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Reviewed, UniProtKB/Swiss-Prot P00974 (BPT1_BOVIN)

Last modified November 25, 2008. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Pancreatic trypsin inhibitor
Alternative name(s):
    Basic protease inhibitor
      Short name=BPTI
      Short name=BPI
    Aprotinin
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length100 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.

Subcellular location

Secreted.

Pharmaceutical use

Available under the name Trasylol (Mile). Used for inhibiting coagulation so as to reduce blood loss during bypass surgery.

Sequence similarities

Contains 1 BPTI/Kunitz inhibitor domain.

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Ontologies

Keywords

   Cellular componentSecreted
   DomainSignal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   Technical term3D-structure
Direct protein sequencing
Pharmaceutical

Gene Ontology (GO)

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionserine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 3514
PRO_0000016852
Chain36 – 9358Pancreatic trypsin inhibitor
PRO_0000016853
Propeptide94 – 1007
PRO_0000016854

Regions

Domain40 – 9051BPTI/Kunitz inhibitor

Sites

Site50 – 512Reactive bond for trypsin

Amino acid modifications

Disulfide bond40 ↔ 90
Disulfide bond49 ↔ 73
Disulfide bond65 ↔ 86

Secondary structure

1 ............ 100
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00974-1 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 6A778A4AD763FB19

FASTA10010,903
        10         20         30         40         50         60 
MKMSRLCLSV ALLVLLGTLA ASTPGCDTSN QAKAQRPDFC LEPPYTGPCK ARIIRYFYNA 

        70         80         90        100 
KAGLCQTFVY GGCRAKRNNF KSAEDCMRTC GGAIGPWENL

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References

[1]"Sequences of the genes and polypeptide precursors for two bovine protease inhibitors."
Creighton T.E., Charles I.G.
J. Mol. Biol. 194:11-22(1987) [PubMed: 2441071] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"Biosynthesis, processing, and evolution of bovine pancreatic trypsin inhibitor."
Creighton T.E., Charles I.G.
Cold Spring Harb. Symp. Quant. Biol. 52:511-519(1987) [PubMed: 2456884] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"Sequences encoding two trypsin inhibitors occur in strikingly similar genomic environments."
Kingston I.B., Anderson S.
Biochem. J. 233:443-450(1986) [PubMed: 2420326] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-97.
[4]"Isolation of a genomic clone for bovine pancreatic trypsin inhibitor by using a unique-sequence synthetic DNA probe."
Anderson S., Kingston I.B.
Proc. Natl. Acad. Sci. U.S.A. 80:6838-6842(1983) [PubMed: 6580617] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-97.
[5]"The basic trypsin inhibitor of bovine pancreas. V. The disulfide linkages."
Kassell B., Laskowski M.
Biochem. Biophys. Res. Commun. 20:463-468(1965) [PubMed: 5860161] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-93, DISULFIDE BONDS.
[6]"The disulfide linkages in kallikrein inactivator of bovine lung."
Anderer F.A., Hornle S.
J. Biol. Chem. 241:1568-1572(1966) [PubMed: 5296424] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-93, DISULFIDE BONDS.
[7]"Covalent structure of a polypeptide inhibitor of trypsin (Kunitz and Northrop inhibitor)."
Chauvet J., Acher R.
Bull. Soc. Chim. Biol. 49:985-1000(1967) [PubMed: 6053284] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-93, DISULFIDE BONDS.
[8]"Sequence of residues 18-20 in pancreatic trypsin inhibitor."
Dlouha V., Pospisilova D., Meloun B., Sorm F.
Collect. Czech. Chem. Commun. 33:1363-1365(1968)
Cited for: PROTEIN SEQUENCE OF 36-93.
[9]"Presence of pancreatic trypsin inhibitor in adrenal medullary chromaffin cells."
Lewis R.V., Ray P., Coguill R., Kruggel W.
Biochem. Biophys. Res. Commun. 167:543-547(1990) [PubMed: 2322242] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-81.
Tissue: Adrenal chromaffin.
[10]"Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5-A resolution."
Deisenhofer J., Steigemann W.
Acta Crystallogr. B 31:238-250(1975)
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[11]"The basic trypsin inhibitor of bovine pancreas. I. Structure analysis and conformation of the polypeptide chain."
Huber R., Kukla D., Ruhlmann A., Epp O., Formanek H.
Naturwissenschaften 57:389-392(1970) [PubMed: 5447861] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[12]"Crystal structure of a Y35G mutant of bovine pancreatic trypsin inhibitor."
Housset D., Kim K.-S., Fuchs J., Woodward C., Wlodawer A.
J. Mol. Biol. 220:757-770(1991) [PubMed: 1714504] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT GLY-70.
[13]"Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures."
Berndt K.D., Guntert P., Orbons L.P.M., Wuethrich K.
J. Mol. Biol. 227:757-775(1992) [PubMed: 1383552] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

