ID   COG1_PARCM              Reviewed;          20 AA.
AC   P20731;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Collagenolytic protease 28 kDa;
DE            EC=3.4.21.32;
DE   Flags: Fragment;
OS   Paralithodes camtschaticus (Red king crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Anomura;
OC   Paguroidea; Lithodidae; Paralithodes.
OX   NCBI_TaxID=6741;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Hepatopancreas;
RX   PubMed=2154979; DOI=10.1016/0006-291x(90)91024-m;
RA   Klimova O.A., Borukhov S.I., Solovyeva N.I., Balaevskaya T.O.,
RA   Strongin A.Y.;
RT   "The isolation and properties of collagenolytic proteases from crab
RT   hepatopancreas.";
RL   Biochem. Biophys. Res. Commun. 166:1411-1420(1990).
CC   -!- FUNCTION: This enzyme is a serine protease capable of degrading the
CC       native triple helix of collagen.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins, with broad specificity for peptide
CC         bonds. Native collagen is cleaved about 75% of the length of the
CC         molecule from the N-terminus. Low activity on small molecule
CC         substrates of both trypsin and chymotrypsin.; EC=3.4.21.32;
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   PIR; A34817; A34817.
DR   MEROPS; S01.122; -.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
PE   1: Evidence at protein level;
KW   Collagen degradation; Direct protein sequencing; Hydrolase; Protease;
KW   Serine protease.
FT   CHAIN           1..>20
FT                   /note="Collagenolytic protease 28 kDa"
FT                   /id="PRO_0000088666"
FT   DOMAIN          1..>20
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2088 MW;  299BAC6FC8A99AA2 CRC64;
     IVGGQEASPG SWPXQVGLFF