| IED ID | IndEnz0002009505 |
| Enzyme Type ID | protease009505 |
| Protein Name |
Serpin A3-1 Endopin-1A Muscle endopin-1A mEndopin-1A |
| Gene Name | SERPINA3-1 SERPINA3A |
| Organism | Bos taurus (Bovine) |
| 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 Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MRAERTSFLLALGLLVAGIRSVHCLPENVVVKDQHRRVDGHTLASSNTDFAFSLYKQLALKNPNKNVILSPLSVSIALAFLSLGARGSTLTEILEGLKFNLTEIQEKEIHHSFQHLLQALNQPSNQLQLSVGNAMFVQEELKLLDKFIEDAQVLYSSEAFPTNFRDSEAARSLINDYVKNKTQGKIEELFKYLSPRTELVLVNYIYFKAQWKTPFDPKHTEQAEFHVSDNKTVEVPMMTLDLETPYFRDEELGCTLVELTYTSNDSALFILPDEGKMRDLEAKLTPETLTRWRNSLQPRRIHELYLPKFSIKSNYELNDILSQLGIRKIFANADLSGITGTADLVVSQVVHGAALDVDEEGTEGAAATGISMERTILRIIVRVNRPFLIAIVLKDTQSIIFLGKVTNPSEA |
| Enzyme Length | 411 |
| Uniprot Accession Number | Q9TTE1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Potent inhibitor of the serine proteases elastase and trypsin. Moderately inhibits the serine proteases plasmin and chymotrypsin, and the thiol protease proenkephalin-processing enzyme. Does not inhibit the serine proteases cathepsin G, furin, kallikrein, thrombin, tissue plasminogen activator and urokinase, or the cysteine proteases cathepsin B, cathepsin L and papain. {ECO:0000269|PubMed:10567388, ECO:0000269|PubMed:15647007}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable at temperatures up to 70 degrees Celsius. Incubation at temperatures above 70 degrees Celsius rapidly decreases inhibitory activity. {ECO:0000269|PubMed:15647007}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Stable in the pH range 4.0-12.0. Incubation at a pH below 4.0 rapidly decreases inhibitory activity. {ECO:0000269|PubMed:15647007}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (4); Sequence conflict (2); Signal peptide (1); Site (1) |
| Keywords | Cytoplasmic vesicle;Direct protein sequencing;Glycoprotein;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000269|PubMed:10567388, ECO:0000269|PubMed:15647007}. Secreted {ECO:0000269|PubMed:10567388, ECO:0000269|PubMed:15647007}. Note=In longissimus muscle myocytes highest levels are found between the plasma membrane and the myofibrils and lower levels are found within the myofibrils. Localized to the chromaffin granules of the adrenal medulla and secreted in response to nicotine or KCL depolarization. {ECO:0000269|PubMed:10567388, ECO:0000269|PubMed:15647007}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:10567388}. |
| Signal Peptide | SIGNAL 1..24; /evidence="ECO:0000269|PubMed:15647007, ECO:0000269|PubMed:16716310" |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19665028; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,237 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |