Detail Information for IndEnz0002002449
IED ID IndEnz0002002449
Enzyme Type ID protease002449
Protein Name Serine protease hepsin
EC 3.4.21.106

Cleaved into: Serine protease hepsin non-catalytic chain; Serine protease hepsin catalytic chain
Gene Name Hpn
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 MAKEDEEPGAHRGGSTCSRPQPGKGGRTAACCSRPKVAALIVGTLLFLTGIGAASWAIVTILLQSDQEPLYQVQLSPGDSRLAVFDKTEGTWRLLCSSRSNARVAGLGCEEMGFLRALAHSELDVRTAGANGTSGFFCVDEGGLPLAQRLLDVISVCDCPRGRFLTATCQDCGRRKLPVDRIVGGQDSSLGRWPWQVSLRYDGTHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVARTSPHAVQLGVQAVIYHGGYLPFRDPTIDENSNDIALVHLSSSLPLTEYIQPVCLPAAGQALVDGKVCTVTGWGNTQFYGQQAMVLQEARVPIISNEVCNSPDFYGNQIKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISGTSRWRLCGIVSWGTGCALARKPGVYTKVTDFREWIFKAIKTHSEASGMVTQP
Enzyme Length 436
Uniprot Accession Number O35453
Absorption
Active Site ACT_SITE 222; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P05981; ACT_SITE 276; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P05981; ACT_SITE 372; /note=Charge relay system; /evidence=ECO:0000305|PubMed:9395459
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:0000305|PubMed:26673890, ECO:0000305|PubMed:9395459};
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. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2 (By similarity). Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization (PubMed:26673890). {ECO:0000250|UniProtKB:P05981, ECO:0000269|PubMed:26673890}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Chain (2); Disulfide bond (8); Domain (2); Frameshift (1); Glycosylation (1); Mutagenesis (1); Region (1); Sequence conflict (6); 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
Induction
Subcellular Location SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:26673890}; Single-pass type II membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P05981}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P05981}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:9395459}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 12744720; 12962630; 15324701; 16428450; 16908524; 17174946; 17918732; 18554416; 18726901; 18784072; 18973680; 19938013; 20152175; 20683358; 21267068; 21386911; 21677750; 21947380; 22912808; 31444371; 32404422; 8346233;
Motif
Gene Encoded By
Mass 46,821
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.106;