| IED ID | IndEnz0002000637 |
| Enzyme Type ID | protease000637 |
| Protein Name |
Pepsin A EC 3.4.23.1 |
| Gene Name | PGA PGNA |
| Organism | Rhinolophus ferrumequinum (Greater horseshoe bat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Chiroptera Microchiroptera Rhinolophidae (Old World leaf-nosed bats) Rhinolophinae Rhinolophus Rhinolophus ferrumequinum (Greater horseshoe bat) |
| Enzyme Sequence | MKWLLLLSLVALSECYIYKVPLVKKKSLRKNLMEQGLLQDYLKTHSINPASKYLKEAASMMATQPLENYMDMEYFGTIGIGTPPQEFTVIFDTGSSNLWVPSVYCSSPACSNHNRFNPQQSSTYQGTNQKLSVAYGTGSMTGILGYDTVQVGGITDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSIASSGATPVFDNIWNQGLVSQDLFSVYLSSNDQGGSVVMFGGIDSSYFTGNLNWVPLSSETYWQITVDSITMNGQVIACSGSCQAIVDTGTSLLSGPTNAIASIQGYIGASQNANGEMVVSCSAINTLPNIVFTINGVQYPLPPSAYVLQSQQGCTSGFQGMDIPTSSGELWILGDVFIRQYFTVFDRGNNQVGLAPVA |
| Enzyme Length | 386 |
| Uniprot Accession Number | Q9GMY7 |
| Absorption | |
| Active Site | ACT_SITE 92; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 275; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.; EC=3.4.23.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10094}; |
| DNA Binding | |
| EC Number | 3.4.23.1 |
| Enzyme Function | FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (3); Domain (1); Propeptide (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Digestion;Disulfide bond;Hydrolase;Protease;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,591 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |