Q9NZC3 · GDE1_HUMAN
- ProteinGlycerophosphodiester phosphodiesterase 1
- GeneGDE1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids331 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Hydrolyzes the phosphodiester bond of glycerophosphodiesters such as glycerophosphoinositol (GroPIns) and glycerophosphoethanolamine (GroPEth), to yield a glycerol phosphate and an alcohol (By similarity).
Hydrolyzes glycerophospho-N-acylethanolamines to N-acylethanolamines in the brain and participates in bioactive N-acylethanolamine biosynthesis such as anandamide (an endocannabinoid), N-palmitoylethanolamine (an anti-inflammatory), and N-oleoylethanolamine (an anorexic). In addition, has a lysophospholipase D activity by hydrolyzing N-acyl-lysoplasmenylethanolamine (N-acyl-lysoPlsEt) to N-acylethanolamine. However lysophospholipase D activity is lower than glycerophosphodiester phosphodiesterase activity (By similarity).
Has little or no activity towards glycerophosphocholine (By similarity).
Hydrolyzes glycerophospho-N-acylethanolamines to N-acylethanolamines in the brain and participates in bioactive N-acylethanolamine biosynthesis such as anandamide (an endocannabinoid), N-palmitoylethanolamine (an anti-inflammatory), and N-oleoylethanolamine (an anorexic). In addition, has a lysophospholipase D activity by hydrolyzing N-acyl-lysoplasmenylethanolamine (N-acyl-lysoPlsEt) to N-acylethanolamine. However lysophospholipase D activity is lower than glycerophosphodiester phosphodiesterase activity (By similarity).
Has little or no activity towards glycerophosphocholine (By similarity).
Catalytic activity
- H2O + sn-glycero-3-phospho-1D-myo-inositol = H+ + myo-inositol + sn-glycerol 3-phosphateThis reaction proceeds in the forward direction.
- 1-O-(1Z-octadecenyl)-sn-glycero-3-phospho-(N-5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + H2O = 1-O-(1Z-octadecenyl)-sn-glycero-3-phosphate + H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamineThis reaction proceeds in the forward direction.
- 1-O-(1Z-octadecenyl)-sn-glycero-3-phospho-(N-9Z-octadecenoyl)-ethanolamine + H2O = 1-O-(1Z-octadecenyl)-sn-glycero-3-phosphate + H+ + N-(9Z-octadecenoyl) ethanolamineThis reaction proceeds in the forward direction.
- 1-O-(1Z-octadecenyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H2O = 1-O-(1Z-octadecenyl)-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamineThis reaction proceeds in the forward direction.
- H2O + N-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-sn-glycero-3-phosphoethanolamine = H+ + N-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl ethanolamine + sn-glycerol 3-phosphateThis reaction proceeds in the forward direction.
- H2O + N-eicosanoyl-sn-glycero-3-phosphoethanolamine = H+ + N-eicosanoyl ethanolamine + sn-glycerol 3-phosphateThis reaction proceeds in the forward direction.
- H2O + N-hexadecanoyl-sn-glycero-3-phosphoethanolamine = H+ + N-hexadecanoylethanolamine + sn-glycerol 3-phosphateThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = H+ + N-(9Z-octadecenoyl) ethanolamine + sn-glycerol 3-phosphateThis reaction proceeds in the forward direction.
- H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine = H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + sn-glycerol 3-phosphateThis reaction proceeds in the forward direction.
Cofactor
Activity regulation
Inhibited by EDTA, calcium chloride, and zinc chloride. Enhanced by magnesium chloride (By similarity).
Glycerophosphodiester phosphodiesterase activity can be modulated by G-protein signaling pathways (By similarity).
Glycerophosphodiester phosphodiesterase activity can be modulated by G-protein signaling pathways (By similarity).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | glycerophosphodiester phosphodiesterase activity | |
Molecular Function | glycerophosphoinositol glycerophosphodiesterase activity | |
Molecular Function | lysophospholipase activity | |
Molecular Function | metal ion binding | |
Biological Process | ethanolamine metabolic process | |
Biological Process | glycerophospholipid catabolic process | |
Biological Process | lipid metabolic process | |
Biological Process | N-acylethanolamine metabolic process | |
Biological Process | phospholipid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycerophosphodiester phosphodiesterase 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NZC3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Cytoplasmic vesicle membrane ; Multi-pass membrane protein
Note: Perinuclear vesicles and cell membrane.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-3 | Cytoplasmic | ||||
Sequence: MWL | ||||||
Transmembrane | 4-24 | Helical | ||||
Sequence: WEDQGGLLGPFSFLLLVLLLV | ||||||
Topological domain | 25-247 | Lumenal | ||||
Sequence: TRSPVNACLLTGSLFVLLRVFSFEPVPSCRALQVLKPRDRISAIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGIPVLMHDNTVDRTTDGTGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLREAVAECLNHNLTIFFDVKGHAHKATEALKKMYMEFPQLYNNSVVCSFLPEVIYKMRQTDRDVITALTHRPWSLSHTGDGKPRYDTFWKH | ||||||
Transmembrane | 248-268 | Helical | ||||
Sequence: FIFVMMDILLDWSMHNILWYL | ||||||
Topological domain | 269-331 | Cytoplasmic | ||||
Sequence: CGISAFLMQKDFVSPAYLKKWSAKGIQVVGWTVNTFDEKSYYESHLGSSYITDSMVEDCEPHF |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_044018 | 218 | in dbSNP:rs2072086 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_044019 | 328 | in dbSNP:rs34137361 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 359 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000251944 | 1-331 | Glycerophosphodiester phosphodiesterase 1 | |||
Sequence: MWLWEDQGGLLGPFSFLLLVLLLVTRSPVNACLLTGSLFVLLRVFSFEPVPSCRALQVLKPRDRISAIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGIPVLMHDNTVDRTTDGTGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLREAVAECLNHNLTIFFDVKGHAHKATEALKKMYMEFPQLYNNSVVCSFLPEVIYKMRQTDRDVITALTHRPWSLSHTGDGKPRYDTFWKHFIFVMMDILLDWSMHNILWYLCGISAFLMQKDFVSPAYLKKWSAKGIQVVGWTVNTFDEKSYYESHLGSSYITDSMVEDCEPHF | ||||||
Glycosylation | 168 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 198 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with PRAF2 (PubMed:16472945).
Interacts with RGS16 (By similarity).
Interacts with RGS16 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NZC3 | CXorf58 Q96LI9 | 2 | EBI-2833330, EBI-20870433 | |
BINARY | Q9NZC3 | SLC10A1 Q14973 | 3 | EBI-2833330, EBI-3923031 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 65-331 | GP-PDE | ||||
Sequence: ISAIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGIPVLMHDNTVDRTTDGTGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLREAVAECLNHNLTIFFDVKGHAHKATEALKKMYMEFPQLYNNSVVCSFLPEVIYKMRQTDRDVITALTHRPWSLSHTGDGKPRYDTFWKHFIFVMMDILLDWSMHNILWYLCGISAFLMQKDFVSPAYLKKWSAKGIQVVGWTVNTFDEKSYYESHLGSSYITDSMVEDCEPHF |
Sequence similarities
Belongs to the glycerophosphoryl diester phosphodiesterase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length331
- Mass (Da)37,718
- Last updated2000-10-01 v1
- ChecksumEFE567E71DBD4AC5
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF212862 EMBL· GenBank· DDBJ | AAF65234.1 EMBL· GenBank· DDBJ | mRNA | ||
AY463154 EMBL· GenBank· DDBJ | AAR25624.1 EMBL· GenBank· DDBJ | mRNA | ||
U91321 EMBL· GenBank· DDBJ | AAC05440.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AC003108 EMBL· GenBank· DDBJ | AAC05803.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BC014981 EMBL· GenBank· DDBJ | AAH14981.1 EMBL· GenBank· DDBJ | mRNA | ||
BC025273 EMBL· GenBank· DDBJ | AAH25273.1 EMBL· GenBank· DDBJ | mRNA |