TRYA_MANSE
ID TRYA_MANSE Reviewed; 256 AA.
AC P35045;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Trypsin, alkaline A;
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; L16805; AAA29339.1; -; mRNA.
DR PIR; T10109; T10109.
DR AlphaFoldDB; P35045; -.
DR SMR; P35045; -.
DR MEROPS; S01.420; -.
DR BRENDA; 3.4.21.4; 3173.
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..17
FT /evidence="ECO:0000255"
FT PROPEP 18..24
FT /note="Activation peptide"
FT /id="PRO_0000028291"
FT CHAIN 25..256
FT /note="Trypsin, alkaline A"
FT /id="PRO_0000028292"
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; 27643 MW; 8E9FEBB979790814 CRC64;
MRLFLALLAL GFAAVAAVPA YPQRIVGGST TTIQQYPTIV ALLFSRNGNT FFQACGGIIL
NNRNVLTAAH CPHGDAVNRW RVRSGSTYAN SGGAVHNLNR VRIHPNFNRR TLDNDIAIMR
TTSNIAFNNA AQPARIAGAN YNLGDNQVVW AAGWGAIRSG GPSSEQLRHV QVWTVNQATC
RSRYASIGRS VTDNMLCSGW LDVGGRDQCQ GDSGGPLYHN GVVVGVCSWG EECALARFPG
VNARVSRFAN WIRNNS
