| IED ID | IndEnz0002001389 |
| Enzyme Type ID | protease001389 |
| Protein Name |
Transmembrane protease serine 4 EC 3.4.21.- Channel-activating protease 2 CAPH2 Membrane-type serine protease 2 MT-SP2 Cleaved into: Transmembrane protease serine 4 catalytic chain |
| Gene Name | TMPRSS4 TMPRSS3 UNQ776/PRO1570 |
| Organism | Homo sapiens (Human) |
| 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 Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MLQDPDSDQPLNSLDVKPLRKPRIPMETFRKVGIPIIIALLSLASIIIVVVLIKVILDKYYFLCGQPLHFIPRKQLCDGELDCPLGEDEEHCVKSFPEGPAVAVRLSKDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSSKPTFRAVEIGPDQDLDVVEITENSQELRMRNSSGPCLSGSLVSLHCLACGKSLKTPRVVGVEEASVDSWPWQVSIQYDKQHVCGGSILDPHWVLTAAHCFRKHTDVFNWKVRAGSDKLGSFPSLAVAKIIIIEFNPMYPKDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQASVQVIDSTRCNADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSDQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWIYNVWKAEL |
| Enzyme Length | 437 |
| Uniprot Accession Number | Q9NRS4 |
| Absorption | |
| Active Site | ACT_SITE 245; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 290; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 387; /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 directly induces processing of pro-uPA/PLAU into the active form through proteolytic activity (PubMed:24434139). Seems to be capable of activating ENaC (By similarity). {ECO:0000250|UniProtKB:Q8VCA5, ECO:0000269|PubMed:24434139}.; FUNCTION: (Microbial infection) In gut epithelial cells, facilitates human coronavirus SARS-CoV-2 infection through, at least, the cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. {ECO:0000269|PubMed:32404436}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (3); Chain (2); Disulfide bond (8); Domain (3); Frameshift (1); Glycosylation (2); Mutagenesis (2); Natural variant (3); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Secreted;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | O60238; P58418; P48730-2; P60508; Q5JX71; Q8TBE3; Q8TED1; Q8N6L0; Q8TDF6-2; Q96PQ1; Q96L08; Q9BSE2; Q9BXN2; Q8N6L0; Q8N205; Q9BSE2 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:24434139}; Single-pass type II membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Transmembrane protease serine 4 catalytic chain]: Secreted {ECO:0000269|PubMed:24434139}. Note=Activated by cleavage and secreted. {ECO:0000269|PubMed:24434139}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically processed; probably by an autocatalytic mechanism. {ECO:0000305|PubMed:25203520}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 25416956; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,246 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |