MMP11

Stromelysin-3 (SL-3) also known as matrix metalloproteinase-11 (MMP-11) is an enzyme that in humans is encoded by the MMP11 gene.^[4][5][6][7]

MMP11
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1HV5
Identifiers
Aliases	MMP11, SL-3, ST3, STMY3, matrix metallopeptidase 11
External IDs	OMIM: 185261; MGI: 97008; HomoloGene: 38116; GeneCards: MMP11; OMA:MMP11 - orthologs
Gene location (Mouse) Chr. Chromosome 10 (mouse)[1] Band 10 C1|10 38.62 cM Start 75,759,056 bp[1] End 75,772,330 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium canal of the cervix right uterine tube smooth muscle tissue gallbladder left ventricle ganglionic eminence right coronary artery left uterine tube rectum Top expressed in genital tubercle Gonadal ridge external carotid artery cervix ankle joint internal carotid artery ovary vas deferens tail of embryo ascending aorta More reference expression data BioGPS More reference expression data
Gene ontology Molecular function zinc ion binding peptidase activity metalloendopeptidase activity hydrolase activity metallopeptidase activity metal ion binding serine-type endopeptidase activity Cellular component Golgi lumen extracellular region extracellular matrix extracellular space Biological process collagen catabolic process multicellular organism development negative regulation of fat cell differentiation extracellular matrix disassembly proteolysis collagen fibril organization basement membrane organization extracellular matrix organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4320 17385 Ensembl n/a ENSMUSG00000000901 UniProt P24347 Q02853 RefSeq (mRNA) NM_005940 NM_008606 NM_001306184 RefSeq (protein) NP_005931 NP_005931.2 NP_001293113 NP_032632 Location (UCSC) n/a Chr 10: 75.76 – 75.77 Mb PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Function

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMPs, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.^[7]