Q8TL28 · ULIL_METAC
- ProteinUlilysin
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids342 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Metalloprotease which in vitro specifically cleaves IGFBP-2 to -6, insulin, and extracellular matrix proteins but not IGFBP-1 or IGF-II. Shows a preference for substrates with an arginine in the P1' position, the first position downstream of the scissile bond.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 calcium ions per subunit.
Note: Binds 1 zinc ion per subunit.
Activity regulation
Inhibited by EDTA, excess zinc, and also significantly by batimastat in vitro. Is not inhibited by other metalloprotease inhibitors like phosphoramidon, captopril and galardine or those targeting other classes of proteases.
pH Dependence
Optimum pH is 7.5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 188-189 | substrate | ||||
Sequence: LG | ||||||
Binding site | 225 | substrate | ||||
Sequence: T | ||||||
Binding site | 228 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 229 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 232 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 238 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 240 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 243 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 249 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 254 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 256 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 259 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 262 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 263 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 295 | substrate | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | metallopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUlilysin
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinaceae > Methanosarcina
Accessions
- Primary accessionQ8TL28
Proteomes
PTM/Processing
Features
Showing features for propeptide, signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000280823 | ?-60 | Removed in mature form | |||
Sequence: MAEKFESRGIEEASSEVPTQRRCGAMEVHHRLLRSASYVRERDQIENLALKYKQGFRAIS | ||||||
Signal | 1-? | |||||
Chain | PRO_0000280824 | 61-322 | Ulilysin | |||
Sequence: RMEIVKIPVVVHVVWNEEEENISDAQIQSQIDILNKDFRKLNSDVSQVPSVWSNLIADLGIEFFLATKDPNGNQTTGITRTQTSVTFFTTSDEVKFASSGGEDAWPADRYLNIWVCHVLKSEIGQDILGYAQFPGGPAETDGVVIVDAAFGTTGTALPPFDKGRTATHEIGHWLNLYHIWGDELRFEDPCSRSDEVDDTPNQADPNFGCPSYPHVSCSNGPNGDMFMNYMDYVDDKCMVMFTQGQATRVNACLDGPRSSFLA | ||||||
Disulfide bond | 250↔277 | |||||
Sequence: CSRSDEVDDTPNQADPNFGCPSYPHVSC | ||||||
Disulfide bond | 269↔297 | |||||
Sequence: CPSYPHVSCSNGPNGDMFMNYMDYVDDKC | ||||||
Propeptide | PRO_0000280825 | 323-342 | Removed in mature form | |||
Sequence: RVEETEKKEAPSKREMPMPR |
Post-translational modification
The inactive zymogen pro-ulilysin undergoes calcium-mediated autolytic activation to the mature ulilysin. Autoproteolytic activation entails removal of the first 60 residues and of a highly charged 20-residue C-terminal tail.
Keywords
- PTM
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MAEKFESRGIEEASSEVPTQ | ||||||
Region | 323-342 | Disordered | ||||
Sequence: RVEETEKKEAPSKREMPMPR |
Domain
Consists of two subdomains separated by an active site cleft containing the catalytic zinc ion.
Sequence similarities
Belongs to the peptidase M43B family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length342
- Mass (Da)38,371
- Last updated2002-06-01 v1
- ChecksumB2480CD7BB2B9574
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE010299 EMBL· GenBank· DDBJ | AAM06585.1 EMBL· GenBank· DDBJ | Genomic DNA |