MMP19
entrez
4327
canonical
uniprot
Q99542
canonical
ensembl
ENSG00000123342
resolver
ensp
ENSP00000313437
resolver
ensp
ENSP00000386625
resolver
ensp
ENSP00000559598
resolver
genesymbol
MMP19
resolver
genesymbol_syn
MMP18
resolver
genesymbol_syn
RASI
resolver
hgnc
HGNC:7165
resolver
uniprot
B4E030
resolver
uniprot
O15278
resolver
uniprot
O95606
resolver
uniprot
Q99580
resolver
uniprot_entry
MMP19_HUMAN
resolver
uniprot_sec
B4E030
resolver
uniprot_sec
O15278
resolver
uniprot_sec
O95606
resolver
uniprot_sec
Q99580
resolver
activity_regulation
ACTIVITY REGULATION: Strongly inhibited by TIMP-2, TIMP-3 and TIMP-4, while TIMP-1 is less efficient.
uniprot
proteins
amino_acid_sequence
MNCQQLWLGFLLPMTVSGRVLGLAEVAPVDYLSQYGYLQKPLEGSNNFKPEDITEALRAFQEASELPVSGQLDDATRARMRQPRCGLEDPFNQKTLKYLLLGRWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGAADIRLSFHGRQSSYCSNTFDGPGRVLAHADIPELGSVHFDEDEFWTEGTYRGVNLRIIAAHEVGHALGLGHSRYSQALMAPVYEGYRPHFKLHPDDVAGIQALYGKKSPVIRDEEEEETELPTVPPVPTEPSPMPDPCSSELDAMMLGPRGKTYAFKGDYVWTVSDSGPGPLFRVSALWEGLPGNLDAAVYSPRTQWIHFFKGDKVWRYINFKMSPGFPKKLNRVEPNLDAALYWPLNQKVFLFKGSGYWQWDELARTDFSSYPKPIKGLFTGVPNQPSAAMSWQDGRVYFFKGKVYWRLNQQLRVEKGYPRNISHNWMHCRPRTIDTTPSGGNTTPSGTGITLDTTLSATETTFEY
uniprot
proteins
disease_involvement
DISEASE: Cavitary optic disc anomalies (CODA) [MIM:611543]: An ocular disease characterized by a profound excavation of the optic nerve. Clinical phenotype is variable and includes congenitally excavated optic nerves as well as other features of optic pit, optic nerve coloboma, and morning glory disk anomaly. Patients with CODA have a strong predilection for retinal detachment and/or separation of the retinal layers (retinoschisis) that lead to profound central vision loss. {ECO:0000269|PubMed:25581579}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin. {ECO:0000269|PubMed:10809722, ECO:0000269|PubMed:10922468}.
uniprot
proteins
mass_dalton
57357
uniprot
proteins
mutagenesis
MUTAGEN 88; /note="E->P: Reduced autolysis rate."; /evidence="ECO:0000269|PubMed:10809722"; MUTAGEN 90; /note="P->V: Reduced autolysis rate."; /evidence="ECO:0000269|PubMed:10809722
uniprot
proteins
post_translational_modification
PTM: Activated by autolytic cleavage after Lys-97.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000269|PubMed:25171405}.
uniprot
proteins
protein_family
Peptidase M10A family
uniprot
proteins
pubmed
10809722
uniprot
proteins
pubmed
10922468
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
25171405
uniprot
proteins
pubmed
25581579
uniprot
proteins
pubmed
8920941
uniprot
proteins
pubmed
9020145
uniprot
proteins
pubmed
9232430
uniprot
proteins
pubmed
9562866
uniprot
proteins
sequence_length
508
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
uniprot
proteins