Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P30709 (ITRA_MOMCH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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 attributes

Sequence length28 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 – 2828Trypsin inhibitor A
PRO_0000044389

Sites

Site5 – 62Reactive bond

Amino acid modifications

Disulfide bond3 ↔ 20
Disulfide bond10 ↔ 22
Disulfide bond16 ↔ 27

Secondary structure

... 28
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30709 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 67E8E6A2D404FEDF

FASTA283,133
        10         20 
RSCPRIWMEC TRDSDCMAKC ICVAGHCG 

« Hide

References

[1]"Amino acid sequencing of a trypsin inhibitor by refined 1.6 A X-ray crystal structure of its complex with porcine beta-trypsin."
Huang Q., Liu S., Tang Y., Zeng F., Qian R.
FEBS Lett. 297:143-146(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRS20393.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MCTX-ray1.60I3-28[»]
ProteinModelPortalP30709.
SMRP30709. Positions 1-28.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1512997.

Protein family/group databases

MEROPSI07.018.

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

EvolutionaryTraceP30709.

Entry information

Entry nameITRA_MOMCH
AccessionPrimary (citable) accession number: P30709
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 74 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