ID   TRYA4_LUCCU             Reviewed;         255 AA.
AC   P35044;
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-4;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
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; AAA65932.1; -; Genomic_DNA.
DR   AlphaFoldDB; P35044; -.
DR   SMR; P35044; -.
DR   MEROPS; S01.110; -.
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; 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   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..30
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028289"
FT   CHAIN           31..255
FT                   /note="Trypsin alpha-4"
FT                   /id="PRO_0000028290"
FT   DOMAIN          31..253
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        71
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        116
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        209
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            203
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        179..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        205..229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   255 AA;  26119 MW;  5756AEDA78A3ED46 CRC64;
     MLKFVVLLCA ISCALGAAVP EGMVPQLDGR IVGGVATTIS SFPWQISLQR SGSHSCGGSV
     YNSRIIVTAA HCLQSVSTSV LKVRRGSSYW NSGGVVVSVA AFKNHEGYNP KTMVNDIAVI
     RLSSSLTMSS TIKAIALTTA APANGAAATV SGWGTTSSGG SIPAQLRYVD LKIVGRTQCA
     SSTYGYGSQI KPSMICAYTV GKDSCQGDSG GPLVSGGRLV GVVSWGYGCA FANYPGVYAD
     VAALRTWVVS AASSV