IED ID | IndEnz0002001392 |
Enzyme Type ID | protease001392 |
Protein Name |
Transmembrane protease serine 7 EC 3.4.21.- Matriptase-3 |
Gene Name | Tmprss7 |
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 | MDKEKSDPSCKSSDLKISNISIQVVSVPGKLPGRRPPRKPIGKPRPRKQPKKRAPFWNVQNKIILFTVFLFILAVTAWTLLWLYISKTESKDAFYFVGMFRITNIEFLPEYRQKESREFLSMAKTVQQVVNLVYTTSAFSKFYKQSVVADVSSNNKGGLLVHFWIVFVMPHAKGHIFCEECVAAILKDSIQTSIINRTSVGSLQGLAVDMDSVVLNAGLRSDYSSAVGSDNGCSRYLYADHLTLRYPLEISATSGQLMCHFKLVAIVGYLIRLSIESIQLEADNCITDSLTVYDSLLPIRSAILYRICEPTRTLMSFVSTNNLMLVILKSPYVRRLAGIRAYFEVIPEQKCESTILVKEINSFEGKISSPYYPSYYPPKCKCTWTFQTSLSTLGIALKFYNYSITKKSAKGCEHGWWEINEHMYCGSYMDHETIFRVPSPLVHIQLQCSSRLSDKPLLVEYGGYNISQPCPAGSFRCSSGLCVPQAQRCDGVNDCFDESDELFCVTVKPACNSSSFRQHGPLVCDGFRDCEDGQDEQNCTRSIPCTSRTFKCGNDICFRKQNAQCDGIVDCPDGSDEEGCGCSRSSSFLHRIVGGSDSQEGTWPWQVSLHFVGSAYCGASVISREWLLSAAHCFHGNRLSDPTPWTAHLGMYVQGNAKFISPVRRIVVHEYYNSQTFDYDIALLQLSIAWPETLKQLIQPICIPPAGQKVRSGEKCWVTGWGRRHEADSKGSPVLQQAEVELIDQTVCVSTYGIITSRMLCAGVMSGKSDACKGDSGGPLSCRRKSDGKWILTGIVSWGHGCGRPNFPGVYTRVSSFVPWIHKYVPSLL |
Enzyme Length | 829 |
Uniprot Accession Number | Q8BIK6 |
Absorption | |
Active Site | ACT_SITE 632; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 680; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 776; /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: Serine protease which preferentially hydrolyzes peptides with Arg at the P1 position. {ECO:0000269|PubMed:15853774}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Compositional bias (1); Disulfide bond (15); Domain (7); Frameshift (1); Glycosylation (2); Region (1); Sequence caution (1); Sequence conflict (5); Site (1); Topological domain (2); Transmembrane (1) |
Keywords | Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Repeat;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15853774}; Single-pass type II membrane protein {ECO:0000269|PubMed:15853774}. |
Modified Residue | |
Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:15853774}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 19592578; 21267068; 21677750; |
Motif | |
Gene Encoded By | |
Mass | 92,590 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=240 nM for Suc-Ala-Ala-Pro-Arg-pNA {ECO:0000269|PubMed:15853774}; KM=534 nM for Suc-Ala-Ala-Pro-Lys-pNA {ECO:0000269|PubMed:15853774}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |