Overview
| Uniprot ID | Q92743 |
| Protein Name | Serine protease HTRA1 |
| Gene Name | HTRA1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 168 |
DPNSLRHKYNFIADV |
| 233 |
HRVKVELKNGATYEA |
| 261 |
IKIDHQGKLPVLLLG |
| 362 |
IPSDKIKKFLTESHD |
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
Protein Sequence
10
MQIPRAALLP
20
LLLLLLAAPA
30
SAQLSRAGRS
40
APLAAGCPDR
50
CEPARCPPQP
60
EHCEGGRARD
70
ACGCCEVCGA
80
PEGAACGLQE
90
GPCGEGLQCV
100
VPFGVPASAT
110
VRRRAQAGLC
120
VCASSEPVCG
130
SDANTYANLC
140
QLRAASRRSE
150
RLHRPPVIVL
160
QRGACGQGQE
170
DPNSLRHKYN
180
FIADVVEKIA
190
PAVVHIELFR
200
KLPFSKREVP
210
VASGSGFIVS
220
EDGLIVTNAH
230
VVTNKHRVKV
240
ELKNGATYEA
250
KIKDVDEKAD
260
IALIKIDHQG
270
KLPVLLLGRS
280
SELRPGEFVV
290
AIGSPFSLQN
300
TVTTGIVSTT
310
QRGGKELGLR
320
NSDMDYIQTD
330
AIINYGNSGG
340
PLVNLDGEVI
350
GINTLKVTAG
360
ISFAIPSDKI
370
KKFLTESHDR
380
QAKGKAITKK
390
KYIGIRMMSL
400
TSSKAKELKD
410
RHRDFPDVIS
420
GAYIIEVIPD
430
TPAEAGGLKE
440
NDVIISINGQ
450
SVVSANDVSD
460
VIKRESTLNM
470
VVRRGNEDIM
480
ITVIPEEIDP
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005576 |
extracellular region |
| Cellular Component |
GO:0005615 |
extracellular space |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Molecular Function |
GO:0019838 |
growth factor binding |
| Molecular Function |
GO:0042802 |
identical protein binding |
| Molecular Function |
GO:0140677 |
molecular function activator activity |
| Molecular Function |
GO:0004252 |
serine-type endopeptidase activity |
| Molecular Function |
GO:0008236 |
serine-type peptidase activity |
| Biological Process |
GO:0043065 |
positive regulation of apoptotic process |
| Biological Process |
GO:0012501 |
programmed cell death |
| Biological Process |
GO:0006508 |
proteolysis |
| Cellular Component |
GO:0070062 |
extracellular exosome |
| Cellular Component |
GO:0031012 |
extracellular matrix |
Reference
[1] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.