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P20734 (COGC_PARCM) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Collagenolytic protease 36 kDa C

EC=3.4.21.32
OrganismParalithodes camtschaticus (Red king crab)
Taxonomic identifier6741 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAnomuraPaguroideaLithodidaeParalithodes

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme is a serine protease capable of degrading the native triple helix of collagen.

Catalytic activity

Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processCollagen degradation
   Molecular functionHydrolase
Protease
Serine protease
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcollagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionserine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›20Collagenolytic protease 36 kDa C
PRO_0000088669

Regions

Domain1 – ›20›20Peptidase S1

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P20734 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: E9133891C9529B10

FASTA202,129
        10         20 
IVGGSEATSG QFPYQXSFQD 

« Hide

References

[1]"The isolation and properties of collagenolytic proteases from crab hepatopancreas."
Klimova O.A., Borukhov S.I., Solovyeva N.I., Balaevskaya T.O., Strongin A.Y.
Biochem. Biophys. Res. Commun. 166:1411-1420(1990) [PubMed: 2154979] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Hepatopancreas.

Cross-references

Sequence databases

PIRD34817.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSS01.122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

PROSITEPS50240. TRYPSIN_DOM. Partial match.
PS00134. TRYPSIN_HIS. Partial match.
PS00135. TRYPSIN_SER. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOGC_PARCM
AccessionPrimary (citable) accession number: P20734
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 16, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families