ADAM22

Disintegrin and metalloproteinase domain-containing protein 22 also known as ADAM22 is an enzyme that in humans is encoded by the ADAM22 gene.[5][6][7]

This article is about the enzyme ADAM22. For the podcast host, see Adam22.

ADAM22
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3G5C
Identifiers
Aliases	ADAM22, ADAM 22, MDC2, ADAM metallopeptidase domain 22, EIEE61
External IDs	OMIM: 603709 MGI: 1340046 HomoloGene: 37898 GeneCards: ADAM22
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7q21.12 Start 87,934,143 bp[1] End 88,202,889 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5 A1|5 3.39 cM Start 8,072,352 bp[2] End 8,368,160 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • integrin binding • metalloendopeptidase activity • GO:0001948 protein binding • metallopeptidase activity Cellular component • integral component of membrane • axon • cell membrane • cell projection • membrane • glutamatergic synapse • integral component of postsynaptic density membrane Biological process • Schwann cell differentiation • adult locomotory behavior • negative regulation of cell adhesion • central nervous system development • cell adhesion • myelination in peripheral nervous system • proteolysis • gliogenesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	53616	11496
Ensembl	ENSG00000008277	ENSMUSG00000040537
UniProt	Q9P0K1	Q9R1V6
RefSeq (mRNA)	NM_004194 NM_016351 NM_021721 NM_021722 NM_021723 NM_001324417 NM_001324418 NM_001324419 NM_001324420 NM_001324421	NM_001007220 NM_001007221 NM_001098225 NM_001310439 NM_001310440
RefSeq (protein)	NP_001311346 NP_001311347 NP_001311348 NP_001311349 NP_001311350 NP_004185 NP_057435 NP_068367 NP_068368 NP_068369	NP_001007221 NP_001007222 NP_001091695 NP_001297368 NP_001297369
Location (UCSC)	Chr 7: 87.93 – 88.2 Mb	Chr 5: 8.07 – 8.37 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[7]

Interactions

ADAM22 has been shown to interact with DLG4.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000008277 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000040537 - 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. Sagane K, Ohya Y, Hasegawa Y, Tanaka I (August 1998). "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain". The Biochemical Journal. 334 ( Pt 1) (Pt 1): 93–8. doi:10.1042/bj3340093. PMC 1219666. PMID 9693107.
6. Poindexter K, Nelson N, DuBose RF, Black RA, Cerretti DP (September 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.
7. "Entrez Gene: ADAM22 ADAM metallopeptidase domain 22".
8. 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. Bibcode:2006Sci...313.1792F. doi:10.1126/science.1129947. PMID 16990550.

Further reading

• Harada T, Nishie A, Torigoe K, Ikezaki K, Shono T, Maehara Y, Kuwano M, Wada M (October 2000). "The specific expression of three novel splice variant forms of human metalloprotease-like disintegrin-like cysteine-rich protein 2 gene inBrain tissues and gliomas". Japanese Journal of Cancer Research. 91 (10): 1001–6. doi:10.1111/j.1349-7006.2000.tb00877.x. PMC 5926265. PMID 11050470.
• Zhu Pc, Sun Y, Xu R, Sang Y, Zhao J, Liu G, Cai L, Li C, Zhao S (February 2003). "The interaction between ADAM 22 and 14-3-3zeta: regulation of cell adhesion and spreading". Biochemical and Biophysical Research Communications. 301 (4): 991–9. doi:10.1016/S0006-291X(03)00056-1. PMID 12589811.
• Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biology. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
• Sagane K, Hayakawa K, Kai J, Hirohashi T, Takahashi E, Miyamoto N, Ino M, Oki T, Yamazaki K, Nagasu T (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, Zhao J, Xu R, Sun Y, Xu T, Wang X, Chen L, Feng H, Li C, Zhao S (June 2005). "ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3". Biochemical and Biophysical Research Communications. 331 (4): 938–46. doi:10.1016/j.bbrc.2005.03.229. PMID 15882968.
• D'Abaco GM, Ng K, Paradiso L, Godde NJ, Kaye A, Novak U (January 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 (August 2006). "Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members". Journal of Cell Science. 119 (Pt 16): 3296–305. doi:10.1242/jcs.03065. PMID 16868027.
• 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. Bibcode:2006Sci...313.1792F. doi:10.1126/science.1129947. PMID 16990550.
• Chabrol E, Gourfinkel-An I, Scheffer IE, Picard F, Couarch P, Berkovic SF, McMahon JM, Bajaj N, Mota-Vieira L, Mota R, Trouillard O, Depienne C, Baulac M, LeGuern E, Baulac S (August 2007). "Absence of mutations in the LGI1 receptor ADAM22 gene in autosomal dominant lateral temporal epilepsy" (PDF). Epilepsy Research. 76 (1): 41–8. doi:10.1016/j.eplepsyres.2007.06.014. PMID 17681454.
• Gödde NJ, D'Abaco GM, Paradiso L, Novak U (November 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
• Human ADAM22 genome location and ADAM22 gene details page in the UCSC Genome Browser.