MMP24

Matrix metalloproteinase-24 is an enzyme that in humans is encoded by the MMP24 gene.[5][6]

MMP24
Identifiers
Aliases	MMP24, MMP-24, MMP25, MT-MMP 5, MT-MMP5, MT5-MMP, MT5MMP, MTMMP5, matrix metallopeptidase 24
External IDs	OMIM: 604871 MGI: 1341867 HomoloGene: 21331 GeneCards: MMP24
Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20q11.22 Start 35,226,690 bp[1] End 35,276,998 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2 H1|2 77.26 cM Start 155,775,342 bp[2] End 155,818,366 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • zinc ion binding • cadherin binding • metal ion binding • peptidase activity • GO:0010577 enzyme activator activity • metalloendopeptidase activity • hydrolase activity • metallopeptidase activity Cellular component • integral component of membrane • Golgi apparatus • trans-Golgi network membrane • membrane • extracellular matrix • cell membrane • integral component of plasma membrane • extracellular region • extracellular exosome • extracellular Biological process • glial cell differentiation • proteolysis • detection of temperature stimulus involved in sensory perception of pain • neuronal stem cell population maintenance • cell-cell adhesion mediated by cadherin • cell adhesion • GO:0048554 positive regulation of catalytic activity • cell-cell adhesion via plasma-membrane adhesion molecules • extracellular matrix organization • collagen catabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10893	17391
Ensembl	ENSG00000125966	ENSMUSG00000027612
UniProt	Q9Y5R2	Q9R0S2
RefSeq (mRNA)	NM_006690	NM_010808
RefSeq (protein)	NP_006681	NP_034938
Location (UCSC)	Chr 20: 35.23 – 35.28 Mb	Chr 2: 155.78 – 155.82 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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 MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 by cleavage. The gene has previously been referred to as MMP25 but has been renamed MMP24.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000125966 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027612 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Llano E, Pendas AM, Freije JP, Nakano A, Knauper V, Murphy G, Lopez-Otin C (Jun 1999). "Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors". Cancer Res. 59 (11): 2570–6. PMID 10363975.
6. "Entrez Gene: MMP24 matrix metallopeptidase 24 (membrane-inserted)".

Further reading

• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
• Kinoh H, Hayashita H, Kajita M, et al. (2000). "Assignment of the genes for membrane-type-4 matrix metalloproteinase (Mmp17, MMP17) to mouse chromosome 5, human chromosome band 12q24.3 and membrane-type-5 matrix metalloproteinase (Mmp24, MMP24) to mouse chromosome 2 and human chromosome band 20q11.2→q12, respectively, by radiation hybrid and in situ hybridization". Cytogenet. Cell Genet. 87 (1–2): 97–8. doi:10.1159/000015402. PMID 10640822. S2CID 24060884.
• Romanic AM, Burns-Kurtis CL, Ao Z, et al. (2001). "Upregulated expression of human membrane type-5 matrix metalloproteinase in kidneys from diabetic patients". Am. J. Physiol. Renal Physiol. 281 (2): F309–17. doi:10.1152/ajprenal.2001.281.2.F309. PMID 11457723.
• Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Jung M, Römer A, Keyszer G, et al. (2003). "mRNA expression of the five membrane-type matrix metalloproteinases MT1-MT5 in human prostatic cell lines and their down-regulation in human malignant prostatic tissue". Prostate. 55 (2): 89–98. doi:10.1002/pros.10194. PMID 12661033.
• Takino T, Koshikawa N, Miyamori H, et al. (2003). "Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases". Oncogene. 22 (30): 4617–26. doi:10.1038/sj.onc.1206542. hdl:2297/2668. PMID 12879005. S2CID 10007952.
• Wang P, Wang X, Pei D (2004). "Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV". J. Biol. Chem. 279 (19): 20461–70. doi:10.1074/jbc.M400264200. PMID 14990567.
• Gaetje R, Holtrich U, Engels K, et al. (2008). "Expression of membrane-type 5 matrix metalloproteinase in human endometrium and endometriosis". Gynecol. Endocrinol. 23 (10): 567–73. doi:10.1080/09513590701556921. PMID 17952761. S2CID 25621136.