ID   COG2_CHIOP              Reviewed;          20 AA.
AC   P34154;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Collagenolytic protease 35 kDa 2;
DE            EC=3.4.21.32;
DE   AltName: Full=Collagenolytic protease 35 kDa II;
DE   Flags: Fragment;
OS   Chionoecetes opilio (Crab-beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Majoidea; Majidae; Chionoecetes.
OX   NCBI_TaxID=41210;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Hepatopancreas;
RX   PubMed=1663026;
RA   Klimova O.A., Vedishcheva Y.V., Strongin A.Y.;
RT   "Isolation and characteristics of collagenolytic enzymes from the
RT   hepatopancreas of the crab Chionoecetes opilio.";
RL   Dokl. Akad. Nauk SSSR 317:482-484(1991).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P34154; -.
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.
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 35 kDa 2"
FT                   /id="PRO_0000088671"
FT   DOMAIN          1..>20
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2150 MW;  45A17C921B801016 CRC64;
     IVGGTEVTPG EIPYQLSFQD