| IED ID | IndEnz0002003381 |
| Enzyme Type ID | protease003381 |
| Protein Name |
Serine protease hepsin EC 3.4.21.106 Transmembrane protease serine 1 Cleaved into: Serine protease hepsin non-catalytic chain; Serine protease hepsin catalytic chain |
| Gene Name | HPN TMPRSS1 |
| 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 | MAQKEGGRTVPCCSRPKVAALTAGTLLLLTAIGAASWAIVAVLLRSDQEPLYPVQVSSADARLMVFDKTEGTWRLLCSSRSNARVAGLSCEEMGFLRALTHSELDVRTAGANGTSGFFCVDEGRLPHTQRLLEVISVCDCPRGRFLAAICQDCGRRKLPVDRIVGGRDTSLGRWPWQVSLRYDGAHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVAQASPHGLQLGVQAVVYHGGYLPFRDPNSEENSNDIALVHLSSPLPLTEYIQPVCLPAAGQALVDGKICTVTGWGNTQYYGQQAGVLQEARVPIISNDVCNGADFYGNQIKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISRTPRWRLCGIVSWGTGCALAQKPGVYTKVSDFREWIFQAIKTHSEASGMVTQL |
| Enzyme Length | 417 |
| Uniprot Accession Number | P05981 |
| Absorption | |
| Active Site | ACT_SITE 203; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:12962630, ECO:0000305|PubMed:15839837"; ACT_SITE 257; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:12962630, ECO:0000305|PubMed:15839837"; ACT_SITE 353; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:12962630, ECO:0000305|PubMed:15839837" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys.; EC=3.4.21.106; Evidence={ECO:0000269|PubMed:15839837, ECO:0000269|PubMed:21875933, ECO:0000305|PubMed:26673890}; |
| DNA Binding | |
| EC Number | 3.4.21.106 |
| Enzyme Function | FUNCTION: Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL (PubMed:21875933, PubMed:15839837). Plays a role in cell growth and maintenance of cell morphology (PubMed:8346233, PubMed:21875933). Plays a role in the proteolytic processing of ACE2 (PubMed:24227843). Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization (PubMed:26673890). {ECO:0000269|PubMed:15839837, ECO:0000269|PubMed:21875933, ECO:0000269|PubMed:24227843, ECO:0000269|PubMed:26673890, ECO:0000269|PubMed:8346233}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (21); Chain (2); Disulfide bond (8); Domain (2); Glycosylation (1); Helix (11); Topological domain (2); Transmembrane (1); Turn (6) |
| Keywords | 3D-structure;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | Q12983; P11686; O00526 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1885621}; Single-pass type II membrane protein {ECO:0000269|PubMed:1885621}. Apical cell membrane {ECO:0000269|PubMed:26673890}; Single-pass type II membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1O5E; 1O5F; 1P57; 1Z8G; 3T2N; 5CE1; |
| Mapped Pubmed ID | 12629351; 1280830; 15324701; 15522303; 15583422; 15792801; 16783571; 16908524; 17309599; 18487557; 18698500; 18784072; 19911255; 20015050; 20166135; 20228799; 20673210; 21383634; 21750652; 22087277; 22132769; 22665141; 24409221; 25576733; 26014348; 26139199; 26165838; 26990747; 28886448; 30227221; 31395734; 31399560; 33300264; 33461973; 34131022; 9045658; 9346890; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,011 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.106; |