External links
- ZMPSTE24+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |
| zinc metalloproteinase STE24 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | ZMPSTE24 | ||||||
| Alt. symbols | FACE1, STE24, FACE-1, Ste24p, FLJ14968 | ||||||
| NCBI gene | 10269 | ||||||
| HGNC | 12877 | ||||||
| OMIM | 606480 | ||||||
| RefSeq | NM_005857 | ||||||
| UniProt | O75844 | ||||||
| Other data | |||||||
| Locus | Chr. 1 p34 | ||||||
| |||||||
Zinc metalloproteinase STE24 is a metalloproteinase enzyme associated with laminopathies.
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Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases; other family members are adamalysins, serralysins, and astacins. The MMPs belong to a larger family of proteases known as the metzincin superfamily.
A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example of this would be ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis.
ADAMs are a family of single-pass transmembrane and secreted metalloendopeptidases. All ADAMs are characterized by a particular domain organization featuring a pro-domain, a metalloprotease, a disintegrin, a cysteine-rich, an epidermal-growth factor like and a transmembrane domain, as well as a C-terminal cytoplasmic tail. Nonetheless, not all human ADAMs have a functional protease domain, which indicates that their biological function mainly depends on protein–protein interactions. Those ADAMs which are active proteases are classified as sheddases because they cut off or shed extracellular portions of transmembrane proteins. For example, ADAM10 can cut off part of the HER2 receptor, thereby activating it. ADAM genes are found in animals, choanoflagellates, fungi and some groups of green algae. Most green algae and all land plants likely lost ADAM proteins.
72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene. The MMP2 gene is located on chromosome 16 at position 12.2.
Matrix metalloproteinase-1 (MMP-1) also known as interstitial collagenase and fibroblast collagenase is an enzyme that in humans is encoded by the MMP1 gene. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP-1 was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA. MMP-1 has an estimated molecular weight of 54 kDa.
Stromelysin-1 also known as matrix metalloproteinase-3 (MMP-3) is an enzyme that in humans is encoded by the MMP3 gene. The MMP3 gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP-3 has an estimated molecular weight of 54 kDa.
Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene. The enzyme has also been known as matrin, putative metalloproteinase-1, matrix metalloproteinase pump 1, PUMP-1 proteinase, PUMP, metalloproteinase pump-1, putative metalloproteinase, MMP). Human MMP-7 has a molecular weight around 30 kDa.
Stromelysin-2 also known as matrix metalloproteinase-10 (MMP-10) or transin-2 is an enzyme that in humans is encoded by the MMP10 gene.
Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene. It is a member of the matrix metalloproteinase (MMP) family. Like most MMPs, it is secreted as an inactive pro-form. MMP-13 has an predicted molecular weight around 54 kDa. It is activated once the pro-domain is cleaved, leaving an active enzyme composed of the catalytic domain and the hemopexin-like domain PDB: 1PEX. Although the actual mechanism has not been described, the hemopexin domain participates in collagen degradation, the catalytic domain alone being particularly inefficient in collagen degradation. During embryonic development, MMP-13 is expressed in the skeleton as required for restructuring the collagen matrix for bone mineralization. In pathological situations it is highly overexpressed; this occurs in human carcinomas, rheumatoid arthritis and osteoarthritis.
Matrix metalloproteinase-12 (MMP-12) also known as macrophage metalloelastase (MME) or macrophage elastase (ME) is an enzyme that in humans is encoded by the MMP12 gene.
Matrix metalloproteinase-26 also known as matrilysin-2 and endometase is an enzyme that in humans is encoded by the MMP26 gene.
Matrix metalloproteinase-19 (MMP-19) also known as matrix metalloproteinase RASI is an enzyme that in humans is encoded by the MMP19 gene.
Matrix metalloproteinase-16 is an enzyme that in humans is encoded by the MMP16 gene.
Matrix metalloproteinase-17 (MMP-17) also known as membrane-type matrix metalloproteinase 4 is an enzyme that in humans is encoded by the MMP17 gene.
Matrix metalloproteinase-25 is an enzyme that in humans is encoded by the MMP25 gene.
Matrix metalloproteinase-24 is an enzyme that in humans is encoded by the MMP24 gene.
Matrix metalloproteinase-20 (MMP-20) also known as enamel metalloproteinase or enamelysin is an enzyme that in humans is encoded by the MMP20 gene.
Matrix metalloproteinase-21 (MMP-21) is an enzyme that in humans is encoded by the MMP21 gene.
Matrix metallopeptidase 27 also known as MMP-27 is an enzyme which in humans is encoded by the MMP27 gene.
Matrix metalloproteinase 15 also known as MMP15 is an enzyme that in humans is encoded by the MMP15 gene.