MMP15

MMP15
Identifiers
Aliases	MMP15 , MT2-MMP, MTMMP2, SMCP-2, MMP-15, MT2MMP, matrix metallopeptidase 15
External IDs	OMIM: 602261; MGI: 109320; HomoloGene: 20549; GeneCards: MMP15; OMA:MMP15 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) [1] Band 16q21 Start 58,025,754 bp [1] End 58,046,901 bp [1]
Gene location (Mouse) Chr. Chromosome 8 (mouse) [2] Band 8 C5|8 47.12 cM Start 96,078,896 bp [2] End 96,101,708 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon apex of heart right lobe of thyroid gland left lobe of thyroid gland right lobe of liver left ventricle right testis left testis right auricle of heart body of stomach Top expressed in external carotid artery internal carotid artery epithelium of stomach Paneth cell trigeminal ganglion atrium supraoptic nucleus aortic valve conjunctival fornix lumbar spinal ganglion More reference expression data BioGPS n/a
Gene ontology Molecular function zinc ion binding metal ion binding peptidase activity protein binding enzyme activator activity metalloendopeptidase activity hydrolase activity metallopeptidase activity metalloaminopeptidase activity Cellular component integral component of membrane membrane extracellular matrix plasma membrane integral component of plasma membrane extracellular space Biological process response to estradiol endodermal cell differentiation extracellular matrix disassembly collagen catabolic process positive regulation of catalytic activity proteolysis extracellular matrix organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4324 17388 Ensembl ENSG00000102996 ENSMUSG00000031790 UniProt P51511 O54732 RefSeq (mRNA) NM_002428 NM_008609 RefSeq (protein) NP_002419 NP_032635 Location (UCSC) Chr 16: 58.03 – 58.05 Mb Chr 8: 96.08 – 96.1 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Matrix metalloproteinase 15 also known as MMP15 is an enzyme that in humans is encoded by the MMP15 gene. ^{[5] [6]}

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 MMP's are secreted as inactive proenzymes 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; members of this subfamily can be anchored to the extracellular membrane by either a transmembrane domain or glycophosphatidylinositol linkage, suggesting that these proteins are expressed at the cell surface rather than secreted in a soluble form. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000102996 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031790 – 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. Sato H, Tanaka M, Takino T, Inoue M, Seiki M (February 1997). "Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization". Genomics. 39 (3): 412–3. doi:10.1006/geno.1996.4496. PMID   9119382.
6. Mattei MG, Roeckel N, Olsen BR, Apte SS (February 1997). "Genes of the membrane-type matrix metalloproteinase (MT-MMP) gene family, MMP14, MMP15, and MMP16, localize to human chromosomes 14, 16, and 8, respectively". Genomics. 40 (1): 168–9. doi:10.1006/geno.1996.4559. PMID   9070935.
7. "Entrez Gene: MMP15".

Further reading

• Terp GE, Christensen IT, Jørgensen FS (June 2000). "Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes". J. Biomol. Struct. Dyn. 17 (6): 933–46. doi:10.1080/07391102.2000.10506582. PMID   10949161. S2CID   1270176.
• Morrison CJ, Overall CM (2006). "TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains". J. Biol. Chem. 281 (36): 26528–39. doi: 10.1074/jbc.M603331200 . PMID   16825197.
• Takino T, Sato H, Shinagawa A, Seiki M (1995). "Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family". J. Biol. Chem. 270 (39): 23013–20. doi: 10.1074/jbc.270.39.23013 . PMID   7559440.
• Will H, Hinzmann B (1995). "cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment". Eur. J. Biochem. 231 (3): 602–8. doi:10.1111/j.1432-1033.1995.tb20738.x (inactive 5 July 2025). PMID   7649159.
• Lu YG, Zhou HY, Ding LC, et al. (2006). "[Analysis of differential expression genes related to different metastasis potential of adenoid cystic carcinoma using restriction fragments differential display PCR]". Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 23 (5): 505–10. PMID   17029196.
• Rozanov DV, Hahn-Dantona E, Strickland DK, Strongin AY (2004). "The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells". J. Biol. Chem. 279 (6): 4260–8. doi: 10.1074/jbc.M311569200 . PMID   14645246.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• d'Ortho MP, Will H, Atkinson S, et al. (1997). "Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases". Eur. J. Biochem. 250 (3): 751–7. doi:10.1111/j.1432-1033.1997.00751.x. PMID   9461298.
• Buisson-Legendre N, Smith S, March L, Jackson C (2004). "Elevation of activated protein C in synovial joints in rheumatoid arthritis and its correlation with matrix metalloproteinase 2". Arthritis Rheum. 50 (7): 2151–6. doi: 10.1002/art.20313 . PMID   15248212.
• Hotary K, Li XY, Allen E, et al. (2006). "A cancer cell metalloprotease triad regulates the basement membrane transmigration program". Genes Dev. 20 (19): 2673–86. doi:10.1101/gad.1451806. PMC   1578694 . PMID   16983145.
• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi: 10.1074/jbc.274.31.21491 . PMID   10419448.
• 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. S2CID   21596144.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Hitchon CA, Danning CL, Illei GG, et al. (2002). "Gelatinase expression and activity in the synovium and skin of patients with erosive psoriatic arthritis". J. Rheumatol. 29 (1): 107–17. PMID   11824946.
• Sato H, Tanaka M, Takino T, et al. (1997). "Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization". Genomics. 39 (3): 412–3. doi:10.1006/geno.1996.4496. PMID   9119382.

External links

• The MEROPS online database for peptidases and their inhibitors: M10.015

This article incorporates text from the United States National Library of Medicine, which is in the public domain.