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Protein

Trypsin inhibitor

Gene
N/A
Organism
Veronica hederifolia (Ivy-leaved speedwell)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits trypsin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei15 – 162Reactive bond for trypsin1 Publication

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI73.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin inhibitor1 Publication
Short name:
VhTI1 Publication
OrganismiVeronica hederifolia (Ivy-leaved speedwell)
Taxonomic identifieri202477 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesPlantaginaceaeVeroniceaeVeronicaCochlidiosperma

Subcellular locationi

Secreted Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3434Trypsin inhibitorPRO_0000351204Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi7 ↔ 291 Publication
Disulfide bondi11 ↔ 251 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
34
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 137Combined sources
Helixi19 – 2911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CMYX-ray2.25B1-34[»]
2PLXX-ray1.56B6-31[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP85981.

Sequencei

Sequence statusi: Complete.

P85981-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
NTDPEQCKVM CYAQRHSSPE LLRRCLDNCE KEHD
Length:34
Mass (Da):4,050
Last modified:September 23, 2008 - v1
Checksum:iBD6BB312733CCE21
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CMYX-ray2.25B1-34[»]
2PLXX-ray1.56B6-31[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI73.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP85981.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "An unusual helix-turn-helix protease inhibitory motif in a novel trypsin inhibitor from seeds of Veronica (Veronica hederifolia L.)."
    Conners R., Konarev A.V., Forsyth J., Lovegrove A., Marsh J., Joseph-Horne T., Shewry P., Brady R.L.
    J. Biol. Chem. 282:27760-27768(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, REACTIVE BOND, DISULFIDE BONDS, X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH BOVINE TRYPSIN.
    Tissue: Seed1 Publication.

Entry informationi

Entry nameiTI_VERHE
AccessioniPrimary (citable) accession number: P85981
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: September 23, 2008
Last modified: January 7, 2015
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Differs dramatically in structure from all previously described families of trypsin inhibitors. Consists of a helix-loop-helix motif with two alpha-helices tightly associated by two disulfide bonds.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.