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P81609 (COG2_CARMA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 36. 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

EC=3.4.21.32
Alternative name(s):
CSC
OrganismCarcinus maenas (Common shore crab) (Green crab)
Taxonomic identifier6759 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataBrachyuraEubrachyuraPortunoideaPortunidaeCarcinus

Protein attributes

Sequence length17 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine protease with chymotryptic, collagenolytic and SANA activities. Ref.1

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. Ref.1

Subunit structure

Monomer. Ref.1

Subcellular location

Secretedextracellular space Ref.1.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7-8.

Temperature dependence:

Optimum temperature is 30 degrees Celsius.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentSecreted
   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

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – ›17›17Collagenolytic protease
PRO_0000088665

Regions

Domain1 – ›17›17Peptidase S1

Experimental info

Non-terminal residue171

Sequences

Sequence LengthMass (Da)Tools
P81609 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 596E7281B91DA968

FASTA171,817
        10 
IVGGMEATPH SWPHQVA 

« Hide

References

[1]"Purification, kinetical and molecular characterizations of a serine collagenolytic protease from greenshore crab (Carcinus maenas) digestive gland."
Roy P., Colas B., Durand P.
Comp. Biochem. Physiol. 115B:87-95(1996) [PubMed: 8896334] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Digestive gland.

Cross-references

3D structure databases

ModBaseSearch...

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 nameCOG2_CARMA
AccessionPrimary (citable) accession number: P81609
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2001
Last modified: November 16, 2011
This is version 36 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