P84781 (ITR3_SPIOL) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 11.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Trypsin inhibitor 3 Alternative name(s): SOTI III Trypsin inhibitor III |
| Organism | Spinacia oleracea (Spinach) |
| Taxonomic identifier | 3562 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia![]() |
Protein attributes
| Sequence length | 37 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Trypsin inhibitor. Ref.1 |
| Domain | The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin By similarity. |
| Sequence similarities | Belongs to the Mirabilis serine proteinase inhibitor family. Ref.1 |
| Mass spectrometry | Molecular mass is 3838.4 Da from positions 1 - 37. Determined by ESI. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Domain | Knottin |
| Molecular function | Protease inhibitor Serine protease inhibitor |
| PTM | Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular_function | serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||
Molecule processing | |||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Peptide | 1 – 37 | 37 | Trypsin inhibitor 3 Ref.1 | PRO_0000292939 | |||||||||||||
Sites | |||||||||||||||||
| Site | 32 – 33 | 2 | Reactive bond for trypsin By similarity UniProtKB P84779 | ||||||||||||||
Amino acid modifications | |||||||||||||||||
| Disulfide bond | 4 ↔ 21 | By similarity UniProtKB P84779 | |||||||||||||||
| Disulfide bond | 11 ↔ 25 | By similarity UniProtKB P84779 | |||||||||||||||
| Disulfide bond | 20 ↔ 36 | By similarity UniProtKB P84779 | |||||||||||||||
Secondary structure | |||||||||||||||||
Helix Strand Turn | |||||||||||||||||
| Beta strand | 9 – 11 | 3 | |||||||||||||||
| Helix | 17 – 19 | 3 | |||||||||||||||
| Beta strand | 25 – 27 | 3 | |||||||||||||||
| Beta strand | 29 – 36 | 8 | |||||||||||||||
Sequences
References
| [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: Seed. |
Cross-references
3D structure databases | |||||||||||||||||||
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| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||||||||
Protein family/group databases | |||||||||||||||||||
| MEROPS | I90.001. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | ITR3_SPIOL | ||||||||
| Accession | Primary (citable) accession number: P84781 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
