| IED ID | IndEnz0002006847 |
| Enzyme Type ID | protease006847 |
| Protein Name |
Serine protease HTRA1 EC 3.4.21.- High-temperature requirement A serine peptidase 1 L56 Serine protease 11 |
| Gene Name | HTRA1 HTRA PRSS11 |
| 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 | MQIPRAALLPLLLLLLAAPASAQLSRAGRSAPLAAGCPDRCEPARCPPQPEHCEGGRARDACGCCEVCGAPEGAACGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDANTYANLCQLRAASRRSERLHRPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELFRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKHRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDKIKKFLTESHDRQAKGKAITKKKYIGIRMMSLTSSKAKELKDRHRDFPDVISGAYIIEVIPDTPAEAGGLKENDVIISINGQSVVSANDVSDVIKRESTLNMVVRRGNEDIMITVIPEEIDP |
| Enzyme Length | 480 |
| Uniprot Accession Number | Q92743 |
| Absorption | |
| Active Site | ACT_SITE 220; /note=Charge relay system; /evidence=ECO:0000269|PubMed:21297635; ACT_SITE 250; /note=Charge relay system; /evidence=ECO:0000269|PubMed:21297635; ACT_SITE 328; /note=Charge relay system; /evidence=ECO:0000269|PubMed:21297635 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. {ECO:0000269|PubMed:16377621, ECO:0000269|PubMed:20671064, ECO:0000269|PubMed:9852107}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (30); Chain (1); Disulfide bond (2); Domain (3); Helix (11); Mutagenesis (1); Natural variant (14); Region (1); Sequence conflict (1); Signal peptide (1); Site (3); Turn (4) |
| Keywords | 3D-structure;Age-related macular degeneration;Cell membrane;Cytoplasm;Direct protein sequencing;Disease variant;Disulfide bond;Growth factor binding;Hydrolase;Membrane;Protease;Reference proteome;Secreted;Serine protease;Signal |
| Interact With | Itself; P83105; P10636-8; P14174; P07996 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21297635}. Secreted {ECO:0000269|PubMed:15208355, ECO:0000269|PubMed:9852107}. Cytoplasm, cytosol {ECO:0000269|PubMed:15208355, ECO:0000269|PubMed:20671064}. Note=Predominantly secreted (PubMed:15208355). Also found associated with the plasma membrane (PubMed:21297635). {ECO:0000269|PubMed:15208355, ECO:0000269|PubMed:21297635}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | NMR spectroscopy (2); X-ray crystallography (9) |
| Cross Reference PDB | 2JOA; 2YTW; 3NUM; 3NWU; 3NZI; 3TJN; 3TJO; 3TJQ; 6Z0E; 6Z0X; 6Z0Y; |
| Mapped Pubmed ID | 12577067; 14716297; 14973287; 15231748; 15855271; 15917099; 16385451; 16650464; 16767218; 17072861; 17094466; 17292962; 17426452; 17438519; 17568988; 17679948; 17692272; 17718385; 17884985; 17904186; 17962403; 18079691; 18156628; 18161619; 18162041; 18164066; 18206206; 18207215; 18241672; 18301036; 18316707; 18362109; 18427598; 18436811; 18452160; 18515590; 18681782; 18682806; 18682812; 18718667; 18806297; 18939352; 19001225; 19026638; 19043567; 19056122; 19065273; 19117936; 19169232; 19187590; 19202148; 19255159; 19259132; 19301262; 19375943; 19424634; 19470753; 19491722; 19636338; 19657146; 19680273; 19688690; 19783326; 19796758; 19798546; 19845562; 19913121; 19933195; 19948975; 20132989; 20140183; 20157352; 20238042; 20346514; 20378180; 20379614; 20381870; 20388781; 20445115; 20456446; 20469960; 20533271; 20538655; 20576771; 20606025; 20628086; 20664794; 20678803; 20688737; 20711500; 20881291; 20888482; 20940247; 20943460; 21031019; 21060055; 21067572; 21115960; 21122828; 21163940; 21191724; 21203342; 21282580; 21320870; 21402993; 21558292; 21622153; 21708937; 21817962; 21844367; 21882634; 21899153; 21959923; 21988832; 22049084; 22155582; 22259222; 22487577; 22491416; 22535953; 22556410; 22578544; 22582805; 22705344; 22761798; 22865667; 22900900; 22923201; 22935172; 23056244; 23060141; 23079781; 23083999; 23204795; 23209669; 23337555; 23362846; 23414945; 23478260; 23534868; 23580433; 23582991; 23592924; 23644223; 23673665; 23687431; 23712470; 23963851; 24013816; 24080590; 24356998; 24493577; 24535794; 24846539; 24854852; 24865190; 24907345; 24979214; 25002585; 25077532; 25277308; 25329061; 25369932; 25519903; 25530301; 25550099; 25627090; 25687108; 25715554; 25726184; 25761858; 25772074; 25776486; 26035313; 26187609; 26310622; 26337002; 26403966; 26427389; 26496610; 26708185; 26848857; 26864869; 27125063; 27164673; 27338780; 27379525; 27388476; 27809811; 27841854; 27879347; 28076935; 28432852; 28586045; 28628911; 28659708; 28667026; 28689406; 28726057; 28782182; 28846052; 28941979; 28992183; 29093542; 29096998; 29101275; 29266444; 29269042; 29269789; 29409460; 29412803; 29414786; 29561953; 29572155; 29695130; 29725820; 29730901; 29801032; 29863874; 29895533; 30015931; 30068478; 30131069; 30795802; 30859180; 30895599; 31088682; 31197037; 31385385; 31583032; 31601092; 31658355; 31884580; 32017060; 32218415; 32328755; 32345717; 32486357; 32777973; 32814029; 32838591; 32878625; 32895092; 33109952; 33198211; 33268848; 33387109; 33493738; 33601219; 33636181; 33661357; 33743591; 33746601; 33930395; 34192300; 34270682; 34301870; 34303089; 34310874; 34472763; 34626176; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,287 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.107;3.4.21.108; |