ADAM22

ADAM22
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases ADAM22, ADAM 22, MDC2, ADAM metallopeptidase domain 22
External IDs MGI: 1340046 HomoloGene: 37898 GeneCards: ADAM22
RNA expression pattern




More reference expression data
Orthologs
Species Human Mouse
Entrez

53616

11496

Ensembl

ENSG00000008277

ENSMUSG00000040537

UniProt

Q9P0K1

Q9R1V6

RefSeq (mRNA)

NM_001007220
NM_001007221
NM_001098225
NM_001310439
NM_001310440

RefSeq (protein)

NP_004185.1
NP_068367.1
NP_068368.2
NP_068369.1

NP_001007221.1
NP_001007222.1
NP_001091695.1
NP_001297368.1
NP_001297369.1

Location (UCSC) Chr 7: 87.93 – 88.2 Mb Chr 5: 8.07 – 8.37 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/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.[3][4][5]

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.[5]

Interactions

ADAM22 has been shown to interact with DLG4.[6]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ 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. PMC 1219666Freely accessible. PMID 9693107.
  4. ↑ 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.
  5. 1 2 "Entrez Gene: ADAM22 ADAM metallopeptidase domain 22".
  6. ↑ 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, 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. 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 395752Freely accessible. 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 1142324Freely accessible. 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. 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". 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


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