BPT1_BOVIN
ID BPT1_BOVIN Reviewed; 100 AA.
AC P00974;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Pancreatic trypsin inhibitor;
DE AltName: Full=Aprotinin;
DE AltName: Full=Basic protease inhibitor;
DE Short=BPI;
DE Short=BPTI;
DE Flags: Precursor;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2441071; DOI=10.1016/0022-2836(87)90711-x;
RA Creighton T.E., Charles I.G.;
RT "Sequences of the genes and polypeptide precursors for two bovine protease
RT inhibitors.";
RL J. Mol. Biol. 194:11-22(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2456884; DOI=10.1101/sqb.1987.052.01.058;
RA Creighton T.E., Charles I.G.;
RT "Biosynthesis, processing, and evolution of bovine pancreatic trypsin
RT inhibitor.";
RL Cold Spring Harb. Symp. Quant. Biol. 52:511-519(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-97.
RX PubMed=2420326; DOI=10.1042/bj2330443;
RA Kingston I.B., Anderson S.;
RT "Sequences encoding two trypsin inhibitors occur in strikingly similar
RT genomic environments.";
RL Biochem. J. 233:443-450(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-97.
RX PubMed=6580617; DOI=10.1073/pnas.80.22.6838;
RA Anderson S., Kingston I.B.;
RT "Isolation of a genomic clone for bovine pancreatic trypsin inhibitor by
RT using a unique-sequence synthetic DNA probe.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:6838-6842(1983).
RN [5]
RP PROTEIN SEQUENCE OF 36-93, AND DISULFIDE BONDS.
RX PubMed=5860161; DOI=10.1016/0006-291x(65)90601-7;
RA Kassell B., Laskowski M.;
RT "The basic trypsin inhibitor of bovine pancreas. V. The disulfide
RT linkages.";
RL Biochem. Biophys. Res. Commun. 20:463-468(1965).
RN [6]
RP PROTEIN SEQUENCE OF 36-93, AND DISULFIDE BONDS.
RX PubMed=5296424; DOI=10.1016/s0021-9258(18)96750-5;
RA Anderer F.A., Hornle S.;
RT "The disulfide linkages in kallikrein inactivator of bovine lung.";
RL J. Biol. Chem. 241:1568-1572(1966).
RN [7]
RP PROTEIN SEQUENCE OF 36-93, AND DISULFIDE BONDS.
RX PubMed=6053284;
RA Chauvet J., Acher R.;
RT "Covalent structure of a polypeptide inhibitor of trypsin (Kunitz and
RT Northrop inhibitor).";
RL Bull. Soc. Chim. Biol. 49:985-1000(1967).
RN [8]
RP PROTEIN SEQUENCE OF 36-93.
RA Dlouha V., Pospisilova D., Meloun B., Sorm F.;
RT "Sequence of residues 18-20 in pancreatic trypsin inhibitor.";
RL Collect. Czech. Chem. Commun. 33:1363-1365(1968).
RN [9]
RP PROTEIN SEQUENCE OF 36-81.
RC TISSUE=Adrenal chromaffin;
RX PubMed=2322242; DOI=10.1016/0006-291x(90)92058-8;
RA Lewis R.V., Ray P., Coguill R., Kruggel W.;
RT "Presence of pancreatic trypsin inhibitor in adrenal medullary chromaffin
RT cells.";
RL Biochem. Biophys. Res. Commun. 167:543-547(1990).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RA Deisenhofer J., Steigemann W.;
RT "Crystallographic refinement of the structure of bovine pancreatic trypsin
RT inhibitor at 1.5-A resolution.";
RL Acta Crystallogr. B 31:238-250(1975).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=5447861; DOI=10.1007/bf00599976;
RA Huber R., Kukla D., Ruhlmann A., Epp O., Formanek H.;
RT "The basic trypsin inhibitor of bovine pancreas. I. Structure analysis and
RT conformation of the polypeptide chain.";
RL Naturwissenschaften 57:389-392(1970).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT GLY-70.
