Detail Information for IndEnz0002001395
IED ID IndEnz0002001395
Enzyme Type ID protease001395
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 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 MEPTVADVHLVPRTTKEVPALDAACCRAASIGVVATSLVVLTLGVLLAFLSTQGFHVDHTAELRGIRWTSSLRRETSDYHRTLTPTLEALLHFLLRPLQTLSLGLEEELLQRGIRARLREHGISLAAYGTIVSAELTGRHKGPLAERDFKSGRCPGNSFSCGNSQCVTKVNPECDDQEDCSDGSDEAHCECGLQPAWRMAGRIVGGMEASPGEFPWQASLRENKEHFCGAAIINARWLVSAAHCFNEFQDPTKWVAYVGATYLSGSEASTVRAQVVQIVKHPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCASLYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWILEATTKASMPLAPTMAPAPAAPSTAWPTSPESPVVSTPTKSMQALSTVPLDWVTVPKLQECGARPAMEKPTRVVGGFGAASGEVPWQVSLKEGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGSPVKIGLRRVVLHPLYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKASVGIIDQKTCSVLYNFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEAPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEIMSSQPLPMSPPSTTRMLATTSPRTTAGLTVPGATPSRPTPGAASRVTGQPANSTLSAVSTTARGQTPFPDAPEATTHTQLPDCGLAPAALTRIVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDVYGDPKQWAAFLGTPFLSGAEGQLERVARIYKHPFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFYPVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWIGQHIQE
Enzyme Length 1059
Uniprot Accession Number Q7Z410
Absorption
Active Site ACT_SITE 243; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 292; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 387; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 544; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 592; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 687; /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:0000269|PubMed:12886014}.
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.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (6); Chain (4); Compositional bias (1); Disulfide bond (15); Domain (4); Frameshift (1); Glycosylation (4); Natural variant (7); Region (2); Sequence caution (1); Sequence conflict (2); 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:0000269|PubMed:12886014}; Single-pass type II membrane protein {ECO:0000269|PubMed:12886014}.
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. {ECO:0000269|PubMed:12886014}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 16872279; 20379614; 23229837; 24756697; 31943016;
Motif
Gene Encoded By
Mass 114,021
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda