| IED ID | IndEnz0002001976 |
| Enzyme Type ID | protease001976 |
| Protein Name |
Cysteine protease Amb a 11.0101 EC 3.4.22.- Amino acid thiol protease Pollen allergen Amb a 11 allergen Amb a 11.0101 |
| Gene Name | |
| Organism | Ambrosia artemisiifolia (Short ragweed) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids campanulids Asterales Asteraceae Asteroideae Heliantheae alliance Heliantheae Ambrosia Ambrosia artemisiifolia (Short ragweed) |
| Enzyme Sequence | MEINKLVCFSFSLVLILGLVESFHYHERELESEEGFMGMYDRWREQHNIEMRSPERFNVFKYNVRRIHESNKMDKPYKLKVNEFADMTNLEFVNTYANSKISHFQALRGSAPGSIDTDPNKDFIYANVTKIPDKVDWREKNAVTDVKGQGGCGSCWAFAAVVALEGINAIRTGKLVKFSEQQLVDCDMTNAGCDGGLMEPAFTYVIKHGGIAPEASYPYVGKRETCDKAKIKDVLKIDGRQNVPGLDEEALRKAVAHQPVATGIQLSGHGLQFYSEGVYTGDCGTEPNHGVGIVGYGENEKGIKFWTVKNSWGPTWGEKGYIHLQRGARKEGLCGVAMHSSFPIMNDPNPPKDDPNGPKDDPDAPKDPKFKTTQRLQGIRTKLLEL |
| Enzyme Length | 386 |
| Uniprot Accession Number | V5LU01 |
| Absorption | |
| Active Site | ACT_SITE 155; /evidence="ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000269|PubMed:27129273"; ACT_SITE 289; /evidence="ECO:0000305|PubMed:27129273"; ACT_SITE 310; /evidence="ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000305|PubMed:27129273" |
| Activity Regulation | ACTIVITY REGULATION: Activated by L-cysteine (PubMed:27129273). Inhibited by cysteine protease inhibitor E64 (PubMed:25865353, PubMed:27129273). Inhibited by cysteine/serine protease inhibitor leupeptin. Not inhibited by serine protease inhibitors 4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride (AEBSF) and phenylmethanesulfonyl fluoride (PMSF), metallo protease inhibitor bestatin or aspartic protease inhibitor pepstatin A (PubMed:27129273). {ECO:0000269|PubMed:25865353, ECO:0000269|PubMed:27129273}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Cysteine protease. Hydrolyzes casein and synthetic peptide Boc-Val-Leu-Lys-7-amino-4-methylcoumarin (Boc-VLK-AMC) in vitro. {ECO:0000269|PubMed:25865353, ECO:0000269|PubMed:27129273}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8 and 9. {ECO:0000269|PubMed:27129273}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (13); Chain (1); Compositional bias (1); Disulfide bond (3); Glycosylation (1); Helix (14); Mutagenesis (2); Propeptide (2); Region (1); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Allergen;Autocatalytic cleavage;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Autocatalytic proteolytic cleavage of N-terminal activation peptide. {ECO:0000269|PubMed:27129273}.; PTM: N-glycosylated. Glycosylation is not required for binding to IgE. {ECO:0000269|PubMed:25865353}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5EF4; 5EGW; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,157 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |