IED ID | IndEnz0002014368 |
Enzyme Type ID | protease014368 |
Protein Name |
Aspartic proteinase EC 3.4.23.- |
Gene Name | |
Organism | Cucurbita pepo (Vegetable marrow) (Summer squash) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Cucurbitales Cucurbitaceae Cucurbiteae Cucurbita (marrows) Cucurbita pepo (Vegetable marrow) (Summer squash) |
Enzyme Sequence | MASYHSKAAFLCLFLLVSFNIVSSASNDGLLRVGLKKIKLDPENRLAARVESKDAEILKAAFRKYNPKGNLGESSDTDIVALKNYLDAQYYGEIAIGTPPQKFTVIFDTGSSNLWVLCECLFSVACHFHARYKSSRSSSYKKNGTSASIRYGTGAVSGFFSYDNVKVGDLVVKEQVFIEATREPSLTFLVAKFDGLLGLGFQEIAVGNAVPVWYNMVEQGLVKEPVFSFWLNRNVEEEEGGEIVFGGVDPKHYRGKHTYVPVTQKGYWQFDMGDVLIDGEPTGFCDGGCSAIADSGTSLLAGPTPVITMINHAIGAKGVVSQQCKAVVAQYGQTIMDLLLSEADPKKICSQINLCTFDGTRGVSMGIESVVDENAGKSSDSLHDGMCSVCEMTVVWMQNQLRQNQTKERIINYINELCDRMPSPMGQSAVDCGQLSSMPTVSFTIGGKIFDLAPEEYILKVGEGPVAQCISGFTAFDIPPPRGPLWILGDVFMGRYHTVFDFGKLRVGSAEAA |
Enzyme Length | 513 |
Uniprot Accession Number | O04057 |
Absorption | |
Active Site | ACT_SITE 108; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 294; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.23.- |
Enzyme Function | FUNCTION: Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (6); Domain (2); Glycosylation (2); Propeptide (1); Signal peptide (1) |
Keywords | Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Signal;Vacuole;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Vacuole {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 55,856 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |