| IED ID | IndEnz0002000482 |
| Enzyme Type ID | protease000482 |
| Protein Name |
Pepsin A-2/A-3 EC 3.4.23.1 Pepsin III-2/III-1 |
| Gene Name | |
| Organism | Macaca fuscata fuscata (Japanese macaque) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Cercopithecoidea Cercopithecidae (Old World monkeys) Cercopithecinae Macaca (macaques) Macaca fuscata (Japanese macaque) Macaca fuscata fuscata (Japanese macaque) |
| Enzyme Sequence | MKWLLLLGLVALSECIIHKVPLVRKKSLRRNLSEHGLLKDFLKKHNFNPASKYFPQAEAPTLIDEQPLENYLDMEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACTNHNRFNPQDSSTYQSTSGTVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVSVEGYWQISVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGEMVVSCSAISSLPDIVFTINGIQYPVPPSAYILQSQGSCISGFQGMDVPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA |
| Enzyme Length | 388 |
| Uniprot Accession Number | P27677 |
| Absorption | |
| Active Site | ACT_SITE 94; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 277; /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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (3); Domain (1); Modified residue (1); Propeptide (2); Signal peptide (1) |
| Keywords | Aspartyl protease;Digestion;Direct protein sequencing;Disulfide bond;Hydrolase;Phosphoprotein;Protease;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 130; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P03954 |
| Post Translational Modification | PTM: Pepsin A-2 is phosphorylated, but not pepsin A-3. {ECO:0000269|PubMed:1935977}.; PTM: Each pepsinogen is converted to corresponding pepsin at pH 2.0 in part as a result of the release of a 47 AA activation segment and in part as a result of stepwise proteolytic cleavage via an intermediate form(s). |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,704 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |