General Information |
MoonProt ID | 450 |
First appeared in release | 3.0 |
Name(s) | Matrix metalloproteinase-3, Human |
UniProt ID | P08254 (MMP3_HUMAN) |
GO terms | GO:0004175 endopeptidase activity
GO:0004222 metalloendopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0005576 extracellular region
GO:0005615 extracellular space
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:0019221 cytokine-mediated signaling pathway
GO:0022617 extracellular matrix disassembly
GO:0030198 extracellular matrix organization
GO:0030574 collagen catabolic process
GO:0031012 extracellular matrix
GO:0031334 positive regulation of protein-containing complex assembly
GO:0046872 metal ion binding
GO:0071492 cellular response to UV-A
GO:0071732 cellular response to nitric oxide
GO:0150077 regulation of neuroinflammatory response
GO:1903209 positive regulation of oxidative stress-induced cell death
GO:1904645 response to amyloid-beta |
Organisms for which functions have been demonstrated | Homo sapiens (human, a mammal) |
Sequence length | 477 amino acids |
FASTA sequence | >sp|P08254|MMP3_HUMAN Stromelysin-1 OS=Homo sapiens OX=9606 GN=MMP3 PE=1 SV=2
MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNWLNC |
Structure Information |
PDB ID | 1SLM_A, 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_450_uniID_P08254 is 477 residues long, with 19 residues (3.98%) predicted as disordered.The protein has 1 short (< 30 residues) disorder segment and 0 long (>= 30 residues) disorder segments.
Segment 1 - Short (< 30 residues) disordered segment Segment is located between positions 269 and 287 in the sequence. The segment is 19 residues long (3.98 % of the total sequence length). |
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 | Min KW, Lee SH, Baek SJ. Moonlighting proteins in cancer. Cancer Lett. 2016;370(1):108-116. doi:10.1016/j.canlet.2015.09.022 |
E.C. number | 3.4.24.17 |
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 | nuclear MMP3 proteolysis is a driver of apoptosis
K. Si-Tayeb, A. Monvoisin, C. Mazzocco, S. Lepreux, M. Decossas, G. Cubel, D. Taras, J.F. Blanc, D.R. Robinson, J. Rosenbaum Matrix metalloproteinase 3 is present in the cell nucleus and is involved in apoptosis Am. J. Pathol., 169 (2006), pp. 1390-1401, 10.2353/ajpath.2006.060005; Cancer:
Min KW, Lee SH, Baek SJ. Moonlighting proteins in cancer. Cancer Lett. 2016;370(1):108-116. doi:10.1016/j.canlet.2015.09.022
Coronary heart disease 6 (CHDS6):
Ye S, Eriksson P, Hamsten A, Kurkinen M, Humphries SE, Henney AM. Progression of coronary atherosclerosis is associated with a common genetic variant of the human stromelysin-1 promoter which results in reduced gene expression. J Biol Chem. 1996;271(22):13055-13060. doi:10.1074/jbc.271.22.13055 |