Mmp14
entrez
17387
canonical
uniprot
P53690
canonical
ensembl
ENSMUSG00000000957
resolver
ensp
ENSMUSP00000087119
resolver
enst
ENSMUST00000089688
resolver
genesymbol
Mmp14
resolver
genesymbol_syn
Mtmmp
resolver
uniprot
O08645
resolver
uniprot
O35369
resolver
uniprot
Q8BTX2
resolver
uniprot_entry
MMP14_MOUSE
resolver
uniprot_sec
O08645
resolver
uniprot_sec
O35369
resolver
uniprot_sec
Q8BTX2
resolver
amino_acid_sequence
MSPAPRPSRSLLLPLLTLGTALASLGWAQGSNFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADLATMMAMRRPRCGVPDKFGTEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMILFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVQNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGSKSGSPTKMPPQPRTTSRPSVPDKPKNPAYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEEFRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGSGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPKRLLYCQRSLLDKV
uniprot
proteins
ec_number
3.4.24.80
uniprot
proteins
function
FUNCTION: Endopeptidase that degrades various components of the extracellular matrix such as collagen (PubMed:10520996, PubMed:10737763). Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (PubMed:10520996, PubMed:10737763). Activates progelatinase A/MMP2, thereby acting as a positive regulator of cell growth and migration (PubMed:10737763). Involved in the formation of the fibrovascular tissues in association with pro-MMP2 (By similarity). May be involved in actin cytoskeleton reorganization by cleaving PTK7 (By similarity). Acts as a regulator of Notch signaling by mediating cleavage and inhibition of DLL1 (By similarity). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (By similarity). Acts as a negative regulator of the GDF15-GFRAL aversive response by mediating cleavage and inactivation of GFRAL (PubMed:35177851). {ECO:0000250|UniProtKB:P50281, ECO:0000269|PubMed:10520996, ECO:0000269|PubMed:10737763, ECO:0000269|PubMed:35177851}.
uniprot
proteins
mass_dalton
65919
uniprot
proteins
post_translational_modification
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250|UniProtKB:P50281}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P50281}.
uniprot
proteins
protein_family
Peptidase M10A family
uniprot
proteins
pubmed
10520996
uniprot
proteins
pubmed
10737763
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16778201
uniprot
proteins
pubmed
35177851
uniprot
proteins
pubmed
7708715
uniprot
proteins
pubmed
9325265
uniprot
proteins
pubmed
9648071
uniprot
proteins
sequence_length
582
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P50281}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P50281}. Melanosome {ECO:0000250|UniProtKB:P50281}. Cytoplasm {ECO:0000250|UniProtKB:P50281}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm. {ECO:0000250|UniProtKB:P50281}.
uniprot
proteins
transmembrane_region
TRANSMEM 542..562; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins