Detail Information for IndEnz0002001396
IED ID IndEnz0002001396
Enzyme Type ID protease001396
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 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 MEPTAPDLQLVPEVTKAVSVSAPDPGPCRTAVIAVVGISMAIVTLGVLSAFFSAQGAHVEHIAELHGIRFTSSLQQENSDFYRLLTHALQTLLHFLLRALQPLSLKQEADILQKGIQARLQEQGLSLAAYGTIVSVELTGRCEGPVTERDLKSGHCPGNVFSCQNGQCVSKENPECDDRVDCSDESDEAQCDCGWQPAWRSAGRIVGGVEAAPGEFPWQVSLRENHEHFCGATIIGARWLVSAAHCFNEFQDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKHPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSSLYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWILEVTSAADMPVVPTATPAPATPSTPWPTSPESWAPNTFAKPTAAPSPVPLHPSTTAKPQECGARPAMDKPTRIVGGISAVSGEVPWQASLKEGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGSPVKLGLRRVALHPRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGALYNFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWILKAMSSDPSSMARPHTSSTRLIPSEPPKTTAAGLIIPEATTSRLATPRATIRVTTRPLNTTLSARSTTTRGQTAAPSAPGTTIHSHLPDCGLAPPGALTRIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDIYGDPMQWAAFLGTPFLSSTEGQLERVARIYRHPFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPARPPDGARCVITGWGSLREGGSMARQLQKAAVRVLSEQTCRRFYPVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPSGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWIGQNIQE
Enzyme Length 1065
Uniprot Accession Number P69525
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 (3); Disulfide bond (15); Domain (4); Glycosylation (4); Region (3); Site (3); Topological domain (2); Transmembrane (1)
Keywords Cell membrane;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 16602821; 16872279; 17655505; 31943016;
Motif
Gene Encoded By
Mass 114,486
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda