ADAM22

Enzyme found in humans
ADAM22
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3G5C

Identifiers
AliasesADAM22, ADAM 22, MDC2, ADAM metallopeptidase domain 22, EIEE61, DEE61
External IDsOMIM: 603709; MGI: 1340046; HomoloGene: 37898; GeneCards: ADAM22; OMA:ADAM22 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for ADAM22
Genomic location for ADAM22
Band7q21.12Start87,934,143 bp[1]
End88,202,889 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for ADAM22
Genomic location for ADAM22
Band5 A1|5 3.39 cMStart8,122,352 bp[2]
End8,418,160 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
  • cerebellar vermis

  • subiculum

  • medial geniculate nucleus

  • nucleus accumbens

  • dorsomedial hypothalamic nucleus

  • ventromedial nucleus

  • medial dorsal nucleus

  • olfactory tubercle

  • paraventricular nucleus of hypothalamus

  • ventral tegmental area
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
SpeciesHumanMouse
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 MbChr 5: 8.12 – 8.42 Mb
PubMed search[3][4]
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.[5][6][7]

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000008277 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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. 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. 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.
Portal:
  • icon Biology


Stub icon

This article on a gene on human chromosome 7 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e