ID   TRYP_PHACE              Reviewed;         258 AA.
AC   O97399; P81524;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Trypsin;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
OS   Phaedon cochleariae (Mustard beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX   NCBI_TaxID=80249;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAA76929.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Larval gut {ECO:0000269|PubMed:10612046};
RX   PubMed=10612046; DOI=10.1016/s0965-1748(99)00104-6;
RA   Girard C., Jouanin L.;
RT   "Molecular cloning of cDNAs encoding a range of digestive enzymes from a
RT   phytophagous beetle, Phaedon cochleariae.";
RL   Insect Biochem. Mol. Biol. 29:1129-1142(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC         Evidence={ECO:0000250|UniProtKB:P35049};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P35049}.
CC   -!- TISSUE SPECIFICITY: Expressed in larval carcasses and gut, and adult
CC       gut. {ECO:0000269|PubMed:10612046}.
CC   -!- DEVELOPMENTAL STAGE: Ovarial and mature eggs, larvae and adult.
CC       {ECO:0000269|PubMed:10612046}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; Y17905; CAA76929.1; -; mRNA.
DR   AlphaFoldDB; O97399; -.
DR   SMR; O97399; -.
DR   MEROPS; S01.130; -.
DR   GO; GO:0005576; C:extracellular region; 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; Trypsin-like serine proteases; 1.
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   PANTHER; PTHR24264:SF42; TISSUE-TYPE PLASMINOGEN ACTIVATOR; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 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.
PE   2: Evidence at transcript level;
KW   Digestion; Disulfide bond; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..29
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000314681"
FT   CHAIN           30..258
FT                   /note="Trypsin"
FT                   /evidence="ECO:0000250|UniProtKB:P35049, ECO:0000255"
FT                   /id="PRO_5000147327"
FT   DOMAIN          30..257
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        70
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P35049"
FT   ACT_SITE        117
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P35049"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P35049"
FT   SITE            207
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250|UniProtKB:P35049"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        55..71
FT                   /evidence="ECO:0000250|UniProtKB:P35049,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        182..197
FT                   /evidence="ECO:0000250|UniProtKB:P35049,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        209..233
FT                   /evidence="ECO:0000250|UniProtKB:P35049,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   258 AA;  28071 MW;  BDBDFAFECB86866C CRC64;
     MIRFTLALAV IGVTFAASTP QIETNPNLEI IGGHDANIID YPWQISFQHR LHHFCGGFLI
     SDTWVVTAAH CIYEGYSDTE NLNIRVGSSE WSAKGKLHDV KRYITHPQYN ITTMDNDIAL
     LELALPVDLN QSVRPAKLPV AGQEIPDNAQ LTITGWGATY VGGYNEYTLQ VVTIPTVNIN
     VCQSAITNDT ITNNMFCAGL IGVGGKDSCS GDSGGPAVID GQVVGIVSWG YSCADPKYPG
     IYTKVSAFRD WINEETEI
//