P08897 · COGS_HYPLI
- ProteinCollagenase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids260 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
This enzyme is a serine protease capable of degrading the native triple helix of collagen. Also cleaves the B chain of insulin at the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl phosphate, 2-naphthyl butyrate, 2-naphthyl caprylate, 2-naphthyl myristate, L-leucine 2-2-naphthylamide, L-valine 2-naphthylamide, L-cysteine 2-naphthylamide or L-glutarylphenylalanine 2-naphthylamide.
Catalytic activity
Activity regulation
Inhibited by diisopropylfluorophosphate.
pH Dependence
Optimum pH is 8.0-8.5. Reversibly inactivated below pH 4.5.
Temperature Dependence
Thermostable. No loss of activity occurs after incubation for 2 hours at 60 degrees Celsius. Inactivated after incubation for 2 hours at 75 degrees Celsius, however 45% of activity remains after incubation for 20 minutes at 75 degrees Celsius.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 75 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 118 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 210 | Charge relay system | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | collagen catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCollagenase
- EC number
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Oestroidea > Oestridae > Hypodermatinae > Hypoderma
Accessions
- Primary accessionP08897
- Secondary accessions
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MKFLLVFALALATTSA | ||||||
Propeptide | PRO_0000027622 | 17-30 | ||||
Sequence: FQHPASIFELREGR | ||||||
Chain | PRO_0000027623 | 31-260 | Collagenase | |||
Sequence: IINGYEAYTGLFPYQAGLDITLQDQRRVWCGGSLIDNKWILTAAHCVHDAVSVVVYLGSAVQYEGEAVVNSERIISHSMFNPDTYLNDVALIKIPHVEYTDNIQPIRLPSGEELNNKFENIWATVSGWGQSNTDTVILQYTYNLVIDNDRCAQEYPPGIIVESTICGDTCDGKSPCFGDSGGPFVLSDKNLLIGVVSFVSGAGCESGKPVGFSRVTSYMDWIQQNTGIIF | ||||||
Disulfide bond | 60↔76 | |||||
Sequence: CGGSLIDNKWILTAAHC | ||||||
Disulfide bond | 181↔196 | |||||
Sequence: CAQEYPPGIIVESTIC | ||||||
Disulfide bond | 206↔234 | |||||
Sequence: CFGDSGGPFVLSDKNLLIGVVSFVSGAGC |
Keywords
- PTM
Expression
Developmental stage
Larval-specific.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-257 | Peptidase S1 | ||||
Sequence: IINGYEAYTGLFPYQAGLDITLQDQRRVWCGGSLIDNKWILTAAHCVHDAVSVVVYLGSAVQYEGEAVVNSERIISHSMFNPDTYLNDVALIKIPHVEYTDNIQPIRLPSGEELNNKFENIWATVSGWGQSNTDTVILQYTYNLVIDNDRCAQEYPPGIIVESTICGDTCDGKSPCFGDSGGPFVLSDKNLLIGVVSFVSGAGCESGKPVGFSRVTSYMDWIQQNTG |
Sequence similarities
Belongs to the peptidase S1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length260
- Mass (Da)28,579
- Last updated1998-07-15 v3
- ChecksumF8B1AF6350F2D74E
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 54 | in Ref. 4; AA sequence | ||||
Sequence: D → E | ||||||
Sequence conflict | 56-57 | in Ref. 4; AA sequence | ||||
Sequence: RR → QD | ||||||
Sequence conflict | 200 | in Ref. 2; BAB20995 and 3; AA sequence | ||||
Sequence: C → S | ||||||
Sequence conflict | 215-216 | in Ref. 5; AA sequence | ||||
Sequence: VL → SK | ||||||
Sequence conflict | 259 | in Ref. 3; AA sequence | ||||
Sequence: I → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X74306 EMBL· GenBank· DDBJ | CAA52359.1 EMBL· GenBank· DDBJ | mRNA | ||
AB054066 EMBL· GenBank· DDBJ | BAB20995.1 EMBL· GenBank· DDBJ | mRNA |