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Protein

Trypsin inhibitor 1

Gene
N/A
Organism
Cucurbita maxima (Pumpkin) (Winter squash)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits trypsin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei5 – 62Reactive bond

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

MEROPSiI07.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin inhibitor 1
Alternative name(s):
CMTI-I
ITD-I
Trypsin inhibitor I
OrganismiCucurbita maxima (Pumpkin) (Winter squash)
Taxonomic identifieri3661 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeCucurbiteaeCucurbita

Subcellular locationi

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
Peptidei1 – 2929Trypsin inhibitor 1PRO_0000044376Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 201 Publication
Disulfide bondi10 ↔ 221 Publication
Disulfide bondi16 ↔ 281 Publication

Keywords - PTMi

Disulfide bond

Miscellaneous databases

PMAP-CutDBP01074.

Interactioni

Protein-protein interaction databases

MINTiMINT-365052.

Structurei

Secondary structure

1
29
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 153Combined sources
Beta strandi21 – 233Combined sources
Beta strandi26 – 283Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CTINMR-A1-29[»]
1LU0X-ray1.03A/B1-29[»]
1PPEX-ray2.00I1-29[»]
2CTINMR-A1-29[»]
2STAX-ray1.80I1-29[»]
2V1VNMR-A1-29[»]
3CTINMR-A1-29[»]
ProteinModelPortaliP01074.
SMRiP01074. Positions 2-29.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01074.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Knottin

Family and domain databases

InterProiIPR000737. Prot_inh_squash.
IPR011052. Proteinase_amylase_inhib_dom.
[Graphical view]
PfamiPF00299. Squash. 1 hit.
[Graphical view]
PRINTSiPR00293. SQUASHINHBTR.
SUPFAMiSSF57027. SSF57027. 1 hit.
PROSITEiPS00286. SQUASH_INHIBITOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01074-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20 
RVCPRILMEC KKDSDCLAEC VCLEHGYCG
Length:29
Mass (Da):3,275
Last modified:July 21, 1986 - v1
Checksum:iCD509120BA52C01F
GO

Sequence databases

PIRiA01313. TIPU.

Cross-referencesi

Sequence databases

PIRiA01313. TIPU.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CTINMR-A1-29[»]
1LU0X-ray1.03A/B1-29[»]
1PPEX-ray2.00I1-29[»]
2CTINMR-A1-29[»]
2STAX-ray1.80I1-29[»]
2V1VNMR-A1-29[»]
3CTINMR-A1-29[»]
ProteinModelPortaliP01074.
SMRiP01074. Positions 2-29.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-365052.

Protein family/group databases

MEROPSiI07.005.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP01074.
PMAP-CutDBP01074.

Family and domain databases

InterProiIPR000737. Prot_inh_squash.
IPR011052. Proteinase_amylase_inhib_dom.
[Graphical view]
PfamiPF00299. Squash. 1 hit.
[Graphical view]
PRINTSiPR00293. SQUASHINHBTR.
SUPFAMiSSF57027. SSF57027. 1 hit.
PROSITEiPS00286. SQUASH_INHIBITOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Amino-acid sequence of two trypsin isoinhibitors, ITD I and ITD III from squash seeds (Cucurbita maxima)."
    Wilusz T., Wieczorek M., Polanowski A., Denton A., Cook J., Laskowski M. Jr.
    Hoppe-Seyler's Z. Physiol. Chem. 364:93-95(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Seed.
  2. "The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes."
    Bode W., Greyling H.J., Huber R., Otlewski J., Wilusz T.
    FEBS Lett. 242:285-292(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  3. "Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing."
    Holak T.A., Gondol D., Otlewski J., Wilusz T.
    J. Mol. Biol. 210:635-648(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  4. "Conservative mutation Met8 --> Leu affects the folding process and structural stability of squash trypsin inhibitor CMTI-I."
    Zhukov I., Jaroszewski L., Bierzynski A.
    Protein Sci. 9:273-279(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiITR1_CUCMA
AccessioniPrimary (citable) accession number: P01074
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 89 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.