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IPR000877 is a Proteinase inhibitor I12, Bowman-Birk.
<p>This family of eukaryotic proteinase inhibitors, belongs to MEROPS inhibitor family I12, clan IF. They predominantly inhibit serine peptidases of the S1 family ([interpro:IPR001254]) [[cite:PUB00014133]]. They play a role in defense response against pathogens and insects, but they also have been studied as therapeutic treatment in cancer and inflammatory disorders [[cite:PUB00097957]]. Exceptionally, cowpea trypsin inhibitor inhibits a cathepsin L-like cysteine proteinase CPL-1 from the nematode Heterodera glycines [[cite:PUB00078839]].</p> <p>The Bowman-Birk inhibitor family [[cite:PUB00097957], [cite:PUB00000032]] is one of the numerous families of serine proteinase inhibitors. They have a duplicated structure and generally possess two distinct inhibitory sites. These inhibitors are primarily found in plants and in particular in the seeds of legumes as well as in cereal grains. In cereals they exist in two forms, one of which is a duplication of the basic structure [[cite:PUB00002332]]. Proteins of the Bowman-Birk inhibitor family of serine proteinase inhibitors interact with the enzymes they inhibit via an exposed surface loop that adopts the canonical proteinase inhibitory conformation. The resulting non-covalent complex renders the proteinase inactive. This inhibition mechanism is common for the majority of serine proteinase inhibitor proteins and many analogous examples are known. A particular feature of the Bowman-Birk inhibitor protein, however, is that the interacting loop is a particularly well-defined disulphide-linked short β-sheet region [[cite:PUB00014484], [cite:PUB00014485], [cite:PUB00014486]].</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. | ||
| Cellular component | Extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | Bowman-Birk type protease inhibitor-like precursor [Glycine max] gi|351722763|ref|NP_001237767.1| | 18 | ||
| – | Trypsin inhibitor; TAIR: AT1G05660.1 Pectin lyase-like superfamily protein; Swiss-Prot: sp|Q41066|IBB2_PEA Seed trypsin/chymotrypsin inhibitor TI5-72; TrEMBL-Plants: tr|I3SII1|I3SII1_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0474900 | 18 | ||
| – | Trypsin inhibitor; TAIR: AT1G16480.1 Tetratricopeptide repeat (TPR)-like superfamily protein; Swiss-Prot: sp|Q41066|IBB2_PEA Seed trypsin/chymotrypsin inhibitor TI5-72; TrEMBL-Plants: tr|I3SII1|I3SII1_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0475000_LC | 16 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd00023 | CDD | 1 | 33.33 |