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IPR000864 is a Proteinase inhibitor I13, potato inhibitor I.
<p>This family of proteinase inhibitors belong to MEROPS inhibitor family I13, clan IG. They inhibit peptidases of the S1 ([interpro:IPR001254]) and S8 ([interpro:IPR000209]) families [[cite:PUB00014133]]. Potato inhibitor type I sequences are not solely restricted to potatoes but are found in other plant species for example: barley endosperm chymotrypsin inhibitor [[cite:PUB00001351]], and pumpkin trypsin inhibitor. Apart from leeches, e.g.Hirudo medicinalis (Medicinal leech), homologues are not found in metazoa [[cite:PUB00001150]]. In general, the proteins have retained a specificity towards chymotrypsin-like and elastase-like proteases. Structurally these inhibitors are small (60 to 90 residues) and in contrast with other families of protease inhibitors, they lack disulphide bonds. The inhibitor is a wedge-shaped molecule, its pointed edge formed by the protease-binding loop, which contains the scissile bond. The loop binds tightly to the protease active site, subsequent cleavage of the scissile bond causing inhibition of the enzyme [[cite:PUB00001150]].</p> <p>The inhibitors (designated type I and II) are synthesised in potato tubers, increasing in concentration as the tuber develops. Synthesis of the inhibitors throughout the plant is also induced by leaf damage; this systemic response being triggered by the release of a putative plant hormone.</p> <p>Examples found in the bacteria and archaea are probable false positives.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Serine-type endopeptidase inhibitor activity | Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme. | ||
| Biological process | Response to wounding | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to the organism. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: inhibitor of trypsin and hageman factor-like [Fragaria vesca subsp]. vesca] gi|470104097|ref|XP_004288451.1| | 8 | ||
| – | PREDICTED: inhibitor of trypsin and hageman factor-like [Fragaria vesca subsp]. vesca] gi|470104097|ref|XP_004288451.1| | 8 | ||
| – | Protease inhibitor [Medicago truncatula] gi|357494051|ref|XP_003617314.1| | 9 | ||
| – | Inhibitor protein; TAIR: AT2G38870.1 Serine protease inhibitor, potato inhibitor I-type family protein; Swiss-Prot: sp|P16064|ICI1_PHAAN Subtilisin inhibitor 1; TrEMBL-Plants: tr|G7IW97|G7IW97_MEDTR Subtilisin inhibitor 1; Found in the gene: LotjaGi3g1v0114000 | 10 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 25.00 |