| General Information |
| MoonProt ID | 449 |
| First appeared in release | 3.0 |
| Name(s) | Stromelysin-1, Matrix metalloproteinase-3, Transin-1
Gene: MMP3 |
| UniProt ID | P28862 (MMP3_MOUSE) |
| GO terms | GO:0004175 endopeptidase activity
GO:0004222 metalloendopeptidase activity
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0006508 proteolysis
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0010727 negative regulation of hydrogen peroxide metabolic process
GO:0016787 hydrolase activity
GO:0030163 protein catabolic process
GO:0030198 extracellular matrix organization
GO:0030334 regulation of cell migration
GO:0030335 positive regulation of cell migration
GO:0030425 dendrite
GO:0030574 collagen catabolic process
GO:0031012 extracellular matrix
GO:0031334 positive regulation of protein-containing complex assembly
GO:0032991 protein-containing complex
GO:0044297 cell body
GO:0044877 protein-containing complex binding
GO:0046872 metal ion binding
GO:0051898 negative regulation of protein kinase B signaling
GO:0071230 cellular response to amino acid stimulus
GO:1903209 positive regulation of oxidative stress-induced cell death |
| Organisms for which functions have been demonstrated | Mus musculus (Mouse, mammal) |
| Sequence length | 477 amino acids |
| FASTA sequence | >sp|P28862|MMP3_MOUSE Stromelysin-1 OS=Mus musculus OX=10090 GN=Mmp3 PE=2 SV=2
MKGLPVLLWLCVVVCSSYPLHDSARDDDAGMELLQKYLENYYGLAKDVKQFIKKKDSSLIVKKIQEMQKFLGLEMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFVPFDGPGTVLAHAYAPGPGINGDAHFDDDERWTEDVTGTNLFLVAAHELGHSLGLYHSAKAEALMYPVYKSSTDLSRFHLSQDDVDGIQSLYGTPTASPDVLVVPTKSNSLEPETSPMCSSTLFFDAVSTLRGEVLFFKDRHFWRKSLRTPEPEFYLISSFWPSLPSNMDAAYEVTNRDTVFIFKGNQFWAIRGHEELAGYPKSIHTLGLPATVKKIDAAISNKEKRKTYFFVEDKYWRFDEKKQSMEPGFPRKIAEDFPGVDSRVDAVFEAFGFLYFFSGSSQLEFDPNAKKVTHILKSNSWFNC |
| Structure Information |
| PDB ID | NA; closest has53% sequence identity, 1SU3_A |
| Quaternary structure | NA |
| SCOP | NA |
| CATH | NA |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
moonID_449_uniID_P28862 is 477 residues long, with 0 residues (0.00%) predicted as disordered.The protein has 0 short (< 30 residues) disorder segments and 0 long (>= 30 residues) disorder segments. |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Metalloprotease (degrades fibronectin, gelatin, proteoglycans, denatured type I collagen, laminin, and other extracellular matrix components) |
| References for function | 26499805 |
| E.C. number | NA |
| Location of functional site(s) | NA |
| Cellular location of function | cell surface |
| Comments | NA |
| Function 2 |
| Function description | transcription factor |
| References for function | Si-Tayeb K, Monvoisin A, Mazzocco C, et al. Matrix metalloproteinase 3 is present in the cell nucleus and is involved in apoptosis. Am J Pathol. 2006;169(4):1390-1401. doi:10.2353/ajpath.2006.060005;
Zuo X, Pan W, Feng T, Shi X, Dai J (2014) Matrix Metalloproteinase 3 Promotes Cellular Anti-Dengue Virus Response via Interaction with Transcription Factor NFkB in Cell Nucleus. PLoS ONE 9(1): e84748. https://doi.org/10.1371/journal.pone.0084748;
Eguchi T, Kubota S, Kawata K, et al. Novel transcription-factor-like function of human matrix metalloproteinase 3 regulating the CTGF/CCN2 gene. Mol Cell Biol. 2008;28(7):2391-2413. doi:10.1128/MCB.01288-07 |
| E.C. number | NA |
| Location of functional site(s) | NA |
| Cellular location of function | nucleus |
| Comments | NA |