| IED ID | IndEnz0002009203 |
| Enzyme Type ID | protease009203 |
| Protein Name |
Transmembrane protease serine 11C EC 3.4.21.- Neurobin Cleaved into: Transmembrane protease serine 11C non-catalytic chain; Transmembrane protease serine 11C catalytic chain |
| Gene Name | Tmprss11c |
| 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 | MARGQPRRSEEQWTALQNRTECKTKIKLTRCGKITLGILTAVLAAVLIGLIAYFAACGKDSFYYHVSFKVNNIDYDSKFAKPYSQEYMDLNKRIVSLMNETFHESKLRKQYVKAHTVQVSKAKGKVVIHAVLKFKACYRNNVEKYWESVETTLYQKLKGQTGLLIDSSSFKFSDIAMPIAEDLLNTCCGRRTIIHRGHKVAGGQDAEEGEWPWQASLQQNSVHRCGATLISNYWLITAAHCFIRAANPKDWKVSFGFLLSKPQAPRAVKNIIIHENYSYPAHDNDIAVVRLSSPVLYESNIRRACLPEATQKFPPNSDVVVTGWGTLKSDGDSPNILQKGKVKIIDNKTCNSGKAYGGMITPGMMCAGFLKGRVDACQGDSGGPLVSEDSKGIWFLAGIVSWGDECALPNKPGVYTRVTYYRDWITSKTGL |
| Enzyme Length | 431 |
| Uniprot Accession Number | Q1JRP2 |
| Absorption | |
| Active Site | ACT_SITE 240; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"; ACT_SITE 285; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"; ACT_SITE 381; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000305|PubMed:18215125" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease which has a preference for Arg or Lys in position P1 and uncharged residues in positions P2 and P3. Shows specificity towards FGF2 in vitro. {ECO:0000269|PubMed:18215125}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:18215125}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (3); Domain (2); Glycosylation (3); Mutagenesis (4); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Autocatalytic cleavage;Cell membrane;Cell projection;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18215125}; Single-pass type II membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:18215125}. Perikaryon {ECO:0000269|PubMed:18215125}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved via an autocatalytic mechanism. {ECO:0000269|PubMed:18215125}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21677750; 31501243; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,073 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |