ID   TRYB_MANSE              Reviewed;         256 AA.
AC   P35046;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Trypsin, alkaline B;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Midgut;
RX   PubMed=8205142; DOI=10.1016/0965-1748(94)90041-8;
RA   Peterson A.M., Barillas-Mury C.V., Wells M.A.;
RT   "Sequence of three cDNAs encoding an alkaline midgut trypsin from Manduca
RT   sexta.";
RL   Insect Biochem. Mol. Biol. 24:463-471(1994).
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}.
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DR   EMBL; L16806; AAA29340.1; -; mRNA.
DR   AlphaFoldDB; P35046; -.
DR   SMR; P35046; -.
DR   MEROPS; S01.420; -.
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:SF100; AT20289P-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; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..24
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028293"
FT   CHAIN           25..256
FT                   /note="Trypsin, alkaline B"
FT                   /id="PRO_0000028294"
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;  27549 MW;  2108BE041DB9CAE0 CRC64;
     MRLFLALLAL GFAAVAAVPA NPQRIVGGST TTIQQYPTIV ALLFSRNGNT FFQACGGIIL
     NNRNILTAAH CPHGDAVNRW RVRSGSTFAN SGGAVHNLNR VRIHPNYNSR TLDNDIAIMR
     TSSNIAFNNA AQPARIAGAN YNVGDNQVVW AAGWGDIRSG GPPSEQLRHV QVWTVNQATC
     RSRYASIGRS VTDNMLCSGW LDVGGRDQCQ GDSGGPLYHN GVVVGVSSWG EECALARFPG
     VNARVSRFAN WIRNNS
//