| IED ID | IndEnz0002000589 |
| Enzyme Type ID | protease000589 |
| Protein Name |
Pepsin A EC 3.4.23.1 |
| Gene Name | PGA |
| Organism | Callithrix jacchus (White-tufted-ear marmoset) |
| 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 Platyrrhini (New World monkeys) Cebidae Callitrichinae (marmosets and tamarins) Callithrix Callithrix Callithrix jacchus (White-tufted-ear marmoset) |
| Enzyme Sequence | MKWLLLLSLVALSECLYKVSLIKKKSLRKNLIEHGLLKDFLKNNTLDPASKYFPQGEAATMIANQPLVNYLDMEYFGTIGIGTPAQEFTVIFDTGSSNLWVPSIYCSSPACTNHNRFNPQESSTYQATSQTLSIAYGTGSMTGILGYDTVQVGGIADTNQIFGLSETEPGSFLYYSPFDGILGLAYPSISSSGATPVFDNIWNQDLVSQDLFSVYLSSNDQSGSVVMFGGIDSSYYTGSLNWVPVSAEGYWQITVDSITMNGEAIACAEGCQAIVDTGTSLLSGPTSPIANIQSYIGASENSNGEMVVSCSAISSLPDIVFTINGIQYPVPASAYILQDEGGCTSGFQGMNIPTAYGELWILGDVFIRQYFAVFDRANNQVGLAPVA |
| Enzyme Length | 387 |
| Uniprot Accession Number | Q9N2D4 |
| Absorption | |
| Active Site | ACT_SITE 93; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 276; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by pepstatin. {ECO:0000269|PubMed:10788784}. |
| 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:0000269|PubMed:10788784}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 2.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (3); Domain (1); Modified residue (1); Propeptide (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Digestion;Direct protein sequencing;Disulfide bond;Hydrolase;Phosphoprotein;Protease;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 129; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P03954 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000269|PubMed:10788784 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,564 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |