| IED ID | IndEnz0002001397 |
| Enzyme Type ID | protease001397 |
| Protein Name |
Transmembrane protease serine 9 EC 3.4.21.- Polyserase-I Polyserine protease 1 Polyserase-1 Cleaved into: Serase-1; Serase-2; Serase-3 |
| Gene Name | Tmprss9 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MEPAAPDLQPVPEVTKGVPVPTPDSGCCRAAVTTVVAISVASLTLGVLSAFLSAQGVQVEHTAQLHGVRFTSLLQQENSDFYRLLTPALQTLLHFLLRALQPLSLDQEADILQKGIQARLQGQGLSLAAYGTITSVELTGRCEGPVTERDLKSGHCPGNAFSCQNSQCVSKENPECDDRVDCSDGSDEAQCDCGWQPAWRSAGRIVGGAEAAPGEFPWQVSLRENHEHFCGATIIGARWLVSAAHCFNEFQDPAQWAAQAGSVHLSGSEASAVRARVLRIAKHPAYNADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPRKKCLISGWGYLKEDFLVKPEVLQKATVELLDQNLCSSLYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPSGRFFLAGVVSWGIGCAEARRPGVYTRVTRLRDWILEVTSSADTPVVPTEAPAPITPSTPWPTSPESRVPNTTAKPTVAPTPAPLHPSTAAKPQECGARPAMDKPTRIVGGISAVSGEVPWQASLKEGSRHFCGATVVGDRWLLSAAHCFNHTKLEQVQAHLGTVSLLGVGGSPVKLGLRSVALHPRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGALYNFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWILKAMSSDPSSTAHPHTSSTRLIPSQPPTTTAAGLIPEASTGRPATLRATIRVTTRPLNTTLSARSTTTRRQTPAPGTTVFSHLPDCGLAPPGALTRIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDVYGDPMQWAAFLGTPFLSSTEGQLERVARIYRHPFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPTRPPEGARCVITGWGSLREGGSMARQLQKAAVRVLSEQTCRRFYPVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPSGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWIGQNIRE |
| Enzyme Length | 1061 |
| Uniprot Accession Number | P69526 |
| Absorption | |
| Active Site | ACT_SITE 245; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 294; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 389; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 546; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 594; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 689; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by serine protease inhibitors PMSF and 4-(2-aminoethyl)benzenesulfonyl fluoride, but not by EDTA. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serase-1 and serase-2 are serine proteases that hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala-Pro-Ala-AMC are not significantly hydrolyzed (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (6); Chain (4); Compositional bias (2); Disulfide bond (15); Domain (4); Glycosylation (5); Region (3); Site (3); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Repeat;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved to generate 3 independent serine protease chains. The cleaved chains may remain attached to the membrane thanks to disulfide bonds. It is unclear whether cleavage always takes place (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16872279; |
| Motif | |
| Gene Encoded By | |
| Mass | 113,890 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |