COG1_CHIOP
ID COG1_CHIOP Reviewed; 20 AA.
AC P34153;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Collagenolytic protease 25 kDa II/III;
DE EC=3.4.21.32;
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}.
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DR AlphaFoldDB; P34153; -.
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.
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 25 kDa II/III"
FT /id="PRO_0000088670"
FT DOMAIN 1..>20
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 20
SQ SEQUENCE 20 AA; 2204 MW; CE0D7B996E7281A7 CRC64;
IVGGQEATPH TWVHQVALFI