P03957
uniprot
P03957
canonical
activity_regulation
ACTIVITY REGULATION: Inhibited by a synthetic peptide corresponding to the inhibitory cysteine switch motif (PubMed:1988438). Inhibited by ethylenediaminetetraacetic acid (EDTA), 1,10-pheanthroline, 2-mecaptoethanol, dithiothreitol and metalloproteinase inhibitor protein TIMP (PubMed:1963430, PubMed:2841336). {ECO:0000269|PubMed:1963430, ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336}.
uniprot
proteins
amino_acid_sequence
MKGLPVLLWLCTAVCSSYPLHGSEEDAGMEVLQKYLENYYGLEKDVKQFTKKKDSSPVVKKIQEMQKFLGLKMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKNHISYRIVNYTLDLPRESVDSAIERALKVWEEVTPLTFSRISEGEADIMISFAVEEHGDFIPFDGPGMVLAHAYAPGPGTNGDAHFDDDERWTDDVTGTNLFLVAAHELGHSLGLFHSANAEALMYPVYKSSTDLARFHLSQDDVDGIQSLYGPPTESPDVLVVPTKSNSLDPETLPMCSSALSFDAVSTLRGEVLFFKDRHFWRKSLRTPEPGFYLISSFWPSLPSNMDAAYEVTNRDTVFILKGNQIWAIRGHEELAGYPKSIHTLGLPETVQKIDAAISLKDQKKTYFFVEDKFWRFDEKKQSMDPEFPRKIAENFPGIGTKVDAVFEAFGFLYFFSGSSQLEFDPNAGKVTHILKSNSWFNC
uniprot
proteins
ec_number
3.4.24.17
uniprot
proteins
function
FUNCTION: Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. {ECO:0000269|PubMed:1963430}.; 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. Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway. Also acts intracellularly. 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. In addition, plays a role in immune response and possesses antiviral activity against various viruses. Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities. {ECO:0000250|UniProtKB:P08254}.
uniprot
proteins
mass_dalton
53428
uniprot
proteins
mutagenesis
MUTAGEN 85; /note="M->L: Does not induce autoproteolytic activation."; /evidence="ECO:0000269|PubMed:1988438"; MUTAGEN 88; /note="P->A: Does not induce autoproteolytic activation."; /evidence="ECO:0000269|PubMed:1988438"; MUTAGEN 88; /note="P->G,L: Induces partial autoproteolytic activation."; /evidence="ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336"; MUTAGEN 89; /note="R->K,L,Q: Induces constitutive autoproteolytic activation."; /evidence="ECO:0000269|PubMed:1988438"; MUTAGEN 90; /note="C->S,H,D: Induces constitutive autoproteolytic activation."; /evidence="ECO:0000269|PubMed:1988438"; MUTAGEN 91; /note="G->A: Induces constitutive autoproteolytic activation."; /evidence="ECO:0000269|PubMed:1988438"; MUTAGEN 92; /note="V->G: Induces constitutive autoproteolytic activation."; /evidence="ECO:0000269|PubMed:1988438"; MUTAGEN 92; /note="V->I,A: Induces partial autoproteolytic activation."; /evidence="ECO:0000269|PubMed:1988438"; MUTAGEN 92; /note="V->L,D: Does not induce autoproteolytic activation."; /evidence="ECO:0000269|PubMed:1988438"; MUTAGEN 93; /note="P->V,G,N: Induces partial autoproteolytic activation."; /evidence="ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336"; MUTAGEN 98; /note="F->S: Loss of autocleavage without affecting activation by APMA."; /evidence="ECO:0000269|PubMed:2841336"; MUTAGEN 216; /note="H->L: Loss of autoproteolytic activation and catalytic activity."; /evidence="ECO:0000269|PubMed:2841336"; MUTAGEN 217; /note="E->G: Loss of autoproteolytic activation and catalytic activity."; /evidence="ECO:0000269|PubMed:2841336"; MUTAGEN 226; /note="H->S: Loss of autoproteolytic activation and catalytic activity."; /evidence="ECO:0000269|PubMed:2841336
uniprot
proteins
protein_family
Peptidase M10A family
uniprot
proteins
pubmed
1963430
uniprot
proteins
pubmed
1988438
uniprot
proteins
pubmed
2431284
uniprot
proteins
pubmed
2841336
uniprot
proteins
pubmed
3875482
uniprot
proteins
sequence_length
475
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:1963430, ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336}.
uniprot
proteins