UniProtKB - Q6IQ20 (NAPEP_HUMAN)
N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
NAPEPLD
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 PublicationsCatalytic activityi
- H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a 1,2-diacyl-sn-glycero-3-phosphate + an N-acylethanolamine + H+4 PublicationsEC:3.1.4.544 PublicationsThis reaction proceeds in the forward4 Publications direction.
- H2O + N-butanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-butanoyl ethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N-hexanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-hexanoyl ethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N-octanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-octanoyl ethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N-decanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-decanoyl ethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N-dodecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-dodecanoylethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N-tetradecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-tetradecanoylethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N-octadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-octadecanoyl ethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N,1,2-tri-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-(9Z-octadecenoyl) ethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a 1,2-diacyl-sn-glycero-3-phosphate + H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H2O = 1-O-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-3-phosphate + an N-acylethanolamine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamineBy similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
Activity regulationi
Kineticsi
- KM=9 µM for N-hexadecanoyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (in the presence of deoxycholic acid)1 Publication
- 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
- Vmax=156 nmol/min/mg enzyme toward N-hexadecanoyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (in the presence of deoxycholic acid)1 Publication
- 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 185 | Zinc 1; via tele nitrogen1 Publication | 1 | |
Metal bindingi | 187 | Zinc 1; via pros nitrogen1 Publication | 1 | |
Binding sitei | 188 | N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine1 Publication | 1 | |
Metal bindingi | 189 | Zinc 21 Publication | 1 | |
Metal bindingi | 190 | Zinc 2; via tele nitrogen1 Publication | 1 | |
Metal bindingi | 253 | Zinc 1; via tele nitrogen1 Publication | 1 | |
Binding sitei | 256 | deoxycholic acidCombined sources1 Publication | 1 | |
Binding sitei | 260 | deoxycholic acid; via amide nitrogenCombined sources1 Publication | 1 | |
Metal bindingi | 284 | Zinc 11 Publication | 1 | |
Metal bindingi | 284 | Zinc 21 Publication | 1 | |
Binding sitei | 321 | N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine1 Publication | 1 | |
Metal bindingi | 343 | Zinc 2; via tele nitrogen1 Publication | 1 | |
Binding sitei | 348 | deoxycholic acid; via carbonyl oxygenCombined sources1 Publication | 1 |
GO - Molecular functioni
- bile acid binding Source: UniProtKB
- identical protein binding Source: IntAct
- N-acetylphosphatidylethanolamine-hydrolysing phospholipase activity Source: UniProtKB-EC
- N-acylphosphatidylethanolamine-specific phospholipase D activity Source: UniProtKB
- zinc ion binding Source: UniProtKB
GO - Biological processi
- host-mediated regulation of intestinal microbiota composition Source: UniProtKB
- N-acylethanolamine metabolic process Source: GO_Central
- N-acylphosphatidylethanolamine metabolic process Source: UniProtKB
- phospholipid catabolic process Source: UniProtKB-KW
- positive regulation of brown fat cell differentiation Source: UniProtKB
- positive regulation of inflammatory response Source: UniProtKB
- retinoid metabolic process Source: Reactome
- temperature homeostasis Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Biological process | Lipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.1.4.54, 2681 |
PathwayCommonsi | Q6IQ20 |
Reactomei | R-HSA-2466712, Biosynthesis of A2E, implicated in retinal degradation |
SignaLinki | Q6IQ20 |
Chemistry databases
SwissLipidsi | SLP:000001132 |
Names & Taxonomyi
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 |
Gene namesi | Name:NAPEPLD Synonyms:C7orf18 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:21683, NAPEPLD |
MIMi | 612334, gene |
neXtProti | NX_Q6IQ20 |
VEuPathDBi | HostDB:ENSG00000161048 |
Subcellular locationi
Golgi apparatus
- Golgi apparatus membrane 1 Publication; Peripheral membrane protein 1 Publication
Endosome
- Early endosome membrane 1 Publication; Peripheral membrane protein 1 Publication
Nucleus
- Nucleus envelope 1 Publication
- nucleoplasm 1 Publication
Note: Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids.1 Publication
Endosome
- early endosome Source: UniProtKB
- early endosome membrane Source: UniProtKB-SubCell
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Golgi apparatus
- Golgi apparatus Source: UniProtKB
- Golgi membrane Source: UniProtKB-SubCell
Nucleus
- nuclear envelope Source: UniProtKB
- nucleoplasm Source: UniProtKB
Plasma Membrane
- photoreceptor outer segment membrane Source: Reactome
Other locations
- cytoplasm Source: GO_Central
- membrane-bounded organelle Source: GO_Central
Keywords - Cellular componenti
Endosome, Golgi apparatus, Membrane, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 158 | Q → S: Impairs homodimerization resulting in loss of activity; when associated with S-159. 1 Publication | 1 | |
Mutagenesisi | 159 | Y → S: Impairs homodimerization resulting in loss of activity; when associated with S-158. 1 Publication | 1 | |
Mutagenesisi | 207 | L → F: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 257 | R → A: Impairs binding to bile acids resulting in loss of activity. 1 Publication | 1 | |
Mutagenesisi | 380 | H → R: Loss of activity. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 222236 |
OpenTargetsi | ENSG00000161048 |
PharmGKBi | PA162396960 |
Miscellaneous databases
Pharosi | Q6IQ20, Tbio |
Chemistry databases
ChEMBLi | CHEMBL4630839 |
DrugBanki | DB14009, Medical Cannabis |
GuidetoPHARMACOLOGYi | 1398 |
Genetic variation databases
BioMutai | NAPEPLD |
DMDMi | 167016292 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000318159 | 1 – 393 | N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase DAdd BLAST | 393 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineCombined sources | 1 |
Keywords - PTMi
AcetylationProteomic databases
EPDi | Q6IQ20 |
jPOSTi | Q6IQ20 |
MassIVEi | Q6IQ20 |
MaxQBi | Q6IQ20 |
PaxDbi | Q6IQ20 |
PeptideAtlasi | Q6IQ20 |
PRIDEi | Q6IQ20 |
ProteomicsDBi | 66476 |
PTM databases
iPTMneti | Q6IQ20 |
PhosphoSitePlusi | Q6IQ20 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000161048, Expressed in dorsal plus ventral thalamus and 219 other tissues |
ExpressionAtlasi | Q6IQ20, baseline and differential |
Genevisiblei | Q6IQ20, HS |
Organism-specific databases
HPAi | ENSG00000161048, Low tissue specificity |
Interactioni
Subunit structurei
Homodimer. Bile acids promote the assembly of inactive monomers into an active dimer and enable catalysis.
1 PublicationBinary interactionsi
Q6IQ20
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-16143143,EBI-16143143 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 128793, 3 interactors |
DIPi | DIP-61398N |
IntActi | Q6IQ20, 1 interactor |
STRINGi | 9606.ENSP00000407112 |
Miscellaneous databases
RNActi | Q6IQ20, protein |
Structurei
Secondary structure
3D structure databases
SMRi | Q6IQ20 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 40 | DisorderedSequence analysisAdd BLAST | 40 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1 – 39 | Polar residuesSequence analysisAdd BLAST | 39 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG3798, Eukaryota |
GeneTreei | ENSGT00390000017990 |
HOGENOMi | CLU_020884_2_1_1 |
