P08897 · COGS_HYPLI

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

  • Hydrolysis of proteins including native collagen at Xaa-|-Ala bond leaving an N-terminal (75%) and a C-terminal (25%) fragment.
    EC:3.4.21.49 (UniProtKB | ENZYME | Rhea)

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.

TypeIDPosition(s)Description
Active site75Charge relay system
Active site118Charge relay system
Active site210Charge relay system

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionserine-type endopeptidase activity
Biological Processcollagen catabolic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Collagenase
  • EC number
  • Alternative names
    • Hypodermin C (HC)

Organism names

Accessions

  • Primary accession
    P08897
  • Secondary accessions
    • Q25083
    • Q9BPQ4

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-16
PropeptidePRO_000002762217-30
ChainPRO_000002762331-260Collagenase
Disulfide bond60↔76
Disulfide bond181↔196
Disulfide bond206↔234

Keywords

Expression

Developmental stage

Larval-specific.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain31-257Peptidase S1

Sequence similarities

Belongs to the peptidase S1 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    260
  • Mass (Da)
    28,579
  • Last updated
    1998-07-15 v3
  • Checksum
    F8B1AF6350F2D74E
MKFLLVFALALATTSAFQHPASIFELREGRIINGYEAYTGLFPYQAGLDITLQDQRRVWCGGSLIDNKWILTAAHCVHDAVSVVVYLGSAVQYEGEAVVNSERIISHSMFNPDTYLNDVALIKIPHVEYTDNIQPIRLPSGEELNNKFENIWATVSGWGQSNTDTVILQYTYNLVIDNDRCAQEYPPGIIVESTICGDTCDGKSPCFGDSGGPFVLSDKNLLIGVVSFVSGAGCESGKPVGFSRVTSYMDWIQQNTGIIF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict54in Ref. 4; AA sequence
Sequence conflict56-57in Ref. 4; AA sequence
Sequence conflict200in Ref. 2; BAB20995 and 3; AA sequence
Sequence conflict215-216in Ref. 5; AA sequence
Sequence conflict259in Ref. 3; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X74306
EMBL· GenBank· DDBJ
CAA52359.1
EMBL· GenBank· DDBJ
mRNA
AB054066
EMBL· GenBank· DDBJ
BAB20995.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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