ID   TRYX_GADMO              Reviewed;         241 AA.
AC   Q91041;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Trypsin-10;
DE            EC=3.4.21.4;
DE   AltName: Full=Trypsin X;
DE   Flags: Precursor;
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pyloric caecum;
RX   PubMed=8223632; DOI=10.1111/j.1432-1033.1993.tb18341.x;
RA   Gudmundsdottir A., Gudmundsdottir E., Oskarsson S., Bjarnason J.B.,
RA   Eakin A.E., Craik C.S.;
RT   "Isolation and characterization of cDNAs from Atlantic cod encoding two
RT   different forms of trypsinogen.";
RL   Eur. J. Biochem. 217:1091-1097(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; X76887; CAA54215.1; -; mRNA.
DR   PIR; S39048; S39048.
DR   AlphaFoldDB; Q91041; -.
DR   SMR; Q91041; -.
DR   STRING; 8049.ENSGMOP00000014559; -.
DR   MEROPS; S01.125; -.
DR   PRIDE; Q91041; -.
DR   Proteomes; UP000694546; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Digestion; Disulfide bond; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000255"
FT   PROPEP          14..19
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028311"
FT   CHAIN           20..241
FT                   /note="Trypsin-10"
FT                   /id="PRO_0000028312"
FT   DOMAIN          20..239
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        59
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        103
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        195
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            189
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        128..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        135..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        166..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        191..215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   241 AA;  25976 MW;  853D7C26BCAF9DD7 CRC64;
     MKSLIFVLLL GAVFAEEDKI VGGYECTRHS QAHQVSLNSG YHFCGGSLVS KDWVVSAAHC
     YKSVLRVRLG EHHIRVNEGT EQFISSSSVI RHPNYSSYNI DNDIMLIKLT EPATLNQYVH
     AVALPTECAA DATMCTVSGW GNTMSSVDDG DKLQCLNLPI LSHADCANSY PGMITQSMFC
     AGYLEGGKDS CQGDSGGPVV CNGVLQGVVS WGYGCAERDN PGVYAKVCVL SGWVRDTMAS
     Y