| IED ID | IndEnz0002004395 |
| Enzyme Type ID | protease004395 |
| 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 | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MTMLWLAVLLTCGAPAALLPTSGVGCPARCDPSSCSPAPTNCQSGETALRCGCCSVCAAAENERCGEGPEDPLCASGLRCVRNGGVTRCQCPSNQPVCGSDGKTYSSLCRLQAESKAVQGRGVAAIIPIQRGDCQQGQKDPDSPRYKYNFIADVVEKIAPAVVHIELFRILPFFKREVPAASGSGFIVSEDGLILTNAHVVTNKHRLKVERSDGSTYDAQIIDVDEKADIALIKIKAKGKLPVLLLGRSEELRPGEFVVAIGSPFSLQNTVTTGIVSTAQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVVGINTLKVTAGISFAIPSDKIRKFMAESHNRQSTGQGTKKKKYLGIRMMSLSQGKLKELKEQVKDFPENTSGAYIVEVLPDTPAEEAGLKEGDIIISISGKTVTSSSEVSEAIKKEGTLQMVIRRGNEDIPISVTPKEIEF |
| Enzyme Length | 459 |
| Uniprot Accession Number | A6YFB5 |
| Absorption | |
| Active Site | ACT_SITE 199; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q92743; ACT_SITE 229; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q92743; ACT_SITE 307; /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 and proteoglycans such as biglycan, syndecan-4 and glypican-4. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Consequently, facilitates inductive processes in the developing embryo, such as posteriorization, mesoderm induction and neuronal differentiation. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. Consequently, may regulate many physiological processes. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. {ECO:0000269|PubMed:17681134}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Domain (3); Erroneous initiation (1); Mutagenesis (1); Region (1); Sequence conflict (1); Signal peptide (1); Site (3) |
| Keywords | Cell membrane;Cytoplasm;Disulfide bond;Growth factor binding;Hydrolase;Membrane;Protease;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated by FGF4 and FGF8. {ECO:0000269|PubMed:17681134}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92743}. Secreted {ECO:0000269|PubMed:17681134}. 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..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,991 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.107; |