ADAM22

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, DEE61
External IDs	OMIM: 603709; MGI: 1340046; HomoloGene: 37898; GeneCards: ADAM22; OMA:ADAM22 - orthologs
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 8,122,352 bp [2] End 8,418,160 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in lateral nuclear group of thalamus middle temporal gyrus pons Brodmann area 23 postcentral gyrus orbitofrontal cortex Brodmann area 46 cerebellum cerebellar hemisphere superior frontal gyrus Top expressed in lobe of cerebellum cerebellar vermis dorsal striatum lateral septal nucleus subiculum anterior amygdaloid area medial geniculate nucleus nucleus accumbens dorsomedial hypothalamic nucleus ventromedial nucleus 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 axon plasma 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_001391975 NM_001391976 NM_001391977 NM_001391978 NM_001391979 NM_001391980 NM_001391981 NM_001391982 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: 8.12 – 8.42 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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]}

Function

ADAM22 is a member of the ADAM (ADisintegrin 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. S2CID   33024022.

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. Bibcode:2003BBRC..301..991Z. 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. Bibcode:2005BBRC..331..938Z. 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. S2CID   24601244.
• 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. S2CID   33024022.
• 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. S2CID   28172409.
• 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 .