Overview
| Uniprot ID | P08254 |
|---|
| Protein Name | Stromelysin-1 |
|---|
| Gene Name | MMP3 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 127 |
NYTPDLPKDAVDSAV |
| 387 |
GFPPTVRKIDAAISD |
| 395 |
IDAAISDKEKNKTYF |
Function
Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9 (PubMed:11029580, PubMed:1371271). Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway (PubMed:2383557). Also acts intracellularly (PubMed:22265821). For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage (PubMed:21330369). In addition, plays a role in immune response and possesses antiviral activity against various viruses such as vesicular stomatitis virus, influenza A virus (H1N1) and human herpes virus 1 (PubMed:35940311). Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities (PubMed:35940311)
Protein Sequence
10
MKSLPILLLL
20
CVAVCSAYPL
30
DGAARGEDTS
40
MNLVQKYLEN
50
YYDLKKDVKQ
60
FVRRKDSGPV
70
VKKIREMQKF
80
LGLEVTGKLD
90
SDTLEVMRKP
100
RCGVPDVGHF
110
RTFPGIPKWR
120
KTHLTYRIVN
130
YTPDLPKDAV
140
DSAVEKALKV
150
WEEVTPLTFS
160
RLYEGEADIM
170
ISFAVREHGD
180
FYPFDGPGNV
190
LAHAYAPGPG
200
INGDAHFDDD
210
EQWTKDTTGT
220
NLFLVAAHEI
230
GHSLGLFHSA
240
NTEALMYPLY
250
HSLTDLTRFR
260
LSQDDINGIQ
270
SLYGPPPDSP
280
ETPLVPTEPV
290
PPEPGTPANC
300
DPALSFDAVS
310
TLRGEILIFK
320
DRHFWRKSLR
330
KLEPELHLIS
340
SFWPSLPSGV
350
DAAYEVTSKD
360
LVFIFKGNQF
370
WAIRGNEVRA
380
GYPRGIHTLG
390
FPPTVRKIDA
400
AISDKEKNKT
410
YFFVEDKYWR
420
FDEKRNSMEP
430
GFPKQIAEDF
440
PGIDSKIDAV
450
FEEFGFFYFF
460
TGSSQLEFDP
470
NAKKVTHTLK
SNSWLNC
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0031012 |
extracellular matrix |
| Cellular Component |
GO:0005576 |
extracellular region |
| Cellular Component |
GO:0005615 |
extracellular space |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0004175 |
endopeptidase activity |
| Molecular Function |
GO:0004222 |
metalloendopeptidase activity |
| Molecular Function |
GO:0008237 |
metallopeptidase activity |
| Molecular Function |
GO:0008233 |
peptidase activity |
| Molecular Function |
GO:0004252 |
serine-type endopeptidase activity |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0071222 |
cellular response to lipopolysaccharide |
| Biological Process |
GO:0071732 |
cellular response to nitric oxide |
| Biological Process |
GO:0034614 |
cellular response to reactive oxygen species |
| Biological Process |
GO:0071492 |
cellular response to UV-A |
| Biological Process |
GO:0030574 |
collagen catabolic process |
| Biological Process |
GO:0022617 |
extracellular matrix disassembly |
| Biological Process |
GO:0030198 |
extracellular matrix organization |
| Biological Process |
GO:0045087 |
innate immune response |
| Biological Process |
GO:0051898 |
negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction |
| Biological Process |
GO:2000378 |
negative regulation of reactive oxygen species metabolic process |
| Biological Process |
GO:0031334 |
positive regulation of protein-containing complex assembly |
| Biological Process |
GO:0030163 |
protein catabolic process |
| Biological Process |
GO:0006508 |
proteolysis |
| Biological Process |
GO:0150077 |
regulation of neuroinflammatory response |
| Biological Process |
GO:1904645 |
response to amyloid-beta |
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.