ID   TRYZ_DROER              Reviewed;         281 AA.
AC   P54630;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=Trypsin zeta;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
GN   Name=zetaTry;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U40653; AAA83236.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54630; -.
DR   SMR; P54630; -.
DR   MEROPS; S01.116; -.
DR   eggNOG; KOG3627; Eukaryota.
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: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   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-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.
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..23
FT                   /evidence="ECO:0000305"
FT   PROPEP          24..39
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028285"
FT   CHAIN           40..281
FT                   /note="Trypsin zeta"
FT                   /id="PRO_0000028286"
FT   DOMAIN          40..279
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        88
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        135
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        235
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            229
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        199..219
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        231..255
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   281 AA;  29736 MW;  A1E0BC1812AAD468 CRC64;
     MSSSSWLGCL LAVLLSALAL SQGLPLLEDL DENSFPDGRI VGGYVTDIAQ VPYQITLRYK
     AISSPENPFR HRCGGSIVNE TTILTAAHCV IGTVASQFKV VAGTNFQTGT DGVITNVKRV
     IMHEGYNSGA AYNNDIAVLF VDPPLPLNNF TIKAIKLATE PPLDGAPSKI SGWGSTYPGG
     YSSNQLLAVD VPIVGNDLCD LDYENFIDET YHITSAMLCA GKRGVGGADA CQGDSGGPLV
     VRDELHGVVS WGNSCALPNY PGVYANVAFL RPWIDAVRAG L
//