InParanoidi | Q6IQ20 |
OMAi | QHWTRRT |
OrthoDBi | 1194556at2759 |
PhylomeDBi | Q6IQ20 |
TreeFami | TF313520 |
Family and domain databases
Gene3Di | 3.60.15.10, 1 hit |
InterProi | View protein in InterPro IPR001279, Metallo-B-lactamas IPR024884, NAPE-PLD IPR036866, RibonucZ/Hydroxyglut_hydro |
Pfami | View protein in Pfam PF12706, Lactamase_B_2, 1 hit |
PIRSFi | PIRSF038896, NAPE-PLD, 1 hit |
SUPFAMi | SSF56281, SSF56281, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketC9JGB1 | C9JGB1_HUMAN | N-acyl-phosphatidylethanolamine-hyd... | NAPEPLD | 124 | Annotation score: | ||
H0Y4Y2 | H0Y4Y2_HUMAN | N-acyl-phosphatidylethanolamine-hyd... | NAPEPLD | 143 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 281 | Missing in CAI56779 (PubMed:17974005).Curated | 1 | |
Sequence conflicti | 371 | N → Y in CAI56779 (PubMed:17974005).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_038695 | 152 | S → A Almost no change in activity. 1 PublicationCorresponds to variant dbSNP:rs12540583Ensembl. | 1 | |
Natural variantiVAR_038694 | 389 | D → N Almost no change in activity. 4 PublicationsCorresponds to variant dbSNP:rs3181009Ensembl. | 1 |
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 |
CCDSi | CCDS5729.1 |
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
Similar proteinsi
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 |
CCDSi | CCDS5729.1 |
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 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4QN9 | X-ray | 2.65 | A/B | 1-393 | [»] | |
SMRi | Q6IQ20 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 128793, 3 interactors |
DIPi | DIP-61398N |
IntActi | Q6IQ20, 1 interactor |
STRINGi | 9606.ENSP00000407112 |
Chemistry databases
ChEMBLi | CHEMBL4630839 |
DrugBanki | DB14009, Medical Cannabis |
GuidetoPHARMACOLOGYi | 1398 |
SwissLipidsi | SLP:000001132 |
PTM databases
iPTMneti | Q6IQ20 |
PhosphoSitePlusi | Q6IQ20 |
Genetic variation databases
BioMutai | NAPEPLD |
DMDMi | 167016292 |
Proteomic databases
EPDi | Q6IQ20 |
jPOSTi | Q6IQ20 |
MassIVEi | Q6IQ20 |
MaxQBi | Q6IQ20 |
PaxDbi | Q6IQ20 |
PeptideAtlasi | Q6IQ20 |
PRIDEi | Q6IQ20 |
ProteomicsDBi | 66476 |
Protocols and materials databases
Antibodypediai | 16885, 171 antibodies from 23 providers |
DNASUi | 222236 |
Genome annotation databases
Organism-specific databases
CTDi | 222236 |
DisGeNETi | 222236 |
GeneCardsi | NAPEPLD |
HGNCi | HGNC:21683, NAPEPLD |
HPAi | ENSG00000161048, Low tissue specificity |
MIMi | 612334, gene |
neXtProti | NX_Q6IQ20 |
OpenTargetsi | ENSG00000161048 |
PharmGKBi | PA162396960 |
VEuPathDBi | HostDB:ENSG00000161048 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3798, Eukaryota |
GeneTreei | ENSGT00390000017990 |
HOGENOMi | CLU_020884_2_1_1 |
InParanoidi | Q6IQ20 |
OMAi | QHWTRRT |
OrthoDBi | 1194556at2759 |
PhylomeDBi | Q6IQ20 |
TreeFami | TF313520 |
Enzyme and pathway databases
BRENDAi | 3.1.4.54, 2681 |
PathwayCommonsi | Q6IQ20 |
Reactomei | R-HSA-2466712, Biosynthesis of A2E, implicated in retinal degradation |
SignaLinki | Q6IQ20 |
Miscellaneous databases
BioGRID-ORCSi | 222236, 4 hits in 1046 CRISPR screens |
ChiTaRSi | NAPEPLD, human |
GenomeRNAii | 222236 |
Pharosi | Q6IQ20, Tbio |
PROi | PR:Q6IQ20 |
RNActi | Q6IQ20, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000161048, Expressed in dorsal plus ventral thalamus and 219 other tissues |
ExpressionAtlasi | Q6IQ20, baseline and differential |
Genevisiblei | Q6IQ20, HS |
Family and domain databases
Gene3Di | 3.60.15.10, 1 hit |
InterProi | View protein in InterPro IPR001279, Metallo-B-lactamas IPR024884, NAPE-PLD IPR036866, RibonucZ/Hydroxyglut_hydro |
Pfami | View protein in Pfam PF12706, Lactamase_B_2, 1 hit |
PIRSFi | PIRSF038896, NAPE-PLD, 1 hit |
SUPFAMi | SSF56281, SSF56281, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | NAPEP_HUMAN | |
Accessioni | Q6IQ20Primary (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: | February 23, 2022 | |
This is version 145 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families