ID   TRYP_SARBU              Reviewed;         254 AA.
AC   P51588;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Trypsin;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
OS   Sarcophaga bullata (Grey flesh fly) (Neobellieria bullata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Sarcophagidae; Sarcophaga; Neobellieria.
OX   NCBI_TaxID=7385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-36, AND 3D-STRUCTURE
RP   MODELING.
RC   TISSUE=Gut;
RX   PubMed=8620885; DOI=10.1111/j.1432-1033.1996.0279n.x;
RA   Borovsky D., Janssen I., Vanden Broeck J., Huybrechts R., Verhaert P.,
RA   de Bondt H.L., Bylemans D., de Loof A.;
RT   "Molecular sequencing and modeling of Neobellieria bullata trypsin.
RT   Evidence for translational control by Neobellieria trypsin-modulating
RT   oostatic factor.";
RL   Eur. J. Biochem. 237:279-287(1996).
CC   -!- FUNCTION: Involved in digestion of a protein meal.
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; X94691; CAA64354.1; -; mRNA.
DR   PIR; S65465; S65465.
DR   AlphaFoldDB; P51588; -.
DR   SMR; P51588; -.
DR   MEROPS; S01.A85; -.
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; -; 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   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   1: Evidence at protein level;
KW   Digestion; Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..26
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:8620885"
FT                   /id="PRO_0000028297"
FT   CHAIN           27..254
FT                   /note="Trypsin"
FT                   /id="PRO_0000028298"
FT   DOMAIN          27..252
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        68
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        113
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        208
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            202
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        154..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        178..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        204..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   254 AA;  27309 MW;  F07542C0EC1452AE CRC64;
     MLRFIAVFAL VNCALAGTLP NDLDGRIVNG VDTTIEAHPY QVPLQNAALS HFCGGSIISE
     DLVVTAAHCM QSYTASQIKV RLGSTIYNEG GELVSVKAFK FHEGYNPKTM VNDVALIKLA
     TPVRESSKIR YIRLADRTPP TGTPAVVTGW GTKCFLTCVS LPKTLQEVEV DIVDQKACAS
     NEFKYGSQIQ DTMVCAYALK KDACQGDSGG PLVANNQLVG IVSWGSGCAR VGYPGVFCDV
     PSVRSWIEKT AKEL