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Reviewed, UniProtKB/Swiss-Prot P01074 (ITR1_CUCMA)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length29 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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
P01074-1 [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: 6840699] [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: 2914611] [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: 2614837] [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: 10716179] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRTIPU. A01313.

3D structure databases

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[»]
ModBaseSearch...

Protein family/group databases

MEROPSI07.005.

Family and domain databases

InterProIPR000737. Prot_inh_squash.
[Graphical view]
PfamPF00299. Squash. 1 hit.
[Graphical view]
PRINTSPR00293. SQUASHINHBTR.
ProDomPD003401. Prot_inh_squash. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00286. PTI. 1 hit.
[Graphical view]
PROSITEPS00286. SQUASH_INHIBITOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

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: June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents