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{{About|the enzyme ''ADAM22''|the podcast host|Adam Grandmaison}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{Infobox_gene}}
{{GNF_Protein_box
'''Disintegrin and metalloproteinase domain-containing protein 22''' also known as '''ADAM22''' is an [[enzyme]] that in humans is encoded by the ''ADAM22'' [[gene]].<ref name="pmid9693107">{{cite journal | vauthors = Sagane K, Ohya Y, Hasegawa Y, Tanaka I | title = Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain | journal = The Biochemical Journal | volume = 334 ( Pt 1) | issue = Pt 1 | pages = 93–8 | date = August 1998 | pmid = 9693107 | pmc = 1219666 | doi =  }}</ref><ref name="pmid10524237">{{cite journal | vauthors = Poindexter K, Nelson N, DuBose RF, Black RA, Cerretti DP | title = The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries | journal = Gene | volume = 237 | issue = 1 | pages = 61–70 | date = September 1999 | pmid = 10524237 | pmc =  | doi = 10.1016/S0378-1119(99)00302-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ADAM22 ADAM metallopeptidase domain 22| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53616| accessdate = }}</ref>
| image = 
| image_source = 
| PDB =
| Name = ADAM metallopeptidase domain 22
| HGNCid = 201
| Symbol = ADAM22
| AltSymbols =; MDC2; MGC149832
| OMIM = 603709
| ECnumber = 
| Homologene = 37898
| MGIid = 1340046
| GeneAtlas_image1 = PBB_GE_ADAM22_206615_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ADAM22_206616_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ADAM22_208226_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase activity}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
  | Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007162 |text = negative regulation of cell adhesion}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 53616
    | Hs_Ensembl = ENSG00000008277
    | Hs_RefseqProtein = NP_004185
    | Hs_RefseqmRNA = NM_004194
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 87401638
    | Hs_GenLoc_end = 87664383
    | Hs_Uniprot = Q9P0K1
    | Mm_EntrezGene = 11496
    | Mm_Ensembl = ENSMUSG00000040537
    | Mm_RefseqmRNA = NM_001007220
    | Mm_RefseqProtein = NP_001007221
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 8083845
    | Mm_GenLoc_end = 8374087
    | Mm_Uniprot = Q9R1V6
  }}
}}
'''ADAM metallopeptidase domain 22''', also known as '''ADAM22''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADAM22 ADAM metallopeptidase domain 22| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53616| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{PBB_Summary
| section_title =  
| summary_text = This gene encodes 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.<ref name="entrez">{{cite web | title = Entrez Gene: ADAM22 ADAM metallopeptidase domain 22| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53616| accessdate = }}</ref>
}}


==References==
ADAM22 is a member of the [[A disintegrin and metalloproteinase|ADAM]] ('''A''' '''D'''isintegrin '''A'''nd '''M'''etalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom [[disintegrin]]s, 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.<ref name="entrez"/>
{{reflist|2}}
 
