ADAM23

ADAM23
Identifiers
Aliases	ADAM23,MDC-3, MDC3, ADAM metallopeptidase domain 23
External IDs	OMIM:603710;MGI:1345162;HomoloGene:2826;GeneCards:ADAM23;OMA:ADAM23 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q33.3 Start 206,443,532bp End 206,621,127bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 C2|1 32.31 cM Start 63,485,050bp End 63,635,435bp
RNA expressionpattern Bgee Human Mouse(ortholog) Top expressed in Brodmann area 10 middle temporal gyrus Brodmann area 23 lateral nuclear group of thalamus primary visual cortex postcentral gyrus superior frontal gyrus Brodmann area 9 left ventricle nucleus accumbens Top expressed in facial motor nucleus superior frontal gyrus substantia nigra cerebellar cortex anterior horn of spinal cord pontine nuclei supraoptic nucleus primary visual cortex medial vestibular nucleus deep cerebellar nuclei More reference expression data BioGPS More reference expression data
Gene ontology Molecular function integrin binding metalloendopeptidase activity protein binding metallopeptidase activity Cellular component integral component of membrane extracellular region plasma membrane integral component of plasma membrane membrane glutamatergic synapse integral component of presynaptic membrane Biological process central nervous system development cell adhesion proteolysis cellular response to leukemia inhibitory factor Sources:Amigo/QuickGO
Orthologs Species Human Mouse Entrez 8745 23792 Ensembl ENSG00000114948 ENSMUSG00000025964 UniProt O75077 Q9R1V7 RefSeq (mRNA) NM_003812 NM_001177600 NM_011780 RefSeq (protein) NP_003803 NP_035910 Location (UCSC) Chr 2: 206.44 – 206.62 Mb Chr 1: 63.49 – 63.64 Mb PubMedsearch
Wikidata
View/Edit Human View/Edit Mouse

Disintegrin and metalloproteinase domain-containing protein 23is a non-catalytic protein that in humans is encoded by theADAM23gene.It is a member of theADAM familyofextracellular matrixmetalloproteinases.

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 gene is highly expressed in the brain and may function as an integrin ligand in the brain.

Further reading

• Roberts CM, Tani PH, Bridges LC, Laszik Z, Bowditch RD (Oct 1999)."MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes".The Journal of Biological Chemistry.274(41): 29251–9.doi:10.1074/jbc.274.41.29251.PMID10506182.
• Poindexter K, Nelson N, DuBose RF, Black RA, Cerretti DP (Sep 1999). "The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries".Gene.237(1): 61–70.doi:10.1016/S0378-1119(99)00302-9.PMID10524237.
• Cal S, Freije JM, López JM, Takada Y, López-Otín C (Apr 2000)."ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alphavbeta3 integrin through an RGD-independent mechanism".Molecular Biology of the Cell.11(4): 1457–69.doi:10.1091/mbc.11.4.1457.PMC14859.PMID10749942.
• Sun YP, Deng KJ, Wang F, Zhang J, Huang X, Qiao S, Zhao S (Jan 2004). "Two novel isoforms of Adam23 expressed in the developmental process of mouse and human brains".Gene.325:171–8.doi:10.1016/j.gene.2003.10.012.PMID14697522.
• Schmitt-Ulms G, Hansen K, Liu J, Cowdrey C, Yang J, DeArmond SJ, Cohen FE, Prusiner SB, Baldwin MA (Jun 2004). "Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues".Nature Biotechnology.22(6): 724–31.doi:10.1038/nbt969.PMID15146195.S2CID36630738.
• Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (Jun 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation".Nature Biotechnology.22(6): 707–16.doi:10.1038/nbt971.PMID15146197.S2CID27764390.
• Costa FF, Colin C, Shinjo SM, Zanata SM, Marie SK, Sogayar MC, Camargo AA (Jun 2005). "ADAM23 methylation and expression analysis in brain tumors".Neuroscience Letters.380(3): 260–4.doi:10.1016/j.neulet.2005.01.050.PMID15862898.S2CID42504882.
• Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R (Aug 2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry".Nature Methods.2(8): 591–8.doi:10.1038/nmeth776.PMID16094384.S2CID20475874.
• Takada H, Imoto I, Tsuda H, Nakanishi Y, Ichikura T, Mochizuki H, Mitsufuji S, Hosoda F, Hirohashi S, Ohki M, Inazawa J (Dec 2005)."ADAM23, a possible tumor suppressor gene, is frequently silenced in gastric cancers by homozygous deletion or aberrant promoter hypermethylation".Oncogene.24(54): 8051–60.doi:10.1038/sj.onc.1208952.PMID16103878.

External links

• TheMEROPSonline database for peptidases and their inhibitors:M12.979
• HumanADAM23genome location andADAM23gene details page in theUCSC Genome Browser.