Protein Information

General Information
MoonProt ID450
First appeared in release3.0
Name(s)Matrix metalloproteinase-3, Human
UniProt IDP08254 (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 demonstratedHomo sapiens (human, a mammal)
Sequence length477 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 ID1SLM_A, 1SU3_A
Quaternary structureNA
SCOPNA
CATHNA
TM Helix Predictionno TM helices
DisProt AnnotationNot in DisProt
Predicted Disorder RegionsUse 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 descriptionMetalloprotease (degrades fibronectin, gelatin, proteoglycans, denatured type I collagen, laminin, and other extracellular matrix components)
References for functionMin 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. number3.4.24.17
Location of functional site(s)NA
Cellular location of functioncell surface
CommentsNA
Function 2
Function descriptiontranscription factor
References for functionSi-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. numberNA
Location of functional site(s)NA
Cellular location of functionnucleus
Commentsnuclear 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