==Further reading==
== Interactions ==
 
ADAM22 has been shown to [[Protein-protein interaction|interact]] with [[DLG4]].<ref name="pmid16990550">{{cite journal | vauthors = Fukata Y, Adesnik H, Iwanaga T, Bredt DS, Nicoll RA, Fukata M | title = Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission | journal = Science | volume = 313 | issue = 5794 | pages = 1792–5 | date = September 2006 | pmid = 16990550 | doi = 10.1126/science.1129947 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Harada T, Nishie A, Torigoe K, Ikezaki K, Shono T, Maehara Y, Kuwano M, Wada M | title = The specific expression of three novel splice variant forms of human metalloprotease-like disintegrin-like cysteine-rich protein 2 gene inBrain tissues and gliomas | journal = Japanese Journal of Cancer Research | volume = 91 | issue = 10 | pages = 1001–6 | date = October 2000 | pmid = 11050470 | doi = 10.1111/j.1349-7006.2000.tb00877.x }}
| citations =
* {{cite journal | vauthors = ((Zhu Pc)), Sun Y, Xu R, Sang Y, Zhao J, Liu G, Cai L, Li C, Zhao S | title = The interaction between ADAM 22 and 14-3-3zeta: regulation of cell adhesion and spreading | journal = Biochemical and Biophysical Research Communications | volume = 301 | issue = 4 | pages = 991–9 | date = February 2003 | pmid = 12589811 | doi = 10.1016/S0006-291X(03)00056-1 }}
*{{cite journal | author=Sagane K, Ohya Y, Hasegawa Y, Tanaka I |title=Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain. |journal=Biochem. J. |volume=334 ( Pt 1) |issue=  |pages= 93-8 |year= 1998 |pmid= 9693107 |doi=  }}
* {{cite journal | vauthors = Hillman RT, Green RE, Brenner SE | title = An unappreciated role for RNA surveillance | journal = Genome Biology | volume = 5 | issue = 2 | pages = R8 | year = 2005 | pmid = 14759258 | pmc = 395752 | doi = 10.1186/gb-2004-5-2-r8 }}
*{{cite journal  | author=Poindexter K, Nelson N, DuBose RF, ''et al.'' |title=The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries. |journal=Gene |volume=237 |issue= 1 |pages= 61-70 |year= 1999 |pmid= 10524237 |doi=  }}
* {{cite journal | vauthors = Sagane K, Hayakawa K, Kai J, Hirohashi T, Takahashi E, Miyamoto N, Ino M, Oki T, Yamazaki K, Nagasu T | title = Ataxia and peripheral nerve hypomyelination in ADAM22-deficient mice | journal = BMC Neuroscience | volume = 6 | pages = 33 | year = 2006 | pmid = 15876356 | pmc = 1142324 | doi = 10.1186/1471-2202-6-33 }}
*{{cite journal  | author=Harada T, Nishie A, Torigoe K, ''et al.'' |title=The specific expression of three novel splice variant forms of human metalloprotease-like disintegrin-like cysteine-rich protein 2 gene inBrain tissues and gliomas. |journal=Jpn. J. Cancer Res. |volume=91 |issue= 10 |pages= 1001-6 |year= 2001 |pmid= 11050470 |doi= }}
* {{cite journal | vauthors = Zhu P, Sang Y, Xu H, Zhao J, Xu R, Sun Y, Xu T, Wang X, Chen L, Feng H, Li C, Zhao S | title = ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3 | journal = Biochemical and Biophysical Research Communications | volume = 331 | issue = 4 | pages = 938–46 | date = June 2005 | pmid = 15882968 | doi = 10.1016/j.bbrc.2005.03.229 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = D'Abaco GM, Ng K, Paradiso L, Godde NJ, Kaye A, Novak U | title = ADAM22, expressed in normal brain but not in high-grade gliomas, inhibits cellular proliferation via the disintegrin domain | journal = Neurosurgery | volume = 58 | issue = 1 | pages = 179–86; discussion 179-86 | date = January 2006 | pmid = 16385342 | doi = 10.1227/01.NEU.0000192363.84287.8B }}
*{{cite journal | author=Zhu P, Sun Y, Xu R, ''et al.'' |title=The interaction between ADAM 22 and 14-3-3zeta: regulation of cell adhesion and spreading. |journal=Biochem. Biophys. Res. Commun. |volume=301 |issue= 4 |pages= 991-9 |year= 2003 |pmid= 12589811 |doi=  }}
* {{cite journal | vauthors = Gödde NJ, D'Abaco GM, Paradiso L, Novak U | title = Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members | journal = Journal of Cell Science | volume = 119 | issue = Pt 16 | pages = 3296–305 | date = August 2006 | pmid = 16868027 | doi = 10.1242/jcs.03065 }}
