ID   TRYU_DROER              Reviewed;         258 AA.
AC   P54629;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Trypsin eta;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
GN   Name=etaTry;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10486967; DOI=10.1093/oxfordjournals.molbev.a026202;
RA   Wang S., Magoulas C., Hickey D.A.;
RT   "Concerted evolution within a trypsin gene cluster in Drosophila.";
RL   Mol. Biol. Evol. 16:1117-1124(1999).
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; U40653; AAA83237.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54629; -.
DR   SMR; P54629; -.
DR   STRING; 7220.FBpp0141209; -.
DR   MEROPS; S01.117; -.
DR   eggNOG; KOG3627; Eukaryota.
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: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; 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; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..27
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028281"
FT   CHAIN           28..258
FT                   /note="Trypsin eta"
FT                   /id="PRO_0000028282"
FT   DOMAIN          28..258
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        74
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        120
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        215
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            209
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        185..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        211..235
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   258 AA;  27343 MW;  4D45051AF8F58145 CRC64;
     MNKVILRILA LLFLLGIGAV SAQPDGRIVG GADTTNYHTK YVVQLRRRSS PSSSYAQTCG
     GCILDAVTIA TAAHCVYNRE AENFLVVAGD DSRGGMSGVV VRVSKLIPHE LYNATIMDND
     IALVIVDPPL PLASSSTMEA IEIAAEQPAV GVQATISGWG YTKENGLSSD QLQQVNVPVV
     DSEKCQEAYY WRPISEGMLC AGLSEGGKDA CQGDSGGPLV VANKLAGIVS WGEGCARPNY
     PGVYANVAYF KDWIASRV