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P34156 (COG4_CHIOP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 48. 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 23 kDa

EC=3.4.24.7
OrganismChionoecetes opilio (Crab-beetle)
Taxonomic identifier41210 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataBrachyuraEubrachyuraMajoideaMajidaeChionoecetes

Protein attributes

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

General annotation (Comments)

Function

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

Catalytic activity

Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Sequence similarities

Belongs to the peptidase M12A family.

Ontologies

Keywords
   Biological processCollagen degradation
   LigandZinc
   Molecular functionHydrolase
Metalloprotease
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 functionmetallopeptidase 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 23 kDa
PRO_0000078184

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P34156 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 2BC7A93D022A97D8

FASTA202,110
        10         20 
AAILQDEYLX SGGVVPYVFG 

« Hide

References

[1]"Isolation and characteristics of collagenolytic enzymes from the hepatopancreas of the crab Chionoecetes opilio."
Klimova O.A., Vedishcheva Y.V., Strongin A.Y.
Dokl. Akad. Nauk SSSR 317:482-484(1991) [PubMed: 1663026] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Hepatopancreas.

Cross-references

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM12.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

PROSITEPS00142. ZINC_PROTEASE. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOG4_CHIOP
AccessionPrimary (citable) accession number: P34156
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 16, 2011
This is version 48 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