*{{cite journal  | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
* {{cite journal | vauthors = Fukata Y, Adesnik H, Iwanaga T, Bredt DS, Nicoll RA, Fukata M | title = Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission | journal = Science | volume = 313 | issue = 5794 | pages = 1792–5 | date = September 2006 | pmid = 16990550 | doi = 10.1126/science.1129947 }}
*{{cite journal | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 }}
* {{cite journal | vauthors = 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 | title = Absence of mutations in the LGI1 receptor ADAM22 gene in autosomal dominant lateral temporal epilepsy | journal = Epilepsy Research | volume = 76 | issue = 1 | pages = 41–8 | date = August 2007 | pmid = 17681454 | doi = 10.1016/j.eplepsyres.2007.06.014 | url = http://www.hal.inserm.fr/inserm-00306474/file/Chabrol_et_al_Epi_Research-2007.pdf }}
*{{cite journal | author=Sagane K, Hayakawa K, Kai J, ''et al.'' |title=Ataxia and peripheral nerve hypomyelination in ADAM22-deficient mice. |journal=BMC neuroscience |volume=6 |issue= 1 |pages= 33 |year= 2006 |pmid= 15876356 |doi= 10.1186/1471-2202-6-33 }}
* {{cite journal | vauthors = Gödde NJ, D'Abaco GM, Paradiso L, Novak U | title = Differential coding potential of ADAM22 mRNAs | journal = Gene | volume = 403 | issue = 1-2 | pages = 80–8 | date = November 2007 | pmid = 17884303 | doi = 10.1016/j.gene.2007.07.033 }}
*{{cite journal | author=Zhu P, Sang Y, Xu H, ''et al.'' |title=ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3. |journal=Biochem. Biophys. Res. Commun. |volume=331 |issue= 4 |pages= 938-46 |year= 2005 |pmid= 15882968 |doi= 10.1016/j.bbrc.2005.03.229 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=D'Abaco GM, Ng K, Paradiso L, ''et al.'' |title=ADAM22, expressed in normal brain but not in high-grade gliomas, inhibits cellular proliferation via the disintegrin domain. |journal=Neurosurgery |volume=58 |issue= 1 |pages= 179-86; discussion 179-86 |year= 2006 |pmid= 16385342 |doi= }}
*{{cite journal | author=Gödde NJ, D'Abaco GM, Paradiso L, Novak U |title=Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members. |journal=J. Cell. Sci. |volume=119 |issue= Pt 16 |pages= 3296-305 |year= 2006 |pmid= 16868027 |doi= 10.1242/jcs.03065 }}
*{{cite journal | author=Fukata Y, Adesnik H, Iwanaga T, ''et al.'' |title=Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission. |journal=Science |volume=313 |issue= 5794 |pages= 1792-5 |year= 2006 |pmid= 16990550 |doi= 10.1126/science.1129947 }}
*{{cite journal | author=Chabrol E, Gourfinkel-An I, Scheffer IE, ''et al.'' |title=Absence of mutations in the LGI1 receptor ADAM22 gene in autosomal dominant lateral temporal epilepsy. |journal=Epilepsy Res. |volume=76 |issue= 1 |pages= 41-8 |year= 2007 |pmid= 17681454 |doi= 10.1016/j.eplepsyres.2007.06.014 }}
*{{cite journal | author=Gödde NJ, D'Abaco GM, Paradiso L, Novak U |title=Differential coding potential of ADAM22 mRNAs. |journal=Gene |volume=403 |issue= 1-2 |pages= 80-8 |year= 2007 |pmid= 17884303 |doi= 10.1016/j.gene.2007.07.033 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M12.978 M12.978]
* {{UCSC gene info|ADAM22}}
 
{{Metalloendopeptidases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
 
 
{{DEFAULTSORT:Adam22}}
[[Category:Peptidase]]
[[Category:Human proteins]]
[[Category:EC 3.4.24]]
 
{{gene-7-stub}}

Latest revision as of 12:34, 4 November 2018

This article is about the enzyme ADAM22. For the podcast host, see Adam Grandmaison.
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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

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 (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 1219666. PMID 9693107.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "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

External links

Retrieved from "https://www.wikidoc.org/index.php?title=ADAM22&oldid=1533903"