A0A1L4BJ95 · A0A1L4BJ95_HEMLE
- ProteinSphingomyelin phosphodiesterase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids615 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Converts sphingomyelin to ceramide.
Catalytic activity
- a sphingomyelin + H2O = phosphocholine + an N-acylsphing-4-enine + H+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 210 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 212 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 282 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 282 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 322 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 429 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 463 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 465 | Zn2+ 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | lysosome | |
Molecular Function | acid sphingomyelin phosphodiesterase activity | |
Molecular Function | hydrolase activity, acting on glycosyl bonds | |
Molecular Function | metal ion binding | |
Biological Process | ceramide biosynthetic process | |
Biological Process | sphingomyelin catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSphingomyelin phosphodiesterase
- EC number
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Scorpiones > Iurida > Scorpionoidea > Hemiscorpiidae
Accessions
- Primary accessionA0A1L4BJ95
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-20 | ||||
Chain | PRO_5013086268 | 21-615 | Sphingomyelin phosphodiesterase | ||
Disulfide bond | 92↔168 | ||||
Disulfide bond | 95↔160 | ||||
Disulfide bond | 123↔134 | ||||
Disulfide bond | 225↔230 | ||||
Disulfide bond | 231↔254 | ||||
Disulfide bond | 389↔437 | ||||
Disulfide bond | 589↔593 | ||||
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length615
- Mass (Da)70,479
- Last updated2017-03-15 v1
- Checksum07CA88772991BE37
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KX932447 EMBL· GenBank· DDBJ | API81380.1 EMBL· GenBank· DDBJ | mRNA |