ADAM19

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ADAM metallopeptidase domain 19 (meltrin beta)
Identifiers
Symbol(s) ADAM19; FKSG34; MADDAM; MLTNB
External IDs OMIM: 603640 MGI105377 Homologene74925
RNA expression pattern

PBB GE ADAM19 209765 at tn.png

More reference expression data

Orthologs
Human Mouse
Entrez 8728 11492
Ensembl ENSG00000135074 ENSMUSG00000011256
Uniprot Q9H013 Q3UH67
Refseq NM_023038 (mRNA)
NP_075525 (protein)
XM_981888 (mRNA)
XP_986982 (protein)
Location Chr 5: 156.84 - 156.94 Mb Chr 11: 45.9 - 45.99 Mb
Pubmed search [1] [2]

ADAM metallopeptidase domain 19 (meltrin beta), also known as ADAM19, is a human gene.[1]


This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. This member is a type I transmembrane protein and serves as a marker for dendritic cell differentiation. It has also been demonstrated to be an active metalloproteinase, which may be involved in normal physiological and pathological processes such as cells migration, cell adhesion, cell-cell and cell-matrix interactions, and signal transduction. Alternative splicing results in two transcript variants.[1]


References

Further reading

  • Adams MD, Kerlavage AR, Fields C, Venter JC (1993). "3,400 new expressed sequence tags identify diversity of transcripts in human brain.". Nat. Genet. 4 (3): 256–67. PMID 8358434. doi:10.1038/ng0793-256. 
  • Inoue D, Reid M, Lum L; et al. (1998). "Cloning and initial characterization of mouse meltrin beta and analysis of the expression of four metalloprotease-disintegrins in bone cells.". J. Biol. Chem. 273 (7): 4180–7. PMID 9461614. 
  • Hirohata S, Seldin MF, Apte SS (1999). "Chromosomal assignment of two ADAM genes, TACE (ADAM17) and MLTNB (ADAM19), to human chromosomes 2 and 5, respectively, and of Mltnb to mouse chromosome 11.". Genomics. 54 (1): 178–9. PMID 9806848. doi:10.1006/geno.1998.5544. 
  • Fritsche J, Moser M, Faust S; et al. (2000). "Molecular cloning and characterization of a human metalloprotease disintegrin--a novel marker for dendritic cell differentiation.". Blood. 96 (2): 732–9. PMID 10887142. 
  • Shirakabe K, Wakatsuki S, Kurisaki T, Fujisawa-Sehara A (2001). "Roles of Meltrin beta /ADAM19 in the processing of neuregulin.". J. Biol. Chem. 276 (12): 9352–8. PMID 11116142. doi:10.1074/jbc.M007913200. 
  • Wei P, Zhao YG, Zhuang L; et al. (2001). "Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/meltrin beta.". Biochem. Biophys. Res. Commun. 280 (3): 744–55. PMID 11162584. doi:10.1006/bbrc.2000.4200. 
  • Zhao YG, Wei P, Sang QX (2001). "Inhibitory antibodies against endopeptidase activity of human adamalysin 19.". Biochem. Biophys. Res. Commun. 289 (1): 288–94. PMID 11708814. doi:10.1006/bbrc.2001.5958. 
  • Kang T, Zhao YG, Pei D; et al. (2002). "Intracellular activation of human adamalysin 19/disintegrin and metalloproteinase 19 by furin occurs via one of the two consecutive recognition sites.". J. Biol. Chem. 277 (28): 25583–91. PMID 12006600. doi:10.1074/jbc.M203532200. 
  • Díaz-Rodríguez E, Montero JC, Esparís-Ogando A; et al. (2002). "Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding.". Mol. Biol. Cell. 13 (6): 2031–44. PMID 12058067. doi:10.1091/mbc.01-11-0561. 
  • Kang T, Park HI, Suh Y; et al. (2003). "Autolytic processing at Glu586-Ser587 within the cysteine-rich domain of human adamalysin 19/disintegrin-metalloproteinase 19 is necessary for its proteolytic activity.". J. Biol. Chem. 277 (50): 48514–22. PMID 12393862. doi:10.1074/jbc.M208961200. 
  • Huang L, Feng L, Yang L; et al. (2003). "Screen and identification of proteins interacting with ADAM19 cytoplasmic tail.". Mol. Biol. Rep. 29 (3): 317–23. PMID 12463424. 
  • 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. PMID 12477932. doi:10.1073/pnas.242603899. 
  • Abram CL, Seals DF, Pass I; et al. (2003). "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells.". J. Biol. Chem. 278 (19): 16844–51. PMID 12615925. doi:10.1074/jbc.M300267200. 
  • Chesneau V, Becherer JD, Zheng Y; et al. (2003). "Catalytic properties of ADAM19.". J. Biol. Chem. 278 (25): 22331–40. PMID 12682046. doi:10.1074/jbc.M302781200. 
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. PMID 14702039. doi:10.1038/ng1285. 
  • Kang T, Tschesche H, Amy Sang QX (2004). "Evidence for disulfide involvement in the regulation of intramolecular autolytic processing by human adamalysin19/ADAM19.". Exp. Cell Res. 298 (1): 285–95. PMID 15242783. doi:10.1016/j.yexcr.2004.04.022. 
  • Ehrnsperger A, Rehli M, Thu-Hang P, Kreutz M (2005). "Epigenetic regulation of the dendritic cell-marker gene ADAM19.". Biochem. Biophys. Res. Commun. 332 (2): 456–64. PMID 15896713. doi:10.1016/j.bbrc.2005.04.149. 
  • Melenhorst WB, van den Heuvel MC, Stegeman CA; et al. (2006). "Upregulation of ADAM19 in chronic allograft nephropathy.". Am. J. Transplant. 6 (7): 1673–81. PMID 16827870. doi:10.1111/j.1600-6143.2006.01384.x. 
  • Tanabe C, Hotoda N, Sasagawa N; et al. (2007). "ADAM19 is tightly associated with constitutive Alzheimer's disease APP alpha-secretase in A172 cells.". Biochem. Biophys. Res. Commun. 352 (1): 111–7. PMID 17112471. doi:10.1016/j.bbrc.2006.10.181. 
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