ADAM19

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)
End	157,575,775 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	46,038,170 bp
RNA expression pattern
	Top expressed in
	oocyte; ; stromal cell of endometrium; ; blood; ; secondary oocyte; ; sural nerve; ; appendix; ; saphenous vein; ; lymph node; ; placenta; ; bone marrow cells;
	Top expressed in
	atrium; ; facial motor nucleus; ; endocardial cushion; ; ascending aorta; ; trigeminal ganglion; ; left lung; ; aortic valve; ; left lung lobe; ; motor neuron; ; belly cord;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	SH3 domain binding ; peptidase activity ; metalloendopeptidase activity ; metallopeptidase activity ; hydrolase activity ; metal ion binding ; protein binding ;
Cellular component	integral component of membrane ; Golgi apparatus ; membrane ; plasma membrane ; nucleus ; collagen-containing extracellular matrix ;
Biological process	heart development ; membrane protein ectodomain proteolysis ; proteolysis ; extracellular matrix organization ; placenta development ; positive regulation of gene expression ; positive regulation of cell-cell adhesion mediated by cadherin ;
	Sources:Amigo / QuickGO
Orthologs
	8728
	11492
	ENSG00000135074
	ENSMUSG00000011256
	Q9H013
	O35674
	NM_023038 ; NM_033274
	NM_001291890 ; NM_001291891 ; NM_009616 ; NM_001311209
	NP_150377
	NP_001278819 ; NP_001278820 ; NP_001298138 ; NP_033746
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated November 13, 2023

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

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]

Related Research Articles

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.

A disintegrin and metalloprotease 17 (ADAM17), also called TACE, is a 70-kDa enzyme that belongs to the ADAM protein family of disintegrins and metalloproteases.

<span class="mw-page-title-main">ADAMTS4</span> Protein-coding gene in the species Homo sapiens

A disintegrin and metalloproteinase with thrombospondin motifs 4 is an enzyme that in humans is encoded by the ADAMTS4 gene.

Elongation factor 1-delta is a protein that in humans is encoded by the EEF1D gene.

Disintegrin and metalloproteinase domain-containing protein 12 is an enzyme that in humans is encoded by the ADAM12 gene. ADAM12 has two splice variants: ADAM12-L, the long form, has a transmembrane region and ADAM12-S, a shorter variant, is soluble and lacks the transmembrane and cytoplasmic domains.

Disintegrin and metalloproteinase domain-containing protein 15 is an enzyme that in humans is encoded by the ADAM15 gene.

A Disintegrin and metalloproteinase domain-containing protein 10, also known as ADAM10 or CDw156 or CD156c is a protein that in humans is encoded by the ADAM10 gene.

<span class="mw-page-title-main">ADAMTS1</span> Protein-coding gene in the species Homo sapiens

A disintegrin and metalloproteinase with thrombospondin motifs 1 is an enzyme that in humans is encoded by the ADAMTS1 gene.

Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ADAM9 gene.

Thrombospondin-2 is a protein that in humans is encoded by the THBS2 gene.

Disintegrin and metalloproteinase domain-containing protein 33 is an enzyme that in humans is encoded by the ADAM33 gene.

Paired box gene 4, also known as PAX4, is a protein which in humans is encoded by the PAX4 gene.

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 is an enzyme that in humans is encoded by the MAGI1 gene.

Microspherule protein 1 is a protein that in humans is encoded by the MCRS1 gene.

Leucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the LARS gene.

Disintegrin and metalloproteinase domain-containing protein 22 also known as ADAM22 is an enzyme that in humans is encoded by the ADAM22 gene.

Disintegrin and metalloproteinase domain-containing protein 2 or Beta-fertilin is an enzyme that in humans is encoded by the ADAM2 gene.

Disintegrin and metalloproteinase domain-containing protein 23 is a non-catalytic protein that in humans is encoded by the ADAM23 gene. It is a member of the ADAM family of extracellular matrix metalloproteinases.

Disintegrin and metalloproteinase domain-containing protein 28 is an enzyme that in humans is encoded by the ADAM28 gene.

A disintegrin and metalloproteinase with thrombospondin motifs 3 is an enzyme that in humans is encoded by the ADAMTS3 gene. The protein encoded by this gene is the major procollagen II N-propeptidase.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000135074 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000011256 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "Entrez Gene: ADAM19 ADAM metallopeptidase domain 19 (meltrin beta)".
↑ 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. S2CID 22611084.

External links

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

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. S2CID 20528590.
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. S2CID 22611084.
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. S2CID 24891674.
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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000135074 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[entrez-5] 1 2 "Entrez Gene: ADAM19 ADAM metallopeptidase domain 19 (meltrin beta)".

[pmid12463424-6] 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. S2CID 22611084.

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v t e Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)