ID   TRYA3_LUCCU             Reviewed;         165 AA.
AC   P35043;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Trypsin alpha-3;
DE            EC=3.4.21.4;
DE   Flags: Fragment;
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7894748; DOI=10.1111/j.1365-2583.1994.tb00163.x;
RA   Casu R.E., Jarmey J.M., Elvin C.M., Eisemann C.H.;
RT   "Isolation of a trypsin-like serine protease gene family from the sheep
RT   blowfly Lucilia cuprina.";
RL   Insect Mol. Biol. 3:159-170(1994).
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; L15632; AAA65931.1; -; Genomic_DNA.
DR   AlphaFoldDB; P35043; -.
DR   SMR; P35043; -.
DR   MEROPS; S01.112; -.
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; -; 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; 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.
FT   CHAIN           <1..165
FT                   /note="Trypsin alpha-3"
FT                   /id="PRO_0000088717"
FT   DOMAIN          <1..163
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        26
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            113
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        115..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         1
SQ   SEQUENCE   165 AA;  16570 MW;  26160B1AFF80F1CD CRC64;
     NSGGVLVSVA AFKNHEGYNS KTMVNDIAVI RLSSSLTTSS TIKTIGLATA APANGAAATV
     SGWGTTSSGG SIPSQLRYVD VKIVGRTQCA SSTYGYGSEI KASMICAYTV GKDSCQGDSG
     GPLVSGGRLV GVVSWGYGCA AVNYPGVYAD VAALRSWVVS AANSV