| IED ID | IndEnz0002009508 |
| Enzyme Type ID | protease009508 |
| Protein Name |
Suppressor of tumorigenicity 14 protein EC 3.4.21.109 Matriptase Membrane-type serine protease 1 MT-SP1 Prostamin Serine protease 14 Serine protease TADG-15 Tumor-associated differentially-expressed gene 15 protein |
| Gene Name | ST14 PRSS14 SNC19 TADG15 |
| 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 | MGSDRARKGGGGPKDFGAGLKYNSRHEKVNGLEEGVEFLPVNNVKKVEKHGPGRWVVLAAVLIGLLLVLLGIGFLVWHLQYRDVRVQKVFNGYMRITNENFVDAYENSNSTEFVSLASKVKDALKLLYSGVPFLGPYHKESAVTAFSEGSVIAYYWSEFSIPQHLVEEAERVMAEERVVMLPPRARSLKSFVVTSVVAFPTDSKTVQRTQDNSCSFGLHARGVELMRFTTPGFPDSPYPAHARCQWALRGDADSVLSLTFRSFDLASCDERGSDLVTVYNTLSPMEPHALVQLCGTYPPSYNLTFHSSQNVLLITLITNTERRHPGFEATFFQLPRMSSCGGRLRKAQGTFNSPYYPGHYPPNIDCTWNIEVPNNQHVKVRFKFFYLLEPGVPAGTCPKDYVEINGEKYCGERSQFVVTSNSNKITVRFHSDQSYTDTGFLAEYLSYDSSDPCPGQFTCRTGRCIRKELRCDGWADCTDHSDELNCSCDAGHQFTCKNKFCKPLFWVCDSVNDCGDNSDEQGCSCPAQTFRCSNGKCLSKSQQCNGKDDCGDGSDEASCPKVNVVTCTKHTYRCLNGLCLSKGNPECDGKEDCSDGSDEKDCDCGLRSFTRQARVVGGTDADEGEWPWQVSLHALGQGHICGASLISPNWLVSAAHCYIDDRGFRYSDPTQWTAFLGLHDQSQRSAPGVQERRLKRIISHPFFNDFTFDYDIALLELEKPAEYSSMVRPICLPDASHVFPAGKAIWVTGWGHTQYGGTGALILQKGEIRVINQTTCENLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEADGRIFQAGVVSWGDGCAQRNKPGVYTRLPLFRDWIKENTGV |
| Enzyme Length | 855 |
| Uniprot Accession Number | Q9Y5Y6 |
| Absorption | |
| Active Site | ACT_SITE 656; /note=Charge relay system; ACT_SITE 711; /note=Charge relay system; ACT_SITE 805; /note=Charge relay system |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position.; EC=3.4.21.109; Evidence={ECO:0000269|PubMed:16407223}; |
| DNA Binding | |
| EC Number | 3.4.21.109 |
| Enzyme Function | FUNCTION: Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site. Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing. {ECO:0000269|PubMed:18843291}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (18); Chain (1); Disulfide bond (18); Domain (8); Glycosylation (4); Helix (5); Mutagenesis (3); Natural variant (3); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1); Turn (4) |
| Keywords | 3D-structure;Disease variant;Disulfide bond;Glycoprotein;Hydrolase;Hypotrichosis;Ichthyosis;Membrane;Protease;Reference proteome;Repeat;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (23) |
| Cross Reference PDB | 1EAW; 1EAX; 2GV6; 2GV7; 3BN9; 3NCL; 3NPS; 3P8F; 3P8G; 3SO3; 4IS5; 4ISL; 4ISN; 4ISO; 4JYT; 4JZ1; 4JZI; 4O97; 4O9V; 4R0I; 5LYO; 6N4T; 6T9T; |
| Mapped Pubmed ID | 11380615; 11792696; 11864986; 12498394; 12738778; 14584072; 14747469; 15075215; 15200890; 15611789; 15803139; 16061697; 16103220; 16237759; 16273651; 16353247; 16439987; 16501837; 16794252; 16820046; 16821772; 17131055; 17228523; 17344310; 17389401; 17456594; 17940283; 17981566; 17981575; 18263585; 18274158; 18514224; 18550704; 18649735; 18649738; 18713750; 18723439; 18813126; 19242518; 19443387; 19535514; 19546220; 19578749; 19940125; 20015050; 20142489; 20145119; 20379614; 20652801; 20657595; 20696767; 20716618; 20971737; 21097670; 21098708; 21123732; 21148558; 21217780; 21276938; 21678412; 21693064; 21795523; 21988832; 22031598; 22081509; 22087277; 22088470; 22118498; 22154938; 22514623; 22582115; 22750143; 22783993; 22811538; 23044656; 23192872; 23365447; 23443661; 23443662; 23466486; 23673661; 23900022; 24004857; 24070417; 24248283; 24382204; 24617769; 24696092; 24705933; 24794746; 24900621; 25556099; 25640309; 25730905; 25786220; 25873032; 26157007; 26513078; 26996264; 27167193; 27316827; 27356668; 27528224; 28362108; 29054928; 29118397; 29438412; 29611532; 29953855; 30087389; 30409910; 30729623; 31543462; 32241917; 32326212; 32493324; 32761920; 33094801; 34418985; |
| Motif | |
| Gene Encoded By | |
| Mass | 94,770 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.109; |