ID   I7D523_HELVI            Unreviewed;       263 AA.
AC   I7D523;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Trypsin {ECO:0000313|EMBL:AFO68325.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:AFO68325.1};
RN   [1] {ECO:0000313|EMBL:AFO68325.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T16h8 {ECO:0000313|EMBL:AFO68325.1};
RX   PubMed=22824002; DOI=10.1016/j.jip.2012.07.003;
RA   Zhu Y.C., Guo Z., Abel C.;
RT   "Cloning eleven midgut trypsin cDNAs and evaluating the interaction of
RT   proteinase inhibitors with Cry1Ac against the tobacco budworm, Heliothis
RT   virescens (F.) (Lepidoptera: Noctuidae).";
RL   J. Invertebr. Pathol. 111:111-120(2012).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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DR   EMBL; JN793545; AFO68325.1; -; mRNA.
DR   AlphaFoldDB; I7D523; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..263
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013062304"
FT   DOMAIN          23..263
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   263 AA;  27984 MW;  B7A6FD56519B764E CRC64;
     MRAVILLTLL GSALAVPKSI NRIVGGTPTT VEAYPYMSNM QYGFWGIWWY QACGGSLLTS
     TSILSAAHCY FGDAPSTWQV RLGTSLASSG GTLHTVSQLV LHPGYSSATL DHDVAIVRLT
     IPATFSNTIQ PASIPGSSYS LPDNTLLTTV GWGTLSSGGG SPEQLQHVDI NSINQELCAE
     RYAFLMTQPG YQNWPDITDN MLCAGILDVG GKDACQGDSG GPLAHNSNII VSVVSWGFQC
     ADPFYPGVNA RVSRYTDWIV ANA
//