Q6L6S1 · EGCSE_HYDVU
- ProteinEndoglycoceramidase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids517 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Hydrolysis of the glycosidic linkage between oligosaccharides and ceramides of glycosphingolipids, optimal substrates appear to be the glycosphingolipids with a gangliotetraose structure.
Catalytic activity
- an oligoglycosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H2O = an N-acyl-sphingoid base + an oligoglycosyl-(1->4)-D-glucose
Activity regulation
Cu2+, zinc, manganese, calcium, magnesium and EDTA have no significant effects on enzyme activity. Enzyme requires presence of detergents such as Triton X-100 and Lubrol PX for the hydrolysis of glycosphingolipids. Taurodeoxycholate strongly inhibits the enzyme activity.
pH Dependence
Optimum pH is 3.0-4.0. Highly stable at acidic pH.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 230 | Proton donor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | endoglycosylceramidase activity | |
Biological Process | cellulose catabolic process | |
Biological Process | glycosphingolipid catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEndoglycoceramidase
- EC number
- Short namesEGCase
- Alternative names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Cnidaria > Hydrozoa > Hydroidolina > Anthoathecata > Aplanulata > Hydridae > Hydra
Accessions
- Primary accessionQ6L6S1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Released from digestive cells into the gastric cavity, and eventually into the surrounding medium, during the digestive process.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MISVALIILFLAKVISG | ||||||
Chain | PRO_0000390382 | 18-517 | Endoglycoceramidase | |||
Sequence: KSDDFISVNPETNMLIDGYGRERFFHGTNVVVKHFPFHPETTGFNKDTFSEDDMKILQKFGLNSIRLGMMLPGYVPKREEYNETYIKVIQSIVTTAAKYGIYTLLDMHQDVFSPKFCVEGMPDWIVNTQGAKDFPMPLHKPFNLDPKTGYPYPEDCAKFSWADYYFTEAAGQAFQNLYDNVDGLRDEWAQFWKKTADVFKEEPSVIGYELINEPFCGNVFKHPTLLIPGVADYLNLQPTYDALQKAIRQVDEEHNIFFEGVTWDFFEVGFTEVPGGKQYQNRSVLSYHYYEPPDFSKKLNFEARLLDLKRLKCGGFLTEMFTVGTDFNSMFEMFDLCDKFKQSWHGWMYKSYGCIEQNLGCLNMSSPGKESIQIANTSRTYPQAVAGRTQSYAFDIKTKVFTLVYETVGSCKSGRTIVYFNKNLHYPNGYRYEINPNFKVTPSENEYFLYLDEVNKVPNTVVTFKLFPLSFTDSEDIHPVTVMGDKHLSENHNENEKKKK | ||||||
Glycosylation | 99 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 298 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 380 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 393 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Expression
Tissue specificity
Expressed uniformly in digestive cells, tentacles and peduncle regions suggesting expression in the endoderm throughout the whole body (at protein level).
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length517
- Mass (Da)59,685
- Last updated2004-07-05 v1
- Checksum9042532367D263F4
Keywords
- Technical term