| IED ID | IndEnz0001000144 |
| Enzyme Type ID | amylase000144 |
| Protein Name |
Alpha-amylase/trypsin inhibitor CMb Chloroform/methanol-soluble protein CMb |
| Gene Name | IAT2 |
| Organism | Hordeum vulgare (Barley) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Hordeinae Hordeum Hordeum vulgare (Barley) |
| Enzyme Sequence | MASKSSCDLLLAAVLVSIFAAVAAVGSEDCTPWTATPITPLPSCRDYVEQQACRIETPGPPYLAKQQCCGELANIPQQCRCQALRFFMGRKSRPDQSGLMELPGCPREVQMDFVRILVTPGFCNLTTVHNTPYCLAMDEWQWNRQFCSS |
| Enzyme Length | 149 |
| Uniprot Accession Number | P32936 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Part of a complex with inhibitory activity, but CMb is inactive as a separate subunit. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Allergen;Alpha-amylase inhibitor;Direct protein sequencing;Disulfide bond;Glycoprotein;Protease inhibitor;Secreted;Serine protease inhibitor;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Five disulfide bonds are present (Probable), which are essential for the inhibitor activity.; PTM: Exists both in a glycosylated and in an unglycosylated form. The glycosylated form is a potent allergen. |
| Signal Peptide | SIGNAL 1..24; /evidence="ECO:0000269|PubMed:3484638, ECO:0000269|PubMed:8125056" |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 16,526 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |