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Protein

Trypsin inhibitor 1

Gene

sfti1

Organism
Helianthus annuus (Common sunflower)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits trypsin, cathepsin G, elastase, chymotrypsin and thrombin. Does not inhibit factor Xa.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei44 – 452Reactive bondBy similarity

GO - Molecular functioni

  • serine-type endopeptidase inhibitor activity Source: UniProtKB

GO - Biological processi

  • negative regulation of endopeptidase activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI12.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin inhibitor 1
Alternative name(s):
SFTI-1
Gene namesi
Name:sfti1Imported
OrganismiHelianthus annuus (Common sunflower)
Taxonomic identifieri4232 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceHeliantheaeHelianthus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Propeptidei26 – 3914Sequence Analysis1 PublicationPRO_0000042672Add
BLAST
Peptidei40 – 5314Trypsin inhibitor 1PRO_0000042673Add
BLAST
Propeptidei54 – 563PRO_0000042674

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki40 ↔ 53Cyclopeptide (Gly-Asp)
Disulfide bondi42 ↔ 502 Publications

Post-translational modificationi

This is a cyclic peptide.1 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
56
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 363Combined sources
Beta strandi41 – 477Combined sources
Beta strandi49 – 524Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JBLNMR-A40-53[»]
1JBNNMR-A40-53[»]
1O8YNMR-A40-53[»]
1O8ZNMR-A40-53[»]
1SFIX-ray1.65I40-53[»]
1T9ENMR-A40-53[»]
2AB9NMR-A26-56[»]
3P8FX-ray2.00I40-53[»]
4ABIX-ray1.55B40-53[»]
4ABJX-ray1.45B40-53[»]
4HGCX-ray1.29I40-53[»]
4K1EX-ray1.30B40-53[»]
4K8YX-ray1.00B40-53[»]
4KELX-ray1.15B40-53[»]
ProteinModelPortaliQ4GWU5.
SMRiQ4GWU5. Positions 26-56.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4GWU5.

Family & Domainsi

Keywords - Domaini

Signal

Sequencei

Sequence statusi: Complete.

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

Q4GWU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTMAKLIT LVVLAILAFV EVSVSGYKTS ISTITIEDNG RCTKSIPPIC

FPDGRP
Length:56
Mass (Da):5,971
Last modified:August 30, 2005 - v1
Checksum:iBF3BAF97C25F19A7
GO

Mass spectrometryi

Molecular mass is 1513 Da from positions 40 - 53. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM050587 Genomic DNA. Translation: CAJ19097.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM050587 Genomic DNA. Translation: CAJ19097.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JBLNMR-A40-53[»]
1JBNNMR-A40-53[»]
1O8YNMR-A40-53[»]
1O8ZNMR-A40-53[»]
1SFIX-ray1.65I40-53[»]
1T9ENMR-A40-53[»]
2AB9NMR-A26-56[»]
3P8FX-ray2.00I40-53[»]
4ABIX-ray1.55B40-53[»]
4ABJX-ray1.45B40-53[»]
4HGCX-ray1.29I40-53[»]
4K1EX-ray1.30B40-53[»]
4K8YX-ray1.00B40-53[»]
4KELX-ray1.15B40-53[»]
ProteinModelPortaliQ4GWU5.
SMRiQ4GWU5. Positions 26-56.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI12.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ4GWU5.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1."
    Mulvenna J.P., Foley F.M., Craik D.J.
    J. Biol. Chem. 280:32245-32253(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRUCTURE BY NMR OF 26-56.
    Tissue: LeafImported.
  2. "High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds."
    Luckett S., Garcia R.S., Barker J.J., Konarev A.V., Shewry P.R., Clarke A.R., Brady R.L.
    J. Mol. Biol. 290:525-533(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-53, CROSS-LINK, FUNCTION, MASS SPECTROMETRY, STRUCTURE BY NMR OF 40-53.
    Tissue: Seed1 Publication.
  3. "Solution structures by 1H NMR of the novel cyclic trypsin inhibitor SFTI-1 from sunflower seeds and an acyclic permutant."
    Korsinczky M.L., Schirra H.J., Rosengren K.J., West J., Condie B.A., Otvos L., Anderson M.A., Craik D.J.
    J. Mol. Biol. 311:579-591(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 40-53.
  4. "Enzymatic cyclization of a potent bowman-birk protease inhibitor, sunflower trypsin inhibitor-1, and solution structure of an acyclic precursor peptide."
    Marx U.C., Korsinczky M.L.J., Schirra H.J., Jones A., Condie B., Otvos L. Jr., Craik D.J.
    J. Biol. Chem. 278:21782-21789(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 40-53, DISULFIDE BOND.

Entry informationi

Entry nameiSFTI1_HELAN
AccessioniPrimary (citable) accession number: Q4GWU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: August 30, 2005
Last modified: May 27, 2015
This is version 38 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

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.