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 02-SEP-2026, entry version 197. 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: PRSS1; 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. 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; 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=36-93. 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=49-73. 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=35-93. 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 AlphaFoldDB; P00974; -. DR BMRB; P00974; -. DR MDposit; P00974; -. DR MDRepo; P00974; -. DR PCDDB; P00974; -. DR SASBDB; P00974; -. DR SMR; P00974; -. DR DIP; DIP-6113N; -. DR FunCoup; P00974; 83. DR IntAct; P00974; 6. DR MINT; P00974; -. DR STRING; 9913.ENSBTAP00000056883; -. DR Allergome; 3890; Bos d TI. DR MEROPS; I02.001; -. DR CPTAC; CPTAC-1472; -. DR PaxDb; 9913-ENSBTAP00000056883; -. DR InParanoid; P00974; -. DR EvolutionaryTrace; P00974; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0097180; C:serine protease inhibitor complex; IDA:CAFA. DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA. DR GO; GO:0140678; F:molecular function inhibitor activity; EXP:DisProt. 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:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; IDA:CACAO. DR CDD; cd22592; Kunitz_BPTI; 1. DR DisProt; DP00729; -. DR FunFam; 4.10.410.10:FF:000005; Pancreatic trypsin inhibitor; 1. DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1. DR InterPro; IPR002223; Kunitz_BPTI. DR InterPro; IPR036880; Kunitz_BPTI_sf. DR InterPro; IPR020901; Prtase_inh_Kunz-CS. DR InterPro; IPR050098; TFPI/VKTCI-like. DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1. DR PANTHER; PTHR10083:SF367; SPLEEN TRYPSIN INHIBITOR I; 1. DR Pfam; PF00014; Kunitz_BPTI; 1. DR PRINTS; PR00759; BASICPTASE. DR SMART; SM00131; KU; 1. DR SUPFAM; SSF57362; BPTI-like; 1. DR PROSITE; PS00280; BPTI_KUNITZ_1; 1. DR PROSITE; PS50279; BPTI_KUNITZ_2; 1. 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; -. 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 HELIX 42..44 FT /evidence="ECO:0007829|PDB:3WNY" 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 //