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Web resources

Trasylol

Clinical information on Trasylol

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Cross-references

Sequence databases

M20934, M20930, M20932 Genomic DNA. Translation: AAD13685.1.
X03365 Genomic DNA. Translation: CAA27062.1. Sequence problems.
X03365 Genomic DNA. Translation: CAA27063.1.
X05274 mRNA. Translation: CAA28886.1.
PIRTIBO. S00277.
UniGeneBt.28518
Bt.53163

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AALX-ray1.60A/B36-93[»]
1B0CX-ray2.80A/B/C/D/E36-93[»]
1BHCX-ray2.70A/B/C/D/E/F/G/H/I/J36-93[»]
1BPIX-ray1.09A36-93[»]
1BPTX-ray2.00A36-93[»]
1BRBX-ray2.10I42-93[»]
1BTHX-ray2.30P/Q36-93[»]
1BTIX-ray2.20A36-93[»]
1BZ5X-ray2.58A/B/C/D/E36-93[»]
1BZXX-ray2.10I36-93[»]
1CBWX-ray2.60D/I36-93[»]
1CO7X-ray1.90I2-100[»]
1D0DX-ray1.62B36-93[»]
1EAWX-ray2.93B/D36-93[»]
1EJMX-ray1.85B/D/F36-93[»]
1F5RX-ray1.65I36-100[»]
1F7ZX-ray1.55I36-100[»]
1FAKX-ray2.10I37-90[»]
1FANX-ray2.00A36-93[»]
1FY8X-ray1.70I36-93[»]
1G6XX-ray0.86A36-93[»]
1JV8NMR-A36-93[»]
1JV9NMR-A36-93[»]
1K09NMR-A/B50-73[»]
1K6UX-ray1.00A36-93[»]
1LD5NMR-A36-93[»]
1LD6NMR-A36-93[»]
1MTNX-ray2.80D/H36-93[»]
1NAGX-ray1.90A36-93[»]
1OA5NMR-536-93[»]
1OA6NMR-536-93[»]
1P2IX-ray1.65I36-93[»]
1P2JX-ray1.35I36-93[»]
1P2KX-ray1.60I36-93[»]
1P2MX-ray1.75B/D36-93[»]
1P2NX-ray1.80B/D36-93[»]
1P2OX-ray2.00B/D36-93[»]
1P2QX-ray1.80B/D36-93[»]
1PITNMR-A36-93[»]
1QLQX-ray1.42A36-93[»]
1T7CX-ray1.85B/D36-93[»]
1T8LX-ray1.75B/D36-93[»]
1T8MX-ray1.80B/D36-93[»]
1T8NX-ray1.75B/D36-93[»]
1T8OX-ray1.70B/D36-93[»]
1TPAX-ray1.90I36-93[»]
1UUANMR-A38-93[»]
1UUBNMR-A38-93[»]
1YKTX-ray1.70B36-91[»]
2FI3X-ray1.58I36-93[»]
2FI4X-ray1.58I36-93[»]
2FI5X-ray1.58I36-93[»]
2FTLX-ray1.62I36-93[»]
2FTMX-ray1.65B36-93[»]
2HEXX-ray2.10A/B/C/D/E36-93[»]
2IJOX-ray2.30I36-93[»]
2KAIX-ray2.50I36-93[»]
2PTCX-ray1.90I36-93[»]
2R9PX-ray1.40E/F/G/I36-93[»]
2RA3X-ray1.46C/I36-93[»]
2TGPX-ray1.90I36-93[»]
2TPIX-ray2.10I36-93[»]
3BTDX-ray1.90I36-93[»]
3BTEX-ray1.85I36-93[»]
3BTFX-ray1.80I36-93[»]
3BTGX-ray1.90I36-93[»]
3BTHX-ray1.75I36-93[»]
3BTKX-ray1.85I36-93[»]
3BTMX-ray1.80I36-93[»]
3BTQX-ray1.90I36-93[»]
3BTTX-ray1.90I36-93[»]
3BTWX-ray2.05I36-93[»]
3TGIX-ray1.80I36-100[»]
3TGJX-ray2.20I36-100[»]
3TGKX-ray1.70I36-100[»]
3TPIX-ray1.90I36-93[»]
4PTIX-ray1.50A36-93[»]
4TPIX-ray2.20I36-93[»]
5PTIX-ray1.00A36-93[»]
6PTIX-ray1.70A36-93[»]
7PTIX-ray1.60A36-93[»]
8PTIX-ray1.80A36-93[»]
9PTIX-ray1.22A36-93[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6113N.

Protein family/group databases

MEROPSI02.001.

Genome annotation databases

EnsemblENSBTAG00000017328. Bos taurus. [Contig view]

Phylogenomic databases

HOVERGENP00974.

Family and domain databases

InterProIPR002223. Prot_inh_Kunz-m.
[Graphical view]
Gene3DG3DSA:4.10.410.10. Prot_inh_Kunz-m. 1 hit.
PfamPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
PRINTSPR00759. BASICPTASE.
ProDomPD000222. Prot_Inh_Kunz-m. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00131. KU. 1 hit.
[Graphical view]
PROSITEPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP00974.
LinkHubP00974.

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Entry information

Entry nameBPT1_BOVIN
AccessionPrimary (citable) accession number: P00974
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: November 25, 2008
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents