TRYDT_DROER
ID TRYDT_DROER Reviewed; 253 AA.
AC C0HKA5; P54626;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Trypsin delta {ECO:0000250|UniProtKB:C0HKA2};
DE EC=3.4.21.4 {ECO:0000255|PROSITE-ProRule:PRU00274};
DE Flags: Precursor;
GN Name=deltaTry {ECO:0000250|UniProtKB:C0HKA2};
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 {ECO:0000250|UniProtKB:P04814}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; U40653; AAA83243.1; -; Genomic_DNA.
DR AlphaFoldDB; C0HKA5; -.
DR SMR; C0HKA5; -.
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; -; 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; 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_0000028267"
FT CHAIN 31..253
FT /note="Trypsin delta"
FT /id="PRO_0000028268"
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:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT SITE 204
FT /note="Required for specificity"
FT /evidence="ECO:0000305"
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 253 AA; 25965 MW; 2768768E9396CA0D CRC64;
MLKFVILLSA VACALGGTIP EGLLPQLDGR IVGGTATTIS SFPWQISLQR SGSHSCGGSI
YTDRVIVTAA HCLQSVSTSS LQIRAGSSYW NSGGVTVKVS SFKNHEGYSA RTMVNDIAVI
RLSSSLSFSS TIKSISLASS NPPNGAAASV SGWGTQSSGS NSIPSQLQYV NVNIVSQSRC
ASSTYGYGSD IRDTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGQGC AYSNYPGVYA
SVADLRAWVV RNA
