ADAM19

ADAM19 (A Disintegrin And Metalloproteinase 19, MADDAM, meltrin beta), is a human gene.[5]

ADAM19
Identifiers
Aliases	ADAM19, MADDAM, MLTNB, FKSG34, ADAM metallopeptidase domain 19
External IDs	OMIM: 603640 MGI: 105377 HomoloGene: 74925 GeneCards: ADAM19
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q33.3 Start 157,395,534 bp[1] End 157,575,775 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 B1.1|11 27.54 cM Start 46,055,992 bp[2] End 46,147,343 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • SH3 domain binding • peptidase activity • metalloendopeptidase activity • metallopeptidase activity • hydrolase activity • metal ion binding • GO:0001948 protein binding Cellular component • integral component of membrane • Golgi apparatus • membrane • cell membrane • cell nucleus • collagen-containing extracellular matrix Biological process • heart development • membrane protein ectodomain proteolysis • proteolysis • extracellular matrix organization • placentation • positive regulation of gene expression • positive regulation of cell-cell adhesion mediated by cadherin Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8728	11492
Ensembl	ENSG00000135074	ENSMUSG00000011256
UniProt	Q9H013	O35674
RefSeq (mRNA)	NM_023038 NM_033274	NM_001291890 NM_001291891 NM_009616 NM_001311209
RefSeq (protein)	NP_150377	NP_001278819 NP_001278820 NP_001298138 NP_033746
Location (UCSC)	Chr 5: 157.4 – 157.58 Mb	Chr 11: 46.06 – 46.15 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[5]

Interactions

ADAM19 has been shown to interact with ABI2.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000135074 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000011256 - 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. "Entrez Gene: ADAM19 ADAM metallopeptidase domain 19 (meltrin beta)".
6. Huang L, Feng L, Yang L, Zhou W, Zhao S, Li C (Sep 2002). "Screen and identification of proteins interacting with ADAM19 cytoplasmic tail". Molecular Biology Reports. 29 (3): 317–23. doi:10.1023/A:1020409217215. PMID 12463424.

External links

• Human ADAM19 genome location and ADAM19 gene details page in the UCSC Genome Browser.

Further reading

• Adams MD, Kerlavage AR, Fields C, Venter JC (Jul 1993). "3,400 new expressed sequence tags identify diversity of transcripts in human brain". Nature Genetics. 4 (3): 256–67. doi:10.1038/ng0793-256. PMID 8358434.
• Inoue D, Reid M, Lum L, Krätzschmar J, Weskamp G, Myung YM, Baron R, Blobel CP (Feb 1998). "Cloning and initial characterization of mouse meltrin beta and analysis of the expression of four metalloprotease-disintegrins in bone cells". The Journal of Biological Chemistry. 273 (7): 4180–7. doi:10.1074/jbc.273.7.4180. PMID 9461614.
• Hirohata S, Seldin MF, Apte SS (Nov 1998). "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. doi:10.1006/geno.1998.5544. PMID 9806848.
• Fritsche J, Moser M, Faust S, Peuker A, Büttner R, Andreesen R, Kreutz M (Jul 2000). "Molecular cloning and characterization of a human metalloprotease disintegrin--a novel marker for dendritic cell differentiation". Blood. 96 (2): 732–9. doi:10.1182/blood.V96.2.732. PMID 10887142.
• Shirakabe K, Wakatsuki S, Kurisaki T, Fujisawa-Sehara A (Mar 2001). "Roles of Meltrin beta /ADAM19 in the processing of neuregulin". The Journal of Biological Chemistry. 276 (12): 9352–8. doi:10.1074/jbc.M007913200. PMID 11116142.
• Wei P, Zhao YG, Zhuang L, Ruben S, Sang QX (Jan 2001). "Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/meltrin beta". Biochemical and Biophysical Research Communications. 280 (3): 744–55. doi:10.1006/bbrc.2000.4200. PMID 11162584.
• Zhao YG, Wei P, Sang QX (Nov 2001). "Inhibitory antibodies against endopeptidase activity of human adamalysin 19". Biochemical and Biophysical Research Communications. 289 (1): 288–94. doi:10.1006/bbrc.2001.5958. PMID 11708814.
• Kang T, Zhao YG, Pei D, Sucic JF, Sang QX (Jul 2002). "Intracellular activation of human adamalysin 19/disintegrin and metalloproteinase 19 by furin occurs via one of the two consecutive recognition sites". The Journal of Biological Chemistry. 277 (28): 25583–91. doi:10.1074/jbc.M203532200. PMID 12006600.
• Díaz-Rodríguez E, Montero JC, Esparís-Ogando A, Yuste L, Pandiella A (Jun 2002). "Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding". Molecular Biology of the Cell. 13 (6): 2031–44. doi:10.1091/mbc.01-11-0561. PMC 117622. PMID 12058067.
• Kang T, Park HI, Suh Y, Zhao YG, Tschesche H, Sang QX (Dec 2002). "Autolytic processing at Glu586-Ser587 within the cysteine-rich domain of human adamalysin 19/disintegrin-metalloproteinase 19 is necessary for its proteolytic activity". The Journal of Biological Chemistry. 277 (50): 48514–22. doi:10.1074/jbc.M208961200. PMID 12393862.
• Huang L, Feng L, Yang L, Zhou W, Zhao S, Li C (Sep 2002). "Screen and identification of proteins interacting with ADAM19 cytoplasmic tail". Molecular Biology Reports. 29 (3): 317–23. doi:10.1023/A:1020409217215. PMID 12463424.
• Abram CL, Seals DF, Pass I, Salinsky D, Maurer L, Roth TM, Courtneidge SA (May 2003). "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells". The Journal of Biological Chemistry. 278 (19): 16844–51. doi:10.1074/jbc.M300267200. PMID 12615925.
• Chesneau V, Becherer JD, Zheng Y, Erdjument-Bromage H, Tempst P, Blobel CP (Jun 2003). "Catalytic properties of ADAM19". The Journal of Biological Chemistry. 278 (25): 22331–40. doi:10.1074/jbc.M302781200. PMID 12682046.
• Kang T, Tschesche H, Amy Sang QX (Aug 2004). "Evidence for disulfide involvement in the regulation of intramolecular autolytic processing by human adamalysin19/ADAM19". Experimental Cell Research. 298 (1): 285–95. doi:10.1016/j.yexcr.2004.04.022. PMID 15242783.
• Ehrnsperger A, Rehli M, Thu-Hang P, Kreutz M (Jul 2005). "Epigenetic regulation of the dendritic cell-marker gene ADAM19". Biochemical and Biophysical Research Communications. 332 (2): 456–64. doi:10.1016/j.bbrc.2005.04.149. PMID 15896713.
• Melenhorst WB, van den Heuvel MC, Stegeman CA, van der Leij J, Huitema S, van den Berg A, van Goor H (Jul 2006). "Upregulation of ADAM19 in chronic allograft nephropathy". American Journal of Transplantation. 6 (7): 1673–81. doi:10.1111/j.1600-6143.2006.01384.x. PMID 16827870.
• Tanabe C, Hotoda N, Sasagawa N, Sehara-Fujisawa A, Maruyama K, Ishiura S (Jan 2007). "ADAM19 is tightly associated with constitutive Alzheimer's disease APP alpha-secretase in A172 cells". Biochemical and Biophysical Research Communications. 352 (1): 111–7. doi:10.1016/j.bbrc.2006.10.181. PMID 17112471.