PTI pancreatic trypsin inhibitor [Bos taurus (domestic cattle)] - Gene

Summary

Gene symbol: PTI
Gene description: pancreatic trypsin inhibitor
See related: BGD:BT21240
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Bos taurus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Also known as: BPI; BPTI
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: chromosome: 13

Exon count:: 3

Annotation release	Status	Assembly	Chr	Location
RS_2023_09	current	ARS-UCD2.0 (GCF_002263795.3)	13	NC_037340.1 (74296024..74300843)

Chromosome 13 - NC_037340.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_037340.1 Chromosome 13 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Protein-Protein Binding as a Two-Step Mechanism: Preselection of Encounter Poses during the Binding of BPTI and Trypsin.
Title: Protein-Protein Binding as a Two-Step Mechanism: Preselection of Encounter Poses during the Binding of BPTI and Trypsin.
Reversible Oligomerization and Reverse Hydrophobic Effect Induced by Isoleucine Tags Attached at the C-Terminus of a Simplified BPTI Variant.
Title: Reversible Oligomerization and Reverse Hydrophobic Effect Induced by Isoleucine Tags Attached at the C-Terminus of a Simplified BPTI Variant.
Data report a structural and thermodynamic analysis of BPTI variants, where 19-24 of its 58 residues are alanines (Ala). A two-state thermal unfolding was observed, typical of a native protein with densely packed interior. Ala substitutions caused the recruitment of novel water molecules facilitating the formation of protein-water hydrogen bonds and improving the hydration shells around Ala methyl groups.
Title: Crystal structures of highly simplified BPTIs provide insights into hydration-driven increase of unfolding enthalpy.
the importance of substrate dynamics in the cleavage of Kunitz-bovine pancreatic trypsin inhibitor protease inhibitors by mesotrypsin, finding that the varied conformational dynamics of structurally similar substrates can profoundly impact the rate of catalysis.
Title: An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis.
analyzed the mechanisms behind a remarkable 13 degrees stabilization produced by a single A14G and a double A14GA38V mutation
Title: Thermodynamic and structural analysis of highly stabilized BPTIs by single and double mutations.
variation of the radius of gyration and the modification of the shape of BPTI between ambient temperature and 368 K
Title: Temperature dependence on structure and dynamics of Bovine Pancreatic Trypsin Inhibitor (BPTI): a neutron scattering study.
insights into the mechanism by which inhibitors like BPTI normally resist hydrolysis when bound to their target proteases.
Title: Structure of a serine protease poised to resynthesize a peptide bond.
high-resolution crystal structures of an extensively simplified variant of bovine pancreatic trypsin inhibitor containing 20 alanines.
Title: Crystal structure of an extensively simplified variant of bovine pancreatic trypsin inhibitor in which over one-third of the residues are alanines.
Results describe the functional and structural roles of the Cys14-Cys38 disulfide of bovine pancreatic trypsin inhibitor.
Title: Functional and structural roles of the Cys14-Cys38 disulfide of bovine pancreatic trypsin inhibitor.
The results herein suggest that not only intramolecular rearrangements but also oxidation of N* and N cent to mixed disulfides and subsequent conversion to native protein, a growth-type pathway, is important for the efficient folding of BPTI.
Title: Balancing conformational and oxidative kinetic traps during the folding of bovine pancreatic trypsin inhibitor (BPTI) with glutathione and glutathione disulfide.

Submit: New GeneRIF Correction See all GeneRIFs (15)

General gene information

Go to the top of the page Help

Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables serine-type endopeptidase inhibitor activity	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
located_in extracellular space	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: pancreatic trypsin inhibitor

Names: aprotinin; basic protease inhibitor; trypsin ihibitor

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001001554.3 → NP_001001554.2 pancreatic trypsin inhibitor precursor

See identical proteins and their annotated locations for NP_001001554.2

Status: PROVISIONAL

Source sequence(s)

BC149368

UniProtKB/TrEMBL

A6QPK7, G3X7A8

Conserved Domains (1) summary

cd00109
Location:38 → 91

KU; BPTI/Kunitz family of serine protease inhibitors; Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure.