Mmp13
entrez
17386
canonical
uniprot
P33435
canonical
ensembl
ENSMUSG00000050578
resolver
ensp
ENSMUSP00000015394
resolver
enst
ENSMUST00000015394
resolver
genesymbol
Mmp13
resolver
uniprot
Q3U9V5
resolver
uniprot_entry
MMP13_MOUSE
resolver
uniprot_entry
Q3U9V5_MOUSE
resolver
amino_acid_sequence
MHSAILATFFLLSWTPCWSLPLPYGDDDDDDLSEEDLVFAEHYLKSYYHPATLAGILKKSTVTSTVDRLREMQSFFGLEVTGKLDDPTLDIMRKPRCGVPDVGEYNVFPRTLKWSQTNLTYRIVNYTPDMSHSEVEKAFRKAFKVWSDVTPLNFTRIYDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQFLYGPGDEDPNPKHPKTPEKCDPALSLDAITSLRGETMIFKDRFFWRLHPQQVEAELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGYDILEGYPRKISDLGFPKEVKRLSAAVHFENTGKTLFFSENHVWSYDDVNQTMDKDYPRLIEEEFPGIGNKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSILWC
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion. {ECO:0000269|PubMed:15539485, ECO:0000269|PubMed:15563592, ECO:0000269|PubMed:17987127, ECO:0000269|PubMed:19590036, ECO:0000269|PubMed:22880047}.
uniprot
proteins
mass_dalton
54182
uniprot
proteins
post_translational_modification
PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro) (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P45452}.
uniprot
proteins
protein_family
Peptidase M10A family
uniprot
proteins
pubmed
10525409
uniprot
proteins
pubmed
1383028
uniprot
proteins
pubmed
15539485
uniprot
proteins
pubmed
15563592
uniprot
proteins
pubmed
17987127
uniprot
proteins
pubmed
19590036
uniprot
proteins
pubmed
22880047
uniprot
proteins
sequence_length
472
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted.
uniprot
proteins