Detail Information for IndEnz0002006845
IED ID IndEnz0002006845
Enzyme Type ID protease006845
Protein Name Serine protease HTRA1
EC 3.4.21.-
High-temperature requirement A serine peptidase 1
Serine protease 11
Gene Name Htra1 Htra Prss11
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 MQFLRTALLSLLLLLLAAPSLALPSGISRSAPAATVCPEHCDPTRCAPPPTDCEGGRVRDACGCCEVCGALEGAVCGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDAKTYTNLCQLRAASRRSEKLRQPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELYRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKNRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDKIKKFLTESHDRQAKGKTVTKKKYIGIRMMSLTSSKAKELKDRHRDFPDVISGAYIIEVIPDTPAEAGGLKENDVIISINGQSVVTANDVSDVIKKENTLNMVVRRGNEDIVITVVPEEIDP
Enzyme Length 480
Uniprot Accession Number Q9QZK5
Absorption
Active Site ACT_SITE 220; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q92743; ACT_SITE 250; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q92743; ACT_SITE 328; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q92743
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 (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (2); Domain (3); Region (1); Signal peptide (1); Site (3)
Keywords Cell membrane;Cytoplasm;Disulfide bond;Growth factor binding;Hydrolase;Membrane;Protease;Reference proteome;Secreted;Serine protease;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92743}. Secreted {ECO:0000250|UniProtKB:Q92743}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92743}. Note=Predominantly secreted. Also found associated with the plasma membrane. {ECO:0000250|UniProtKB:Q92743}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 15333144; 16396496; 22595117;
Motif
Gene Encoded By
Mass 51,330
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda