TRYP_SIMVI
ID TRYP_SIMVI Reviewed; 247 AA.
AC P35048;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Trypsin;
DE EC=3.4.21.4;
DE Flags: Precursor; Fragment;
OS Simulium vittatum (Striped black fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Simuliidae;
OC Simulium.
OX NCBI_TaxID=7192;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gut;
RX PubMed=8269093; DOI=10.1111/j.1365-2583.1993.tb00116.x;
RA Ramos A., Mahowald A., Jacobs-Lorena M.;
RT "Gut-specific genes from the black fly Simulium vittatum encoding trypsin-
RT like and carboxypeptidase-like proteins.";
RL Insect Mol. Biol. 1:149-163(1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Midgut.
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; L08428; AAA18530.2; -; mRNA.
DR AlphaFoldDB; P35048; -.
DR SMR; P35048; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL <1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..30
FT /note="Activation peptide"
FT /id="PRO_0000028299"
FT CHAIN 31..247
FT /note="Trypsin"
FT /id="PRO_0000028300"
FT DOMAIN 31..>247
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 76
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 61..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 185..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 212..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_TER 1
FT NON_TER 247
SQ SEQUENCE 247 AA; 26247 MW; 90891564E3BA5FCD CRC64;
LTTVISYFAL VAFALVGVSY ATPKASINGR IVGGEMTDIS LIPYQVSVQT AISSYGFIHH
CGGSIISPRW VVTAAHCAQK TNSAYQVYTG SSNKVEGGQA YRVKTIINHP LYDEETTDYD
VALLELAEPI VMNYKTAAIE LAEVGEEVET DAMAIVSGWG DTKNFGEEPN MLRSAEVPIF
DQELCAYLNA NHGVVTERMI CAGYLAGGRD SCQGDSGGPL AVDGKLVGIV SWGVGCAQSN
FPGVYGI
