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Protein

Trypsin inhibitor 3

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Trypsin inhibitor.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei32 – 332Reactive bond for trypsinBy similarity

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

MEROPSiI90.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin inhibitor 3
Alternative name(s):
SOTI III
Trypsin inhibitor III
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 3737Trypsin inhibitor 3PRO_0000292939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 21By similarity
Disulfide bondi11 ↔ 25By similarity
Disulfide bondi20 ↔ 36By similarity

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
37
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Helixi17 – 193Combined sources
Beta strandi25 – 273Combined sources
Beta strandi29 – 368Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AOQX-ray2.00D/E/F1-37[»]
4AORX-ray1.70D/E/F1-37[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.By similarity

Sequence similaritiesi

Belongs to the Mirabilis serine proteinase inhibitor family.1 Publication

Keywords - Domaini

Knottin

Sequencei

Sequence statusi: Complete.

P84781-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
EDKCSPSGAI CSGFGPPEQC CSGACVPHPI LRIFVCQ
Length:37
Mass (Da):3,837
Last modified:June 26, 2007 - v1
Checksum:iD1F1F78D4EF22274
GO

Mass spectrometryi

Molecular mass is 3838.4 Da from positions 1 - 37. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AOQX-ray2.00D/E/F1-37[»]
4AORX-ray1.70D/E/F1-37[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI90.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Trypsin inhibitors from the garden four o'clock (Mirabilis jalapa) and spinach (Spinacia oleracea) seeds: isolation, characterization and chemical synthesis."
    Kowalska J., Pszczola K., Wilimowska-Pelc A., Lorenc-Kubis I., Zuziak E., Lugowski M., Legowska A., Kwiatkowska A., Sleszynska M., Lesner A., Walewska A., Zablotna E., Rolka K., Wilusz T.
    Phytochemistry 68:1487-1496(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY.
    Tissue: Seed1 Publication.

Entry informationi

Entry nameiITR3_SPIOL
AccessioniPrimary (citable) accession number: P84781
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: November 26, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.