Reviewed, UniProtKB/Swiss-Prot P20734 (COGC_PARCM)

Names and origin

Protein names	Recommended name:     Collagenolytic protease 36 kDa C     EC=3.4.21.32
Organism	Paralithodes camtschaticus (Red king crab)
Taxonomic identifier	6741 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Pleocyemata › Anomura › Paguroidea › Lithodidae › Paralithodes

Protein attributes

Sequence length	20 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	Collagen degradation
Molecular function	Hydrolase Protease Serine protease
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›20	›20	Collagenolytic protease 36 kDa C		PRO_0000088669
Regions
	Domain	1 – ›20	›20	Peptidase S1
Experimental info
	Non-terminal residue	20	1

Sequences

	Sequence		Length	Mass (Da)
	P20734-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: E9133891C9529B10	FASTA	20	2,129
	10 20 IVGGSEATSG QFPYQXSFQD

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
PIR	D34817.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	S01.122.
Enzyme and pathway databases
BRENDA	3.4.21.32. 39339.
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. Partial match. PS00134. TRYPSIN_HIS. Partial match. PS00135. TRYPSIN_SER. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COGC_PARCM

Accession

Primary (citable) accession number: P20734

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	March 24, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)