| IED ID | IndEnz0002010427 |
| Enzyme Type ID | protease010427 |
| Protein Name |
Transmembrane protease serine 11D EC 3.4.21.- Adrenal secretory serine protease AsP Airway trypsin-like protease AT Cleaved into: Transmembrane protease serine 11D non-catalytic chain; Transmembrane protease serine 11D catalytic chain |
| Gene Name | Tmprss11d Rat |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MYRPRSMVSPSRFFNPFMVALIVIITVGLLAMTAGLLIHFLAFDKRAYFYHSNFHILNVDYTEALNSPATHEYRTLSERIESMITDAFRESNLRSEFIRTHVVKLRKEGSGVVADVVMKFRSSKRNNKKAIKTRIQSVLQRLSSSGNLEIAPSNGITSLTDQDTENVLTQECGARPDLITLSEERIIGGTQAETGDWPWQVSLQLNNVHHCGGTLISNLWVLTAAHCFRSYSNPQQWTATFGVSTISPRLRVRVRAILAHAEYNSITRDNDIAVVQLDRPVTFTRNIHRVCLPAATQNIMPDSVAYVTGWGSLTYGGNTVTNLQQGEVRIVSSEVCNEPAGYGGSVLPGMLCAGVRSGAVDACQGDSGGPLVQEDTRRLWFVVGIVSWGYQCGLPNKPGVYTRVTAYRNWIRQQTGI |
| Enzyme Length | 417 |
| Uniprot Accession Number | Q8VHJ4 |
| Absorption | |
| Active Site | ACT_SITE 226; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 271; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 367; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Preferentially cleaves the C-terminal side of arginine residues at the P1 position of certain peptides (By similarity). Isoform 2 may play a key role in regulating adrenal proliferation by specifically cleaving N-POMC. {ECO:0000250, ECO:0000269|PubMed:11439186}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Chain (2); Disulfide bond (4); Domain (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Cell membrane;Disulfide bond;Hydrolase;Membrane;Protease;Reference proteome;Secreted;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Transmembrane protease serine 11D catalytic chain]: Secreted {ECO:0000250}. Note=Activated by cleavage and secreted. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12851306; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,288 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |