Q8BGJ0 · ZDH15_MOUSE
- ProteinPalmitoyltransferase ZDHHC15
- GeneZdhhc15
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids337 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (PubMed:15603741, PubMed:17012030, PubMed:28167757).
Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (Probable). Palmitoylates IGF2R and SORT1, promoting their partitioning to an endosomal membrane subdomain where they can interact with the retromer cargo-selective complex (By similarity).
Thereby, regulates retrograde transport from endosomes to the Golgi apparatus of these lysosomal sorting receptors and plays a role in trafficking of lysosomal proteins (By similarity).
In the nervous system, catalyzes the palmitoylation of DLG4/PSD95 and regulates its synaptic clustering and function in synaptogenesis (PubMed:15603741).
Could be involved in the differentiation of dopaminergic neurons and the development of the diencephalon (By similarity).
Could also catalyze the palmitoylation of GAP43 (PubMed:15603741, PubMed:17012030).
Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane (PubMed:18596047).
Could also palmitoylate FYN as shown in vitro (By similarity).
May palmitoylate CALHM3 subunit of gustatory voltage-gated ion channels and modulate channel gating and kinetics
Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (Probable). Palmitoylates IGF2R and SORT1, promoting their partitioning to an endosomal membrane subdomain where they can interact with the retromer cargo-selective complex (By similarity).
Thereby, regulates retrograde transport from endosomes to the Golgi apparatus of these lysosomal sorting receptors and plays a role in trafficking of lysosomal proteins (By similarity).
In the nervous system, catalyzes the palmitoylation of DLG4/PSD95 and regulates its synaptic clustering and function in synaptogenesis (PubMed:15603741).
Could be involved in the differentiation of dopaminergic neurons and the development of the diencephalon (By similarity).
Could also catalyze the palmitoylation of GAP43 (PubMed:15603741, PubMed:17012030).
Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane (PubMed:18596047).
Could also palmitoylate FYN as shown in vitro (By similarity).
May palmitoylate CALHM3 subunit of gustatory voltage-gated ion channels and modulate channel gating and kinetics
Catalytic activity
- hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]This reaction proceeds in the forward direction.
- L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-tetradecanoyl-L-cysteinyl-[protein]This reaction proceeds in the forward direction.
- L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-octadecanoyl-L-cysteinyl-[protein]This reaction proceeds in the forward direction.
Activity regulation
Inhibited by 2-bromopalmitate.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 131 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 134 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 144 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 145 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 148 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 151 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 158 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 159 | S-palmitoyl cysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 165 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | postsynapse | |
Cellular Component | postsynaptic density | |
Molecular Function | palmitoyltransferase activity | |
Molecular Function | protein-cysteine S-myristoyltransferase activity | |
Molecular Function | protein-cysteine S-palmitoyltransferase activity | |
Molecular Function | protein-cysteine S-stearoyltransferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | establishment of protein localization | |
Biological Process | peptidyl-L-cysteine S-palmitoylation | |
Biological Process | positive regulation of dendrite development | |
Biological Process | protein localization to membrane | |
Biological Process | protein localization to postsynapse | |
Biological Process | protein palmitoylation | |
Biological Process | protein targeting to Golgi apparatus | |
Biological Process | protein targeting to membrane | |
Biological Process | regulation of dendritic spine morphogenesis | |
Biological Process | synaptic vesicle maturation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePalmitoyltransferase ZDHHC15
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8BGJ0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-20 | Cytoplasmic | ||||
Sequence: MRRGWKMALSGGLRCCRRVL | ||||||
Transmembrane | 21-41 | Helical | ||||
Sequence: SWVPVLVIVLVVLWSYYAYVF | ||||||
Topological domain | 42-56 | Lumenal | ||||
Sequence: ELCLVTVLSPAEKVI | ||||||
Transmembrane | 57-77 | Helical | ||||
Sequence: YLILYHAIFVFFAWTYWKSIF | ||||||
Topological domain | 78-172 | Cytoplasmic | ||||
Sequence: TLPQQPNQKFHLSYTDKERYKNEERPEVQKQMLVDMAKKLPVYTRTGSGAVRFCDRCHLIKPDRCHHCSVCAMCVLKMDHHCPWVNNCIGFSNYK | ||||||
Transmembrane | 173-193 | Helical | ||||
Sequence: FFLQFLAYSVLYCLYIATTVF | ||||||
Topological domain | 194-210 | Lumenal | ||||
Sequence: SYFIKYWRGELPSVRSK | ||||||
Transmembrane | 211-234 | Helical | ||||
Sequence: FHVLFLLFVACMFFVSLVILFGYH | ||||||
Topological domain | 235-337 | Cytoplasmic | ||||
Sequence: CWLVSRNKTTLEAFCTPVFTSGPEKNGFNLGFIKNIQQVFGDNKKFWLIPIGSSPGDGHSFPMRSMNESQNPLLANEEPWEDNEDDSRDYPEGSSSLAVESET |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 156-157 | Fails to enhance DLG4 palmitoylation. | ||||
Sequence: DH → AA | ||||||
Mutagenesis | 159 | Fails to enhance DLG4 palmitoylation. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 22 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000212894 | 1-337 | Palmitoyltransferase ZDHHC15 | |||
Sequence: MRRGWKMALSGGLRCCRRVLSWVPVLVIVLVVLWSYYAYVFELCLVTVLSPAEKVIYLILYHAIFVFFAWTYWKSIFTLPQQPNQKFHLSYTDKERYKNEERPEVQKQMLVDMAKKLPVYTRTGSGAVRFCDRCHLIKPDRCHHCSVCAMCVLKMDHHCPWVNNCIGFSNYKFFLQFLAYSVLYCLYIATTVFSYFIKYWRGELPSVRSKFHVLFLLFVACMFFVSLVILFGYHCWLVSRNKTTLEAFCTPVFTSGPEKNGFNLGFIKNIQQVFGDNKKFWLIPIGSSPGDGHSFPMRSMNESQNPLLANEEPWEDNEDDSRDYPEGSSSLAVESET |
Post-translational modification
Autopalmitoylated (in vitro).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 129-179 | DHHC | ||||
Sequence: RFCDRCHLIKPDRCHHCSVCAMCVLKMDHHCPWVNNCIGFSNYKFFLQFLA | ||||||
Region | 293-337 | Disordered | ||||
Sequence: HSFPMRSMNESQNPLLANEEPWEDNEDDSRDYPEGSSSLAVESET |
Domain
The DHHC domain is required for palmitoyltransferase activity.
Sequence similarities
Belongs to the DHHC palmitoyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length337
- Mass (Da)39,269
- Last updated2003-03-01 v1
- Checksum93FFBDB720B09421
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK029137 EMBL· GenBank· DDBJ | BAC26317.1 EMBL· GenBank· DDBJ | mRNA | ||
AK032922 EMBL· GenBank· DDBJ | BAC28087.1 EMBL· GenBank· DDBJ | mRNA | ||
AK077949 EMBL· GenBank· DDBJ | BAC37081.1 EMBL· GenBank· DDBJ | mRNA | ||
AK160360 EMBL· GenBank· DDBJ | BAE35757.1 EMBL· GenBank· DDBJ | mRNA |