| IED ID | IndEnz0002000524 |
| Enzyme Type ID | protease000524 |
| Protein Name |
Pepsin A-5 EC 3.4.23.1 Pepsin F |
| Gene Name | Pga5 Pepf |
| Organism | Mus musculus (Mouse) |
| 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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MKWLWVLGLVALSECLVKIPLMKIKSMRENLRESQVLKDYLEKYPRSRAHVLLEQRRNPAVTYEPMRNYLDLVYIGIISIGTPPQEFRVVLDTGSSVLWVPSIYCSSPACAHHKAFNPLRSSTFLVSGRPVNVAYGSGEMSGFLAYDTVRIGDLTVVAQAFGLSLEEPGIFMEYAVFDGILGLGYPNLGLQGITPVFDNLWLQGLIPQNLFAFYLSSKDEKGSMLMLGGVDPSYYHGELHWVPVSKPSYWQLAVDSISMNGEVIACDGGCQGIMDTGTSLLTGPRSSIVNIQNLIGAKASGDGEYFLKCDTINTLPDIVFTIGSVTYPVPASAYIRKDRSHNCRSNFEEGMDDPSDPEMWVLGDVFLRLYFTVFDRANNRIGLAPAA |
| Enzyme Length | 387 |
| Uniprot Accession Number | Q9D106 |
| Absorption | |
| Active Site | ACT_SITE 92; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 275; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by pepstatin A. {ECO:0000269|PubMed:11566730}. |
| 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:0000269|PubMed:11566730}; |
| 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 (By similarity). May play a role as a specialized neonatal digestive enzyme (Probable). {ECO:0000250|UniProtKB:Q9N2D4, ECO:0000305|PubMed:11566730}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (3); Domain (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Disulfide bond;Hydrolase;Protease;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 11915945; 12466851; 14610273; 18799693; 21362171; 23676500; 29700203; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,824 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |