TRYE_DROER
ID TRYE_DROER Reviewed; 256 AA.
AC P54627;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Trypsin epsilon;
DE EC=3.4.21.4;
DE Flags: Precursor;
GN Name=epsilonTry;
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; AAA83240.1; -; Genomic_DNA.
DR AlphaFoldDB; P54627; -.
DR SMR; P54627; -.
DR STRING; 7220.FBpp0141206; -.
DR MEROPS; S01.A82; -.
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; 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..22
FT /evidence="ECO:0000305"
FT PROPEP 23..30
FT /note="Activation peptide"
FT /id="PRO_0000028271"
FT CHAIN 31..256
FT /note="Trypsin epsilon"
FT /id="PRO_0000028272"
FT DOMAIN 31..254
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 210
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 204
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 56..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 180..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 206..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 256 AA; 27612 MW; 6A9193173D0E37F5 CRC64;
MLKIAVLLSV LACALAGTIP DGLLPQLDGR IVGGYETSID AHPYQVSLQR FGSHFCGGSI
YSHDIVITAA HCLQSVDAKD LKIRVGSTYW RSGGSVHSVR SFRNHEGYNA RTMVNDIAIV
RIESDLSFRS SIRAVRIADH NPREGATAVV SGWGTTESGG STIPDHLLAV DLEIVDVSRC
RSGEFGYGKK IKDTMLCAYA PNKDACQGDS GGPLVSGDRL VGVVSWGYGC GDVRYPGVYA
DVAHFHEWIE RTAREV
