ID   TRYP_CHOFU              Reviewed;         256 AA.
AC   P35042;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Trypsin CFT-1;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
OS   Choristoneura fumiferana (Spruce budworm moth) (Archips fumiferana).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tortricoidea;
OC   Tortricidae; Tortricinae; Choristoneura.
OX   NCBI_TaxID=7141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8294037; DOI=10.1016/0378-1119(93)90501-s;
RA   Wang S., Magoulas C., Hickey D.A.;
RT   "Isolation and characterization of a full-length trypsin-encoding cDNA
RT   clone from the Lepidopteran insect, Choristoneura fumiferana.";
RL   Gene 136:375-376(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-69, AND CHARACTERIZATION.
RC   TISSUE=Gut juice;
RX   PubMed=8353523; DOI=10.1016/0965-1748(93)90040-y;
RA   Milne R., Kaplan H.;
RT   "Purification and characterization of a trypsin-like digestive enzyme from
RT   spruce budworm (Choristoneura fumiferana) responsible for the activation of
RT   delta-endotoxin from Bacillus thuringiensis.";
RL   Insect Biochem. Mol. Biol. 23:663-673(1993).
CC   -!- FUNCTION: Responsible for the activation of delta-endotoxin from
CC       Bacillus thuringiensis.
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; L04749; AAA81525.1; -; mRNA.
DR   AlphaFoldDB; P35042; -.
DR   SMR; P35042; -.
DR   MEROPS; S01.112; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..24
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:8353523"
FT                   /id="PRO_0000028257"
FT   CHAIN           25..256
FT                   /note="Trypsin CFT-1"
FT                   /id="PRO_0000028258"
FT   DOMAIN          25..256
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        70
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        115
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            207
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        180..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        209..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   256 AA;  27333 MW;  4C2A8CBA74CFEF67 CRC64;
     MRVTLALVAL CLASVAALPE KQQRIVGGSV TTIEQWPSGS ALLYSWNLVT YSQACGGAIL
     NTRSILSAAH CFIGDAANRW RIRTGSTWAN SGGVVHNTAL IIIHPSYNTR TLDNDIAILR
     SATTIAQNNQ ARPASIAGAN YNLADNQAVW AIGWGATCPG CAGSEQLRHI QIWTVNQNTC
     RSRYLEVGGT ITDNMLCSGW LDVGGRDQCQ GDSGGPLFHN NVVVGVCSWG QSCALARYPG
     VNARVSRFTA WIQANA
//