
XP_005250272.1, XM_005250215.2
XP_005250275.1, XM_005250218.2
XP_011514235.1, XM_011515933.2
XP_016867343.1, XM_017011854.1
XP_016867344.1, XM_017011855.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000341533; 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

Database of genes from NCBI RefSeq genomes

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GeneIDi
222236

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:222236

UCSC genome browser

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UCSCi
uc003vbc.3, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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_005250214.4
XP_005250272.1, XM_005250215.2
XP_005250275.1, XM_005250218.2
XP_011514235.1, XM_011515933.2
XP_016867343.1, XM_017011854.1
XP_016867344.1, XM_017011855.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QN9X-ray2.65A/B1-393[»]
SMRiQ6IQ20
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi128793, 1 interactor
DIPiDIP-61398N
IntActiQ6IQ20, 1 interactor
STRINGi9606.ENSP00000407112

Chemistry databases

DrugBankiDB14009, Medical Cannabis
GuidetoPHARMACOLOGYi1398
SwissLipidsiSLP:000001132

PTM databases

iPTMnetiQ6IQ20
PhosphoSitePlusiQ6IQ20

Genetic variation databases

BioMutaiNAPEPLD
DMDMi167016292

Proteomic databases

EPDiQ6IQ20
jPOSTiQ6IQ20
MassIVEiQ6IQ20
MaxQBiQ6IQ20
PaxDbiQ6IQ20
PeptideAtlasiQ6IQ20
PRIDEiQ6IQ20
ProteomicsDBi66476

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
16885, 168 antibodies

The DNASU plasmid repository

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DNASUi
222236

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

Comparative Toxicogenomics Database

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CTDi
222236
DisGeNETi222236

GeneCards: human genes, protein and diseases

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GeneCardsi
NAPEPLD
HGNCiHGNC:21683, NAPEPLD
HPAiENSG00000161048, Low tissue specificity
MIMi612334, gene
neXtProtiNX_Q6IQ20
OpenTargetsiENSG00000161048
PharmGKBiPA162396960
VEuPathDBiHostDB:ENSG00000161048.11

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3798, Eukaryota
GeneTreeiENSGT00390000017990
HOGENOMiCLU_020884_2_1_1
InParanoidiQ6IQ20
OMAiQHWTRRT
OrthoDBi1194556at2759
PhylomeDBiQ6IQ20
TreeFamiTF313520

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000161048-MONOMER
BRENDAi3.1.4.54, 2681
PathwayCommonsiQ6IQ20
ReactomeiR-HSA-2466712, Biosynthesis of A2E, implicated in retinal degradation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
222236, 4 hits in 995 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
NAPEPLD, human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
222236
PharosiQ6IQ20, Tbio

Protein Ontology

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PROi
PR:Q6IQ20
RNActiQ6IQ20, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000161048, Expressed in dorsal plus ventral thalamus and 219 other tissues
ExpressionAtlasiQ6IQ20, baseline and differential
GenevisibleiQ6IQ20, HS

Family and domain databases

Gene3Di3.60.15.10, 1 hit
InterProiView protein in InterPro
IPR001279, Metallo-B-lactamas
IPR024884, NAPE-PLD
IPR036866, RibonucZ/Hydroxyglut_hydro
PfamiView protein in Pfam
PF12706, Lactamase_B_2, 1 hit
PIRSFiPIRSF038896, NAPE-PLD, 1 hit
SUPFAMiSSF56281, SSF56281, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNAPEP_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6IQ20
Secondary accession number(s): Q5CZ87, Q769K1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: April 7, 2021
This is version 142 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
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