Q5VWZ2 · LYPL1_HUMAN
- ProteinLysophospholipase-like protein 1
- GeneLYPLAL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids237 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Palmitoyl thioesterase that catalyzes depalmitoylation of CGAS and KCNMA1 (PubMed:22052940, PubMed:22399288, PubMed:37802025).
Acts as a regulator of innate immunity by mediating depalmitoylation of CGAS, thereby preventing CGAS homodimerization and cyclic GMP-AMP synthase activity (PubMed:37802025).
Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site (PubMed:22052940).
Acts as a regulator of innate immunity by mediating depalmitoylation of CGAS, thereby preventing CGAS homodimerization and cyclic GMP-AMP synthase activity (PubMed:37802025).
Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site (PubMed:22052940).
Catalytic activity
- H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H+ + hexadecanoate + L-cysteinyl-[protein]This reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 124 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 179 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 211 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | carboxylic ester hydrolase activity | |
Molecular Function | hydrolase activity, acting on ester bonds | |
Molecular Function | lysophospholipase activity | |
Molecular Function | palmitoyl-(protein) hydrolase activity | |
Biological Process | negative regulation of cGAS/STING signaling pathway |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLysophospholipase-like protein 1
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5VWZ2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 1
Isoform 2
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_025607 | 131 | in dbSNP:rs940570 | |||
Sequence: I → M | ||||||
Mutagenesis | 179 | Abolished palmitoyl thioesterase activity; when associated with A-211. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_060992 | 197 | in dbSNP:rs34201999 | |||
Sequence: L → V | ||||||
Mutagenesis | 211 | Abolished palmitoyl thioesterase activity; when associated with A-179. | ||||
Sequence: H → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 331 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000227557 | 2-237 | UniProt | Lysophospholipase-like protein 1 | |||
Sequence: AAASGSVLQRCIVSPAGRHSASLIFLHGSGDSGQGLRMWIKQVLNQDLTFQHIKIIYPTAPPRSYTPMKGGISNVWFDRFKITNDCPEHLESIDVMCQVLTDLIDEEVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQKSNGVLPELFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPNVYHELSKTELDILKLWILTKLPGEMEKQK | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5VWZ2 | CT55 Q8WUE5 | 3 | EBI-6268634, EBI-6873363 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q5VWZ2-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length237
- Mass (Da)26,316
- Last updated2007-01-23 v3
- ChecksumA813A55DADDAF55E
Q5VWZ2-2
- Name2
- NoteMay be due to a competing acceptor splice site.
- Differences from canonical
- 65-80: Missing
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 32 | in Ref. 2; BAF84231 | ||||
Sequence: D → G | ||||||
Alternative sequence | VSP_017556 | 65-80 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY341430 EMBL· GenBank· DDBJ | AAQ17077.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291542 EMBL· GenBank· DDBJ | BAF84231.1 EMBL· GenBank· DDBJ | mRNA | ||
AL360093 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC016711 EMBL· GenBank· DDBJ | AAH16711.1 EMBL· GenBank· DDBJ | mRNA |