ID   TRY2_SALSA              Reviewed;         231 AA.
AC   P35032;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Trypsin-2;
DE            EC=3.4.21.4;
DE   AltName: Full=Trypsin II;
DE   Flags: Precursor; Fragment;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=7556223; DOI=10.1111/j.1432-1033.1995.tb20860.x;
RA   Male R., Lorens J.B., Smals A.O., Torrissen K.R.;
RT   "Molecular cloning and characterization of anionic and cationic variants of
RT   trypsin from Atlantic salmon.";
RL   Eur. J. Biochem. 232:677-685(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
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; X70073; CAA49678.1; -; mRNA.
DR   PIR; S66658; S31778.
DR   AlphaFoldDB; P35032; -.
DR   SMR; P35032; -.
DR   MEROPS; S01.125; -.
DR   Proteomes; UP000087266; Genome assembly.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Calcium; Digestion; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          <1..4
FT                   /evidence="ECO:0000255"
FT   PROPEP          5..9
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028227"
FT   CHAIN           10..231
FT                   /note="Trypsin-2"
FT                   /id="PRO_0000028228"
FT   DOMAIN          10..229
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        49
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        93
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        185
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            179
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        16..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        34..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        118..218
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        125..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        156..170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        181..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         1
SQ   SEQUENCE   231 AA;  24823 MW;  C54A1CAFE74FAE18 CRC64;
     AAFATEDDKI VGGYECKAYS QPHQVSLNSG YHFCGGSLVN ENWVVSAAHC YQSRVEVRLG
     EHNIQVTEGS EQFISSSRVI RHPNYSSYNI DNDIMLIKLS KPATLNTYVQ PVALPTSCAP
     AGTMCTVSGW GNTMSSTADK NKLQCLNIPI LSYSDCNNSY PGMITNAMFC AGYLEGGKDS
     CQGDSGGPVV CNGELQGVVS WGYGCAEPGN PGVYAKVCIF NDWLTSTMAT Y