ID   COG4_CHIOP              Reviewed;          20 AA.
AC   P34156;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Collagenolytic protease 23 kDa;
DE            EC=3.4.24.7;
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 metal protease capable of degrading the
CC       native triple helix of collagen.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of the triple helix of collagen at about three-
CC         quarters of the length of the molecule from the N-terminus, at 775-
CC         Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates
CC         and alpha-macroglobulins at bonds where P1' is a hydrophobic
CC         residue.; EC=3.4.24.7;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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   MEROPS; M12.001; -.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   PROSITE; PS51864; ASTACIN; 1.
PE   1: Evidence at protein level;
KW   Collagen degradation; Direct protein sequencing; Hydrolase;
KW   Metalloprotease; Protease; Zinc.
FT   CHAIN           1..>20
FT                   /note="Collagenolytic protease 23 kDa"
FT                   /id="PRO_0000078184"
FT   DOMAIN          1..>20
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2110 MW;  2BC7A93D022A97D8 CRC64;
     AAILQDEYLX SGGVVPYVFG