| IED ID | IndEnz0002001384 |
| Enzyme Type ID | protease001384 |
| Protein Name |
Transmembrane protease serine 2 EC 3.4.21.- Epitheliasin Plasmic transmembrane protein X Cleaved into: Transmembrane protease serine 2 non-catalytic chain; Transmembrane protease serine 2 catalytic chain |
| Gene Name | Tmprss2 |
| 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 | MALNSGSPPGIGPCYENHGYQSEHICPPRPPVAPNGYNLYPAQYYPSPVPQYAPRITTQASTSVIHTHPKSSGALCTSKSKKSLCLALALGTVLTGAAVAAVLLWRFWDSNCSTSEMECGSSGTCISSSLWCDGVAHCPNGEDENRCVRLYGQSFILQVYSSQRKAWYPVCQDDWSESYGRAACKDMGYKNNFYSSQGIPDQSGATSFMKLNVSSGNVDLYKKLYHSDSCSSRMVVSLRCIECGVRSVKRQSRIVGGLNASPGDWPWQVSLHVQGVHVCGGSIITPEWIVTAAHCVEEPLSSPRYWTAFAGILRQSLMFYGSRHQVEKVISHPNYDSKTKNNDIALMKLQTPLAFNDLVKPVCLPNPGMMLDLDQECWISGWGATYEKGKTSDVLNAAMVPLIEPSKCNSKYIYNNLITPAMICAGFLQGSVDSCQGDSGGPLVTLKNGIWWLIGDTSWGSGCAKALRPGVYGNVTVFTDWIYQQMRANS |
| Enzyme Length | 490 |
| Uniprot Accession Number | Q9JIQ8 |
| Absorption | |
| Active Site | ACT_SITE 294; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 343; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 439; /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: Plasma membrane-anchored serine protease that participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption (By similarity). In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia (PubMed:25734995). {ECO:0000250|UniProtKB:O15393, ECO:0000269|PubMed:25734995}.; FUNCTION: (Microbial infection) Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9) and is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity. {ECO:0000269|PubMed:24348248, ECO:0000269|PubMed:24522916, ECO:0000269|PubMed:24600012}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (9); Domain (3); Glycosylation (3); Sequence conflict (12); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Autocatalytic cleavage;Cell membrane;Disulfide bond;Glycoprotein;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|UniProtKB:O15393}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O15393}.; SUBCELLULAR LOCATION: [Transmembrane protease serine 2 catalytic chain]: Secreted {ECO:0000250|UniProtKB:O15393}. Note=Activated by cleavage and secreted. {ECO:0000250|UniProtKB:O15393}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically processed; by an autocatalytic mechanism. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10725249; 11322890; 11374901; 11707078; 12466854; 12466855; 16141072; 16602821; 17328885; 17576135; 19592578; 20152175; 20562862; 21267068; 21905163; 22008794; 23512661; 24227843; 25122198; 25263440; 25673722; 25780911; 26880803; 26889029; 26903501; 27389476; 27536883; 27728805; 27935821; 28759649; 30078722; 30084768; 30496141; 30626688; 30728831; 31099738; 31391268; 32303635; 32321537; 32379417; 32413319; 32441816; 32701507; 32837584; 33008593; 33168188; 33422505; 33558541; 34230470; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,526 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.B60; |