RX PubMed=1714504; DOI=10.1016/0022-2836(91)90115-m;
RA Housset D., Kim K.-S., Fuchs J., Woodward C., Wlodawer A.;
RT "Crystal structure of a Y35G mutant of bovine pancreatic trypsin
RT inhibitor.";
RL J. Mol. Biol. 220:757-770(1991).
RN [13]
RP STRUCTURE BY NMR.
RX PubMed=1383552; DOI=10.1016/0022-2836(92)90222-6;
RA Berndt K.D., Guntert P., Orbons L.P.M., Wuethrich K.;
RT "Determination of a high-quality nuclear magnetic resonance solution
RT structure of the bovine pancreatic trypsin inhibitor and comparison with
RT three crystal structures.";
RL J. Mol. Biol. 227:757-775(1992).
CC -!- FUNCTION: Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
CC -!- INTERACTION:
CC P00974; P00760; NbExp=4; IntAct=EBI-1032263, EBI-986385;
CC P00974; Q52V24; Xeno; NbExp=5; IntAct=EBI-1032263, EBI-8755401;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PHARMACEUTICAL: Previously available under the name Trasylol (Mile).
CC Used for inhibiting coagulation so as to reduce blood loss during
CC bypass surgery.
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DR EMBL; M20934; AAD13685.1; -; Genomic_DNA.
DR EMBL; M20930; AAD13685.1; JOINED; Genomic_DNA.
DR EMBL; M20932; AAD13685.1; JOINED; Genomic_DNA.
DR EMBL; X03365; CAA27062.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X03365; CAA27063.1; -; Genomic_DNA.
DR EMBL; X05274; CAA28886.1; -; mRNA.
DR PIR; S00277; TIBO.
DR PDB; 1AAL; X-ray; 1.60 A; A/B=36-93.
DR PDB; 1B0C; X-ray; 2.80 A; A/B/C/D/E=36-91.
DR PDB; 1BHC; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=36-93.
DR PDB; 1BPI; X-ray; 1.09 A; A=36-93.
DR PDB; 1BPT; X-ray; 2.00 A; A=36-93.
DR PDB; 1BRB; X-ray; 2.10 A; I=36-93.
DR PDB; 1BTH; X-ray; 2.30 A; P/Q=36-93.
DR PDB; 1BTI; X-ray; 2.20 A; A=36-93.
DR PDB; 1BZ5; X-ray; 2.58 A; A/B/C/D/E=36-93.
DR PDB; 1BZX; X-ray; 2.10 A; I=36-93.
DR PDB; 1CBW; X-ray; 2.60 A; D/I=36-93.
DR PDB; 1CO7; X-ray; 1.90 A; I=2-100.
DR PDB; 1D0D; X-ray; 1.62 A; B=36-93.
DR PDB; 1EAW; X-ray; 2.93 A; B/D=36-93.
DR PDB; 1EJM; X-ray; 1.85 A; B/D/F=36-93.
DR PDB; 1F5R; X-ray; 1.65 A; I=36-100.
DR PDB; 1F7Z; X-ray; 1.55 A; I=36-100.
DR PDB; 1FAK; X-ray; 2.10 A; I=37-90.
DR PDB; 1FAN; X-ray; 2.00 A; A=36-93.
DR PDB; 1FY8; X-ray; 1.70 A; I=36-93.
DR PDB; 1G6X; X-ray; 0.86 A; A=36-93.
DR PDB; 1JV8; NMR; -; A=36-93.
DR PDB; 1JV9; NMR; -; A=36-93.
DR PDB; 1K09; NMR; -; A/B=50-73.
DR PDB; 1K6U; X-ray; 1.00 A; A=36-93.
DR PDB; 1LD5; NMR; -; A=36-93.
DR PDB; 1LD6; NMR; -; A=36-93.
DR PDB; 1MTN; X-ray; 2.80 A; D/H=36-93.
DR PDB; 1NAG; X-ray; 1.90 A; A=36-93.
DR PDB; 1OA5; NMR; -; 5=36-93.
DR PDB; 1OA6; NMR; -; 5=36-93.
DR PDB; 1P2I; X-ray; 1.65 A; I=36-93.
DR PDB; 1P2J; X-ray; 1.35 A; I=36-93.
DR PDB; 1P2K; X-ray; 1.60 A; I=36-93.
DR PDB; 1P2M; X-ray; 1.75 A; B/D=36-93.
DR PDB; 1P2N; X-ray; 1.80 A; B/D=36-93.
DR PDB; 1P2O; X-ray; 2.00 A; B/D=36-93.
DR PDB; 1P2Q; X-ray; 1.80 A; B/D=36-93.
DR PDB; 1PIT; NMR; -; A=36-93.
DR PDB; 1QLQ; X-ray; 1.42 A; A=36-93.
DR PDB; 1T7C; X-ray; 1.85 A; B/D=36-93.
DR PDB; 1T8L; X-ray; 1.75 A; B/D=36-93.
DR PDB; 1T8M; X-ray; 1.80 A; B/D=36-93.
DR PDB; 1T8N; X-ray; 1.75 A; B/D=36-93.
DR PDB; 1T8O; X-ray; 1.70 A; B/D=36-93.
DR PDB; 1TPA; X-ray; 1.90 A; I=36-93.
DR PDB; 1UUA; NMR; -; A=38-93.
DR PDB; 1UUB; NMR; -; A=38-93.
DR PDB; 1YKT; X-ray; 1.70 A; B=36-91.
DR PDB; 1YLC; X-ray; 1.70 A; B=36-91.
DR PDB; 1YLD; X-ray; 1.70 A; B=36-91.
DR PDB; 2FI3; X-ray; 1.58 A; I=36-93.
DR PDB; 2FI4; X-ray; 1.58 A; I=36-93.
DR PDB; 2FI5; X-ray; 1.58 A; I=36-93.
DR PDB; 2FTL; X-ray; 1.62 A; I=36-93.
DR PDB; 2FTM; X-ray; 1.65 A; B=36-93.
DR PDB; 2HEX; X-ray; 2.10 A; A/B/C/D/E=36-93.
DR PDB; 2IJO; X-ray; 2.30 A; I=36-93.
DR PDB; 2KAI; X-ray; 2.50 A; I=36-93.
DR PDB; 2PTC; X-ray; 1.90 A; I=36-93.
DR PDB; 2R9P; X-ray; 1.40 A; E/F/G/I=36-93.
DR PDB; 2RA3; X-ray; 1.46 A; C/I=36-93.
DR PDB; 2TGP; X-ray; 1.90 A; I=36-93.
DR PDB; 2TPI; X-ray; 2.10 A; I=36-93.
DR PDB; 2ZJX; X-ray; 1.09 A; A/B=36-93.
DR PDB; 2ZVX; X-ray; 1.09 A; A/B=36-93.
DR PDB; 3BTD; X-ray; 1.90 A; I=36-93.
DR PDB; 3BTE; X-ray; 1.85 A; I=36-93.
DR PDB; 3BTF; X-ray; 1.80 A; I=36-93.
DR PDB; 3BTG; X-ray; 1.90 A; I=36-93.
DR PDB; 3BTH; X-ray; 1.75 A; I=36-93.
DR PDB; 3BTK; X-ray; 1.85 A; I=36-93.
DR PDB; 3BTM; X-ray; 1.80 A; I=36-93.
DR PDB; 3BTQ; X-ray; 1.90 A; I=36-93.
DR PDB; 3BTT; X-ray; 1.90 A; I=36-93.
DR PDB; 3BTW; X-ray; 2.05 A; I=36-93.
DR PDB; 3FP6; X-ray; 1.49 A; I=36-93.
DR PDB; 3FP7; X-ray; 1.46 A; I=36-50, J=51-93.
DR PDB; 3FP8; X-ray; 1.46 A; I=36-93.
DR PDB; 3GYM; X-ray; 2.80 A; I/J=36-93.
DR PDB; 3LDI; X-ray; 2.20 A; A/B/C/D/E=36-93.
DR PDB; 3LDJ; X-ray; 1.70 A; A/B/C=36-93.
DR PDB; 3LDM; X-ray; 2.60 A; A/B/C/D/E=36-93.
DR PDB; 3OTJ; Other; 2.15 A; I=36-93.
DR PDB; 3P92; X-ray; 1.60 A; E=36-93.
DR PDB; 3P95; X-ray; 1.30 A; E=36-93.
DR PDB; 3TGI; X-ray; 1.80 A; I=36-100.
DR PDB; 3TGJ; X-ray; 2.20 A; I=36-100.
DR PDB; 3TGK; X-ray; 1.70 A; I=36-100.
DR PDB; 3TPI; X-ray; 1.90 A; I=36-93.
DR PDB; 3U1J; X-ray; 1.80 A; E=36-93.
DR PDB; 3WNY; X-ray; 1.30 A; A/B/C/E/F/G/H/I=36-95.
DR PDB; 4BNR; X-ray; 2.00 A; I/J=1-100.
DR PDB; 4DG4; X-ray; 1.40 A; C/E/F/H=36-93.
DR PDB; 4PTI; X-ray; 1.50 A; A=36-93.
DR PDB; 4TPI; X-ray; 2.20 A; I=36-93.
DR PDB; 4WWY; X-ray; 1.70 A; C/I=36-93.
DR PDB; 4WXV; X-ray; 2.10 A; C/I=36-90.
DR PDB; 4Y0Y; X-ray; 1.25 A; I=36-93.
DR PDB; 4Y0Z; X-ray; 1.37 A; I=36-93.
DR PDB; 4Y10; X-ray; 1.37 A; I=36-93.
DR PDB; 4Y11; X-ray; 1.30 A; I=36-93.
DR PDB; 5JB4; X-ray; 1.99 A; A/B/C=36-93.
DR PDB; 5JB5; X-ray; 1.60 A; A/B/C=36-93.
DR PDB; 5JB6; X-ray; 1.90 A; A/B/C=36-93.
DR PDB; 5JB7; X-ray; 1.90 A; A/B/C=36-93.
DR PDB; 5PTI; X-ray; 1.00 A; A=36-93.
DR PDB; 5XX2; X-ray; 1.12 A; A/B=36-93.
DR PDB; 5XX3; X-ray; 1.12 A; A/B=36-93.
DR PDB; 5XX4; X-ray; 1.67 A; A/B=36-93.
DR PDB; 5XX5; X-ray; 1.38 A; A/B=36-93.
DR PDB; 5XX6; X-ray; 1.31 A; A/B=36-93.
DR PDB; 5XX7; X-ray; 1.38 A; A/D=36-93.
DR PDB; 5XX8; X-ray; 1.30 A; A/B=36-93.
DR PDB; 5YVU; X-ray; 2.49 A; I=36-90.
DR PDB; 5YW1; X-ray; 2.60 A; I=36-90.
DR PDB; 6F1F; X-ray; 1.72 A; A/B/C/D/E=36-93.
DR PDB; 6PTI; X-ray; 1.70 A; A=36-93.
DR PDB; 7PH1; X-ray; 1.18 A; I=37-93.
DR PDB; 7PTI; X-ray; 1.60 A; A=36-93.
DR PDB; 7QIQ; X-ray; 1.85 A; D/H=36-93.
DR PDB; 7QIR; X-ray; 1.90 A; D/H=36-93.
DR PDB; 7QIS; X-ray; 1.83 A; D/H=36-93.
DR PDB; 7QIT; X-ray; 1.99 A; D/H=36-93.
DR PDB; 8PTI; X-ray; 1.80 A; A=36-93.
DR PDB; 9PTI; X-ray; 1.22 A; A=36-93.
DR PDBsum; 1AAL; -.
DR PDBsum; 1B0C; -.
DR PDBsum; 1BHC; -.
DR PDBsum; 1BPI; -.
DR PDBsum; 1BPT; -.
DR PDBsum; 1BRB; -.
DR PDBsum; 1BTH; -.
DR PDBsum; 1BTI; -.
DR PDBsum; 1BZ5; -.
DR PDBsum; 1BZX; -.
DR PDBsum; 1CBW; -.
DR PDBsum; 1CO7; -.
DR PDBsum; 1D0D; -.
DR PDBsum; 1EAW; -.
DR PDBsum; 1EJM; -.
DR PDBsum; 1F5R; -.
DR PDBsum; 1F7Z; -.
DR PDBsum; 1FAK; -.
DR PDBsum; 1FAN; -.
DR PDBsum; 1FY8; -.
DR PDBsum; 1G6X; -.
DR PDBsum; 1JV8; -.
DR PDBsum; 1JV9; -.
DR PDBsum; 1K09; -.
DR PDBsum; 1K6U; -.
DR PDBsum; 1LD5; -.
DR PDBsum; 1LD6; -.
DR PDBsum; 1MTN; -.
DR PDBsum; 1NAG; -.
DR PDBsum; 1OA5; -.
DR PDBsum; 1OA6; -.
DR PDBsum; 1P2I; -.
DR PDBsum; 1P2J; -.
DR PDBsum; 1P2K; -.
DR PDBsum; 1P2M; -.
DR PDBsum; 1P2N; -.
DR PDBsum; 1P2O; -.
DR PDBsum; 1P2Q; -.
DR PDBsum; 1PIT; -.
DR PDBsum; 1QLQ; -.
DR PDBsum; 1T7C; -.
DR PDBsum; 1T8L; -.
DR PDBsum; 1T8M; -.
DR PDBsum; 1T8N; -.
DR PDBsum; 1T8O; -.
DR PDBsum; 1TPA; -.
DR PDBsum; 1UUA; -.
DR PDBsum; 1UUB; -.
DR PDBsum; 1YKT; -.
DR PDBsum; 1YLC; -.
DR PDBsum; 1YLD; -.
DR PDBsum; 2FI3; -.
DR PDBsum; 2FI4; -.
DR PDBsum; 2FI5; -.
DR PDBsum; 2FTL; -.
DR PDBsum; 2FTM; -.
DR PDBsum; 2HEX; -.
DR PDBsum; 2IJO; -.
DR PDBsum; 2KAI; -.
DR PDBsum; 2PTC; -.
DR PDBsum; 2R9P; -.
DR PDBsum; 2RA3; -.
DR PDBsum; 2TGP; -.
DR PDBsum; 2TPI; -.
DR PDBsum; 2ZJX; -.
DR PDBsum; 2ZVX; -.
DR PDBsum; 3BTD; -.
DR PDBsum; 3BTE; -.
DR PDBsum; 3BTF; -.
DR PDBsum; 3BTG; -.
DR PDBsum; 3BTH; -.
DR PDBsum; 3BTK; -.
DR PDBsum; 3BTM; -.
DR PDBsum; 3BTQ; -.
DR PDBsum; 3BTT; -.
DR PDBsum; 3BTW; -.
DR PDBsum; 3FP6; -.
DR PDBsum; 3FP7; -.
DR PDBsum; 3FP8; -.
DR PDBsum; 3GYM; -.
DR PDBsum; 3LDI; -.
DR PDBsum; 3LDJ; -.
DR PDBsum; 3LDM; -.
DR PDBsum; 3OTJ; -.
DR PDBsum; 3P92; -.
DR PDBsum; 3P95; -.
DR PDBsum; 3TGI; -.
DR PDBsum; 3TGJ; -.
DR PDBsum; 3TGK; -.
DR PDBsum; 3TPI; -.
DR PDBsum; 3U1J; -.
DR PDBsum; 3WNY; -.
DR PDBsum; 4BNR; -.
DR PDBsum; 4DG4; -.
DR PDBsum; 4PTI; -.
DR PDBsum; 4TPI; -.
DR PDBsum; 4WWY; -.
DR PDBsum; 4WXV; -.
DR PDBsum; 4Y0Y; -.
DR PDBsum; 4Y0Z; -.
DR PDBsum; 4Y10; -.
DR PDBsum; 4Y11; -.
DR PDBsum; 5JB4; -.
DR PDBsum; 5JB5; -.
DR PDBsum; 5JB6; -.
DR PDBsum; 5JB7; -.
DR PDBsum; 5PTI; -.
DR PDBsum; 5XX2; -.
DR PDBsum; 5XX3; -.
DR PDBsum; 5XX4; -.
DR PDBsum; 5XX5; -.
DR PDBsum; 5XX6; -.
DR PDBsum; 5XX7; -.
DR PDBsum; 5XX8; -.
DR PDBsum; 5YVU; -.
DR PDBsum; 5YW1; -.
DR PDBsum; 6F1F; -.
DR PDBsum; 6PTI; -.
DR PDBsum; 7PH1; -.
DR PDBsum; 7PTI; -.
DR PDBsum; 7QIQ; -.
DR PDBsum; 7QIR; -.
DR PDBsum; 7QIS; -.
DR PDBsum; 7QIT; -.
DR PDBsum; 8PTI; -.
DR PDBsum; 9PTI; -.
DR AlphaFoldDB; P00974; -.
DR BMRB; P00974; -.
DR PCDDB; P00974; -.
DR SASBDB; P00974; -.
DR SMR; P00974; -.
DR DIP; DIP-6113N; -.
DR IntAct; P00974; 6.
DR MINT; P00974; -.
DR Allergome; 3890; Bos d TI.
DR MEROPS; I02.001; -.
DR CPTAC; CPTAC-1472; -.
DR PRIDE; P00974; -.
DR EvolutionaryTrace; P00974; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0097180; C:serine protease inhibitor complex; IDA:CAFA.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR GO; GO:0019870; F:potassium channel inhibitor activity; IDA:AgBase.
DR GO; GO:0002020; F:protease binding; IDA:CAFA.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:CAFA.
DR GO; GO:0043199; F:sulfate binding; IDA:CAFA.
DR GO; GO:0035375; F:zymogen binding; IDA:CAFA.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; IDA:CACAO.
DR GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IDA:CAFA.
DR GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; IDA:CACAO.
DR GO; GO:0032023; P:trypsinogen activation; IDA:CAFA.
DR CDD; cd00109; KU; 1.
DR DisProt; DP00729; -.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Pharmaceutical;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..35
FT /id="PRO_0000016852"
FT CHAIN 36..93
FT /note="Pancreatic trypsin inhibitor"
FT /id="PRO_0000016853"
FT PROPEP 94..100
FT /id="PRO_0000016854"
FT DOMAIN 40..90
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 50..51
FT /note="Reactive bond for trypsin"
FT DISULFID 40..90
FT DISULFID 49..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT ECO:0000269|PubMed:5296424"
FT DISULFID 65..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT ECO:0000269|PubMed:5296424"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1G6X"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1JV9"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1G6X"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:1G6X"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1G6X"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1G6X"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:8PTI"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1G6X"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1G6X"
SQ SEQUENCE 100 AA; 10903 MW; 6A778A4AD763FB19 CRC64;
MKMSRLCLSV ALLVLLGTLA ASTPGCDTSN QAKAQRPDFC LEPPYTGPCK ARIIRYFYNA
KAGLCQTFVY GGCRAKRNNF KSAEDCMRTC GGAIGPWENL
