| Gene Symbol |
Htra1
|
| Entrez Gene |
56213
|
| Alt Symbol |
AI429470, HTRA, L56, Prss11, RSPP11
|
| Species |
Mouse
|
| Gene Type |
protein-coding
|
| Description |
HtrA serine peptidase 1
|
| Other Description |
high-temperature requirement A serine peptidase 1|insulin-like growth factor binding protein 5 protease|protease, serine, 11 (Igf binding)|serine protease 11|serine protease HTRA1
|
| Swissprots |
Q91WS3 Q9R118 Q9QZK6 Q8BN05 Q8BN04
|
| Accessions |
EDL17688 EDL17689 Q9R118 AF172994 AAD49422 AF179369 AAD52682 AI429470 AK090320 BAC41168 AK090321 BAC41169 AK128916 AK132270 BAE21071 AK167667 BAE39716 BC013516 AAH13516 CB193609 NM_019564 NP_062510
|
| 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, but it is unclear whether it leads to the proteolytic degradation of TGF-beta proteins themselves (PubMed:18551132) or not (PubMed:14973287). By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrad
|
| Subcellular Location |
Secreted {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Predominantly secreted. Also found associated with the plasma membrane. {ECO:0000250}.
|
| Tissue Specificity |
In the brain, mainly expressed in cortical areas both in glial cells and neurons (at protein level). In bones, deposited in the matrix, with higher level in newly formed bone compared to fully calcified bone (at protein level). Also expressed in the tendons (at protein level). In the articular cartilage, detected only in the deepest zone of the joint cartilage. Not detected in the chondrocytes of the growth plate (at protein level). In an experimental arthritis model, at early disease stages, up-regulated in articular chondrocytes in the deep layers of the cartilage (at protein level). As arthritis progresses, chondrocyte expression expands toward the surface. {ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:15993670, ECO:0000269|PubMed:18551132}.
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