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Protein

Pancreatic trypsin inhibitor

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei50 – 512Reactive bond for trypsin

GO - Molecular functioni

  1. potassium channel inhibitor activity Source: AgBase
  2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI02.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Pancreatic trypsin inhibitor
Alternative name(s):
Aprotinin
Basic protease inhibitor
Short name:
BPI
Short name:
BPTI
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

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

Protein family/group databases

Allergomei3890. Bos d TI.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 3514PRO_0000016852Add
BLAST
Chaini36 – 9358Pancreatic trypsin inhibitorPRO_0000016853Add
BLAST
Propeptidei94 – 1007PRO_0000016854

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 90
Disulfide bondi49 ↔ 73PROSITE-ProRule annotation1 Publication
Disulfide bondi65 ↔ 86PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP00974.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
P007604EBI-1032263,EBI-986385
Q52V245EBI-1032263,EBI-8755401From a different organism.

Protein-protein interaction databases

DIPiDIP-6113N.
IntActiP00974. 5 interactions.
MINTiMINT-90698.
STRINGi9913.ENSBTAP00000023042.

Structurei

Secondary structure

1
100
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 414Combined sources
Beta strandi48 – 503Combined sources
Beta strandi53 – 597Combined sources
Turni60 – 634Combined sources
Beta strandi64 – 707Combined sources
Beta strandi72 – 743Combined sources
Beta strandi76 – 783Combined sources
Beta strandi80 – 823Combined sources
Helixi83 – 908Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AALX-ray1.60A/B36-93[»]
1B0CX-ray2.80A/B/C/D/E36-91[»]
1BHCX-ray2.70A/B/C/D/E/F/G/H/I/J36-93[»]
1BPIX-ray1.09A36-93[»]
1BPTX-ray2.00A36-93[»]
1BRBX-ray2.10I36-93[»]
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[»]
1YLCX-ray1.70B36-91[»]
1YLDX-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[»]
2ZJXX-ray1.09A/B36-93[»]
2ZVXX-ray1.09A/B36-93[»]
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[»]
3FP6X-ray1.49I36-93[»]
3FP7X-ray1.46I36-50[»]
J51-93[»]
3FP8X-ray1.46I36-93[»]
3GYMX-ray2.80I/J36-93[»]
3LDIX-ray2.20A/B/C/D/E36-93[»]
3LDJX-ray1.70A/B/C36-93[»]
3LDMX-ray2.60A/B/C/D/E36-93[»]
3OTJOther2.15I36-93[»]
3P92X-ray1.60E36-93[»]
3P95X-ray1.30E36-93[»]
3TGIX-ray1.80I36-100[»]
3TGJX-ray2.20I36-100[»]
3TGKX-ray1.70I36-100[»]
3TPIX-ray1.90I36-93[»]
3U1JX-ray1.80E36-93[»]
3WNYX-ray1.30A/B/C/E/F/G/H/I36-95[»]
4BNRX-ray2.00I/J1-100[»]
4DG4X-ray1.40C/E/F/H36-93[»]
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[»]
DisProtiDP00729.
ProteinModelPortaliP00974.
SMRiP00974. Positions 36-93.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00974.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 9051BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 BPTI/Kunitz inhibitor domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3540.
HOGENOMiHOG000007327.
HOVERGENiHBG006193.

Family and domain databases

Gene3Di4.10.410.10. 1 hit.
InterProiIPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PfamiPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00131. KU. 1 hit.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00974-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMSRLCLSV ALLVLLGTLA ASTPGCDTSN QAKAQRPDFC LEPPYTGPCK
60 70 80 90 100
ARIIRYFYNA KAGLCQTFVY GGCRAKRNNF KSAEDCMRTC GGAIGPWENL
Length:100
Mass (Da):10,903
Last modified:June 30, 1989 - v2
Checksum:i6A778A4AD763FB19
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS00277. TIBO.
UniGeneiBt.28518.

Cross-referencesi

Web resourcesi

Trasylol

Clinical information on Trasylol

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS00277. TIBO.
UniGeneiBt.28518.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AALX-ray1.60A/B36-93[»]
1B0CX-ray2.80A/B/C/D/E36-91[»]
1BHCX-ray2.70A/B/C/D/E/F/G/H/I/J36-93[»]
1BPIX-ray1.09A36-93[»]
1BPTX-ray2.00A36-93[»]
1BRBX-ray2.10I36-93[»]
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[»]
1YLCX-ray1.70B36-91[»]
1YLDX-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[»]
2ZJXX-ray1.09A/B36-93[»]
2ZVXX-ray1.09A/B36-93[»]
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[»]
3FP6X-ray1.49I36-93[»]
3FP7X-ray1.46I36-50[»]
J51-93[»]
3FP8X-ray1.46I36-93[»]
3GYMX-ray2.80I/J36-93[»]
3LDIX-ray2.20A/B/C/D/E36-93[»]
3LDJX-ray1.70A/B/C36-93[»]
3LDMX-ray2.60A/B/C/D/E36-93[»]
3OTJOther2.15I36-93[»]
3P92X-ray1.60E36-93[»]
3P95X-ray1.30E36-93[»]
3TGIX-ray1.80I36-100[»]
3TGJX-ray2.20I36-100[»]
3TGKX-ray1.70I36-100[»]
3TPIX-ray1.90I36-93[»]
3U1JX-ray1.80E36-93[»]
3WNYX-ray1.30A/B/C/E/F/G/H/I36-95[»]
4BNRX-ray2.00I/J1-100[»]
4DG4X-ray1.40C/E/F/H36-93[»]
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[»]
DisProtiDP00729.
ProteinModelPortaliP00974.
SMRiP00974. Positions 36-93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6113N.
IntActiP00974. 5 interactions.
MINTiMINT-90698.
STRINGi9913.ENSBTAP00000023042.

Protein family/group databases

Allergomei3890. Bos d TI.
MEROPSiI02.001.

Proteomic databases

PRIDEiP00974.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG3540.
HOGENOMiHOG000007327.
HOVERGENiHBG006193.

Miscellaneous databases

EvolutionaryTraceiP00974.

Family and domain databases

Gene3Di4.10.410.10. 1 hit.
InterProiIPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PfamiPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00131. KU. 1 hit.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1986) [PubMed] [Europe PMC] [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(1986) [PubMed] [Europe PMC] [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(1985) [PubMed] [Europe PMC] [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(1982) [PubMed] [Europe PMC] [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(1964) [PubMed] [Europe PMC] [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(1965) [PubMed] [Europe PMC] [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(1966) [PubMed] [Europe PMC] [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(1967)
    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(1989) [PubMed] [Europe PMC] [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(1974)
    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(1969) [PubMed] [Europe PMC] [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(1990) [PubMed] [Europe PMC] [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(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiBPT1_BOVIN
AccessioniPrimary (citable) accession number: P00974
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: June 30, 1989
Last modified: January 6, 2015
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.