ID   COG2_CARMA              Reviewed;          17 AA.
AC   P81609;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Collagenolytic protease;
DE            EC=3.4.21.32;
DE   AltName: Full=CSC;
DE   Flags: Fragment;
OS   Carcinus maenas (Common shore crab) (Green crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Portunoidea; Carcinidae; Carcinus.
OX   NCBI_TaxID=6759;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Digestive gland {ECO:0000269|PubMed:8896334};
RX   PubMed=8896334; DOI=10.1016/0305-0491(96)00090-9;
RA   Roy P., Colas B., Durand P.;
RT   "Purification, kinetical and molecular characterizations of a serine
RT   collagenolytic protease from greenshore crab (Carcinus maenas) digestive
RT   gland.";
RL   Comp. Biochem. Physiol. 115B:87-95(1996).
CC   -!- FUNCTION: Serine protease with chymotryptic, collagenolytic and SANA
CC       activities. {ECO:0000269|PubMed:8896334}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7-8.;
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.;
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8896334}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
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; P81609; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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   Secreted; Serine protease.
FT   CHAIN           1..>17
FT                   /note="Collagenolytic protease"
FT                   /id="PRO_0000088665"
FT   DOMAIN          1..>17
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         17
FT                   /evidence="ECO:0000303|PubMed:8896334"
SQ   SEQUENCE   17 AA;  1817 MW;  596E7281B91DA968 CRC64;
     IVGGMEATPH SWPHQVA