ADAM23

ADAM metallopeptidase domain 23
Identifiers
Symbols	ADAM23; MDC3
External IDs	OMIM: 603710 MGI: 1345162 HomoloGene: 2826 GeneCards: ADAM23 Gene
Gene Ontology Molecular function • metalloendopeptidase activity • integrin binding • protein binding • metallopeptidase activity • zinc ion binding Cellular component • extracellular region • plasma membrane • integral to plasma membrane Biological process • proteolysis • cell adhesion • central nervous system development Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8745	23792
Ensembl	ENSG00000114948	ENSMUSG00000025964
UniProt	O75077	Q5SRA3
RefSeq (mRNA)	NM_003812	XM_622578
RefSeq (protein)	NP_003803	XP_622578
Location (UCSC)	Chr 2: 207.31 – 207.49 Mb	Chr 1: 63.49 – 63.64 Mb
PubMed search	[1]	[2]

Disintegrin and metalloproteinase domain-containing protein 23 is an enzyme that in humans is encoded by the ADAM23 gene.

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 et al (1999). "MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes". J. Biol. Chem. 274 (41): 29251–9. doi:10.1074/jbc.274.41.29251. PMID 10506182. 
• Poindexter K, Nelson N, DuBose RF et al (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. PMID 10524237. 
• Cal S, Freije JM, López JM et al (2000). "ADAM 23/MDC3, a Human Disintegrin That Promotes Cell Adhesion via Interaction with the αvβ3 Integrin through an RGD-independent Mechanism". Mol. Biol. Cell 11 (4): 1457–69. PMC 14859. PMID 10749942. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=14859. 
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Sun YP, Deng KJ, Wang F et al (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. PMID 14697522. 
• Schmitt-Ulms G, Hansen K, Liu J et al (2005). "Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues". Nat. Biotechnol. 22 (6): 724–31. doi:10.1038/nbt969. PMID 15146195. 
• Brandenberger R, Wei H, Zhang S et al (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. 
• Costa FF, Colin C, Shinjo SM et al (2005). "ADAM23 methylation and expression analysis in brain tumors". Neurosci. Lett. 380 (3): 260–4. doi:10.1016/j.neulet.2005.01.050. PMID 15862898. 
• Tao WA, Wollscheid B, O'Brien R et al (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nat. Methods 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384. 
• Takada H, Imoto I, Tsuda H et al (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. PMID 16103878. 

External links

• The MEROPS online database for peptidases and their inhibitors: M12.979