ADAM22

ADAM metallopeptidase domain 22
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3G5C​
Identifiers
Symbols	ADAM22 ; ADAM 22; MDC2
External IDs	OMIM: 603709 MGI: 1340046 HomoloGene: 37898 GeneCards: ADAM22 Gene
Gene ontology Molecular function • metalloendopeptidase activity • integrin binding • protein binding • zinc ion binding Cellular component • integral component of membrane • axon Biological process • proteolysis • cell adhesion • negative regulation of cell adhesion • central nervous system development • adult locomotory behavior • myelination in peripheral nervous system Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	53616	11496
Ensembl	ENSG00000008277	ENSMUSG00000040537
UniProt	Q9P0K1	Q9R1V6
RefSeq (mRNA)	NM_004194	NM_001007220
RefSeq (protein)	NP_004185	NP_001007221
Location (UCSC)	Chr 7: 87.93 – 88.2 Mb	Chr 5: 8.07 – 8.37 Mb
PubMed search

Disintegrin and metalloproteinase domain-containing protein 22 also known as ADAM22 is an enzyme that in humans is encoded by the ADAM22 gene.^[1][2][3]

Function

ADAM22 is 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. Alternative splicing results in several transcript variants.^[3]

Interactions

ADAM22 has been shown to interact with DLG4.^[4]

References

1. Sagane K, Ohya Y, Hasegawa Y, Tanaka I (Oct 1998). "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain". Biochem J. 334 ( Pt 1) (Pt 1): 93–8. PMC 1219666. PMID 9693107.
2. Poindexter K, Nelson N, DuBose RF, Black RA, Cerretti DP (Nov 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.
3. "Entrez Gene: ADAM22 ADAM metallopeptidase domain 22".
4. Fukata Y, Adesnik H, Iwanaga T, Bredt DS, Nicoll RA, Fukata M (September 2006). "Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission". Science 313 (5794): 1792–5. doi:10.1126/science.1129947. PMID 16990550.

Further reading

• Harada T, Nishie A, Torigoe K; et al. (2001). "The specific expression of three novel splice variant forms of human metalloprotease-like disintegrin-like cysteine-rich protein 2 gene inBrain tissues and gliomas". Jpn. J. Cancer Res. 91 (10): 1001–6. doi:10.1111/j.1349-7006.2000.tb00877.x. PMID 11050470.
• 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.
• Zhu P, Sun Y, Xu R; et al. (2003). "The interaction between ADAM 22 and 14-3-3zeta: regulation of cell adhesion and spreading". Biochem. Biophys. Res. Commun. 301 (4): 991–9. doi:10.1016/S0006-291X(03)00056-1. PMID 12589811.
• Hillier LW, Fulton RS, Fulton LA; et al. (2003). "The DNA sequence of human chromosome 7". Nature 424 (6945): 157–64. doi:10.1038/nature01782. PMID 12853948.
• Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
• Sagane K, Hayakawa K, Kai J; et al. (2006). "Ataxia and peripheral nerve hypomyelination in ADAM22-deficient mice". BMC neuroscience 6: 33. doi:10.1186/1471-2202-6-33. PMC 1142324. PMID 15876356.
• Zhu P, Sang Y, Xu H; et al. (2005). "ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3". Biochem. Biophys. Res. Commun. 331 (4): 938–46. doi:10.1016/j.bbrc.2005.03.229. PMID 15882968.
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• D'Abaco GM, Ng K, Paradiso L; et al. (2006). "ADAM22, expressed in normal brain but not in high-grade gliomas, inhibits cellular proliferation via the disintegrin domain". Neurosurgery 58 (1): 179–86; discussion 179–86. doi:10.1227/01.NEU.0000192363.84287.8B. PMID 16385342.
• Gödde NJ, D'Abaco GM, Paradiso L, Novak U (2006). "Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members". J. Cell. Sci. 119 (Pt 16): 3296–305. doi:10.1242/jcs.03065. PMID 16868027.
• Fukata Y, Adesnik H, Iwanaga T; et al. (2006). "Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission". Science 313 (5794): 1792–5. doi:10.1126/science.1129947. PMID 16990550.
• Chabrol E, Gourfinkel-An I, Scheffer IE; et al. (2007). "Absence of mutations in the LGI1 receptor ADAM22 gene in autosomal dominant lateral temporal epilepsy". Epilepsy Res. 76 (1): 41–8. doi:10.1016/j.eplepsyres.2007.06.014. PMID 17681454.
• Gödde NJ, D'Abaco GM, Paradiso L, Novak U (2007). "Differential coding potential of ADAM22 mRNAs". Gene 403 (1–2): 80–8. doi:10.1016/j.gene.2007.07.033. PMID 17884303.

External links

• The MEROPS online database for peptidases and their inhibitors: M12.978