Mmp24
entrez
17391
canonical
uniprot
Q9R0S2
canonical
ensembl
ENSMUSG00000027612
resolver
ensp
ENSMUSP00000029141
resolver
ensp
ENSMUSP00000311864
resolver
enst
ENSMUST00000029141
resolver
genesymbol
Mmp24
resolver
genesymbol_syn
Mmp21
resolver
genesymbol_syn
Mt5mmp
resolver
uniprot
A2AUV7
resolver
uniprot
Q9Z0J9
resolver
uniprot_entry
MMP24_MOUSE
resolver
uniprot_sec
A2AUV7
resolver
uniprot_sec
Q9Z0J9
resolver
amino_acid_sequence
MPRSRGGRAAPGQASRWSGWRAPGRLLPLLPALCCLAAAAGAGKPAGADAPFAGQNWLKSYGYLLPYESRASALHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWMKKPRCGVPDHPHLSRRRRNKRYALTGQKWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEIKSDRKEADIMIFFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQGIQKIYGPPAEPLEPTRPLPTLPVRRIHSPSERKHERHPRPPRPPLGDRPSTPGAKPNICDGNFNTVALFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLPARIDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPKPITVWKGIPQAPQGAFISKEGYYTYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGCKQKEVERRKERRLPQDDVDIMVTIDDVPGSVNAVAVVVPCTLSLCLLVLLYTIFQFKNKAGPQPVTYYKRPVQEWV
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence (PubMed:19805319, PubMed:24952463). Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia (PubMed:19805319). Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence (PubMed:24952463). May play a role in axonal growth (PubMed:11714638). Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (PubMed:10622708). {ECO:0000269|PubMed:10622708, ECO:0000269|PubMed:11714638, ECO:0000269|PubMed:19805319, ECO:0000269|PubMed:24952463}.
uniprot
proteins
mass_dalton
70460
uniprot
proteins
mutagenesis
MUTAGEN 256; /note="E->A: Loss of function. Does not prevent proteolytic processing."; /evidence="ECO:0000269|PubMed:10085137, ECO:0000269|PubMed:11470782"; MUTAGEN 549..554; /note="Missing: Abolishes proteolytic processing. Gain of function mutant."; MUTAGEN 616..618; /note="Missing: Impaired recycling affecting its internalization, leading to decreased activity on the plasma surface."; /evidence="ECO:0000269|PubMed:14990567
uniprot
proteins
post_translational_modification
PTM: Cleaved by a furin endopeptidase in the trans-Golgi network.
uniprot
proteins
protein_family
Peptidase M10A family
uniprot
proteins
pubmed
10085137
uniprot
proteins
pubmed
10622708
uniprot
proteins
pubmed
11470782
uniprot
proteins
pubmed
11714638
uniprot
proteins
pubmed
14990567
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19805319
uniprot
proteins
pubmed
24952463
uniprot
proteins
sequence_length
618
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Matrix metalloproteinase-24]: Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3. {ECO:0000269|PubMed:14990567}.; SUBCELLULAR LOCATION: [Processed matrix metalloproteinase-24]: Secreted, extracellular space, extracellular matrix. Note=Also shed from cell surface as soluble proteinase, by a proteolytic cleavage. {ECO:0000269|PubMed:11470782}.
uniprot
proteins
transmembrane_region
TRANSMEM 576..596; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins