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Reviewed, UniProtKB/Swiss-Prot P34154 (COG2_CHIOP)

Last modified March 3, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Collagenolytic protease 35 kDa 2
    EC=3.4.21.32
Alternative name(s):
    Collagenolytic protease 35 kDa II
OrganismChionoecetes opilio (Crab-beetle)
Taxonomic identifier41210 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataBrachyuraEubrachyuraMajoideaMajidaeChionoecetes

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
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

   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 35 kDa 2
PRO_0000088671

Regions

Domain1 – ›20›20Peptidase S1

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P34154-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 45A17C921B801016

FASTA202,150
        10         20 
IVGGTEVTPG EIPYQLSFQD 

« 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...

Enzyme and pathway databases

BRENDA3.4.21.32. 299542.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. Partial match.
PS00134. TRYPSIN_HIS. Partial match.
PS00135. TRYPSIN_SER. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOG2_CHIOP
AccessionPrimary (citable) accession number: P34154
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: March 3, 2009
This is version 45 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents