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P01074 (ITR1_CUCMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trypsin inhibitor 1
Alternative name(s):
CMTI-I
ITD-I
Trypsin inhibitor I
OrganismCucurbita maxima (Pumpkin) (Winter squash)
Taxonomic identifier3661 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeCucurbiteaeCucurbita

Protein attributes

Sequence length29 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits trypsin.

Subcellular location

Secreted.

Domain

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

Sequence similarities

Belongs to the protease inhibitor I7 (squash-type serine protease inhibitor) family. [View classification]

Ontologies

Keywords
   Cellular componentSecreted
   DomainKnottin
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 2929Trypsin inhibitor 1
PRO_0000044376

Sites

Site5 – 62Reactive bond

Amino acid modifications

Disulfide bond3 ↔ 20 Ref.2
Disulfide bond10 ↔ 22 Ref.2
Disulfide bond16 ↔ 28 Ref.2

Secondary structure

....... 29
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01074 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: CD509120BA52C01F

FASTA293,275
        10         20 
RVCPRILMEC KKDSDCLAEC VCLEHGYCG 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRTIPU. A01313.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP01074.
SMRP01074. Positions 2-29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-365052.

Protein family/group databases

MEROPSI07.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000737. Prot_inh_squash.
IPR011052. Proteinase_amylase_inhib_dom.
[Graphical view]
PfamPF00299. Squash. 1 hit.
[Graphical view]
PRINTSPR00293. SQUASHINHBTR.
SUPFAMSSF57027. SSF57027. 1 hit.
PROSITEPS00286. SQUASH_INHIBITOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01074.
PMAP-CutDBP01074.

Entry information

Entry nameITR1_CUCMA
AccessionPrimary (citable) accession number: P01074
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references