ID   TRYP_ASTAS              Reviewed;         237 AA.
AC   P00765;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Trypsin-1;
DE            EC=3.4.21.4;
DE   AltName: Full=Trypsin I;
OS   Astacus astacus (Noble crayfish) (Astacus fluviatilis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Astacoidea; Astacidae; Astacus.
OX   NCBI_TaxID=6715;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6838862; DOI=10.1021/bi00275a021;
RA   Titani K., Sasagawa T., Woodbury R.G., Ericsson L.H., Dorsam H.,
RA   Kraemer M., Neurath H., Zwilling R.;
RT   "Amino acid sequence of crayfish (Astacus fluviatilis) trypsin If.";
RL   Biochemistry 22:1459-1465(1983).
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   -!- MISCELLANEOUS: Trypsin I is one of five forms of the enzyme known to be
CC       present in crayfish. This protein is more acidic than mammalian
CC       trypsin.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   PIR; A00951; TRCY1.
DR   AlphaFoldDB; P00765; -.
DR   SMR; P00765; -.
DR   MEROPS; S01.035; -.
DR   GO; GO:0005576; C:extracellular region; 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; Trypsin-like serine proteases; 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   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF7; HYALIN; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Calcium; Digestion; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Metal-binding; Protease; Secreted; Serine protease.
FT   CHAIN           1..237
FT                   /note="Trypsin-1"
FT                   /id="PRO_0000088715"
FT   DOMAIN          1..237
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        45
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        96
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        189
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            183
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..46
FT   DISULFID        159..174
FT   DISULFID        185..213
SQ   SEQUENCE   237 AA;  25022 MW;  4072133E55022C76 CRC64;
     IVGGTDAVLG EFPYQLSFQE TFLGFSFHFC GASIYNENYA ITAGHCVYGD DYENPSGLQI
     VAGELDMSVN EGSEQTITVS KIILHENFDY DLLDNDISLL KLSGSLTFNN NVAPIALPAQ
     GHTATGNVIV TGWGTTSEGG NTPDVLQKVT VPLVSDAECR DDYGADEIFD SMICAGVPEG
     GKDSCQGDSG GPLAASDTGS TYLAGIVSWG YGCARPGYPG VYTEVSYHVD WIKANAV
//