| IED ID | IndEnz0002003574 |
| Enzyme Type ID | protease003574 |
| Protein Name |
Serine protease HTRA3 EC 3.4.21.- High-temperature requirement factor A3 Pregnancy-related serine protease |
| Gene Name | HTRA3 PRSP |
| 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 | MQARALLLAALAALALAREPPAAPCPARCDVSRCPSPRCPGGYVPDLCNCCLVCAASEGEPCGGPLDSPCGESLECVRGLCRCRWSHAVCGTDGHTYANVCALQAASRRALQLSGTPVRQLQKGACPLGLHQLSSPRYKFNFIADVVEKIAPAVVHIELFLRHPLFGRNVPLSSGSGFIMSEAGLIITNAHVVSSNSAAPGRQQLKVQLQNGDSYEATIKDIDKKSDIATIKIHPKKKLPVLLLGHSADLRPGEFVVAIGSPFALQNTVTTGIVSTAQREGRELGLRDSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDRITRFLTEFQDKQIKDWKKRFIGIRMRTITPSLVDELKASNPDFPEVSSGIYVQEVAPNSPSQRGGIQDGDIIVKVNGRPLVDSSELQEAVLTESPLLLEVRRGNDDLLFSIAPEVVM |
| Enzyme Length | 453 |
| Uniprot Accession Number | P83110 |
| Absorption | |
| Active Site | ACT_SITE 191; /note="Charge relay system"; /evidence="ECO:0000269|PubMed:26110759"; ACT_SITE 227; /note="Charge relay system"; /evidence="ECO:0000269|PubMed:26110759"; ACT_SITE 305; /note="Charge relay system"; /evidence="ECO:0000269|PubMed:22229724, ECO:0000269|PubMed:26110759" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease that cleaves beta-casein/CSN2 as well as several extracellular matrix (ECM) proteoglycans such as decorin/DCN, biglycan/BGN and fibronectin/FN1. Inhibits signaling mediated by TGF-beta family proteins possibly indirectly by degradation of these ECM proteoglycans (By similarity). May act as a tumor suppressor. Negatively regulates, in vitro, trophoblast invasion during placental development and may be involved in the development of the placenta in vivo. May also have a role in ovarian development, granulosa cell differentiation and luteinization (PubMed:21321049, PubMed:22229724). {ECO:0000250|UniProtKB:Q9D236, ECO:0000269|PubMed:21321049, ECO:0000269|PubMed:22229724}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Beta strand (20); Chain (1); Disulfide bond (2); Domain (3); Helix (8); Mutagenesis (1); Region (1); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Alternative splicing;Disulfide bond;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal |
| Interact With | P60709; Itself; P83105; P17987; P98170; P02666; Itself; P17987; P08670; P98170; P17987; P08670; P98170 |
| Induction | INDUCTION: Down-regulated in ovarian and endometrial cancers (EC). Decrease of 3.2-fold in endometrial cancer. {ECO:0000269|PubMed:16650464, ECO:0000269|PubMed:19424634}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21321049}. Note=Secretion increased during decidualization of endometrial stromal cells. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2P3W; 4RI0; |
| Mapped Pubmed ID | 16251496; 18241672; 19359045; 19951697; 20068077; 20154083; 20379614; 20469960; 20711500; 21035848; 21047919; 21555518; 22923201; 23049902; 23812730; 25002585; 25274382; 25456008; 27166271; 28642151; 28716573; 28860718; 29266444; 29477555; 30139517; 30940659; 31013509; 31180543; 31260151; 31280864; 31899476; 32486357; 33462352; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,608 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.108; |