ADAM8

Protein-coding gene in the species Homo sapiens

ADAM8
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4DD8

Identifiers
AliasesADAM8, CD156, CD156a, MS2, ADAM metallopeptidase domain 8
External IDsOMIM: 602267 MGI: 107825 HomoloGene: 74384 GeneCards: ADAM8
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for ADAM8
Genomic location for ADAM8
Band10q26.3Start133,262,420 bp[1]
End133,276,868 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for ADAM8
Genomic location for ADAM8
Band7|7 F4Start139,558,845 bp[2]
End139,572,475 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • blood

  • spleen

  • monocyte

  • bone marrow cells

  • pancreatic ductal cell

  • periodontal fiber

  • appendix

  • upper lobe of left lung

  • right lung

  • oocyte
Top expressed in
  • trachea

  • calvaria

  • vein

  • thymus

  • olfactory epithelium

  • cervix

  • inferior vena cava

  • blood

  • spleen

  • lip
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • metal ion binding
  • protein self-association
  • peptidase activity
  • protein binding
  • metalloendopeptidase activity
  • hydrolase activity
  • cell adhesion molecule binding
  • calcium ion binding
  • serine-type endopeptidase activity
  • metallopeptidase activity
  • zinc ion binding
Cellular component
  • cytoplasm
  • integral component of membrane
  • alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex
  • membrane
  • tertiary granule
  • integral component of plasma membrane
  • cell surface
  • specific granule
  • dense core granule membrane
  • podosome
  • phagolysosome
  • alpha9-beta1 integrin-ADAM8 complex
  • plasma membrane
  • specific granule membrane
  • tertiary granule membrane
  • ficolin-1-rich granule membrane
Biological process
  • positive regulation of inflammatory response
  • extracellular matrix disassembly
  • proteolysis
  • positive regulation of cellular extravasation
  • positive regulation of neutrophil extravasation
  • positive regulation of protein processing
  • regulation of cell-cell adhesion
  • positive regulation of protein secretion
  • inflammatory response
  • cellular response to hypoxia
  • positive regulation of T cell migration
  • positive regulation of tumor necrosis factor (ligand) superfamily member 11 production
  • positive regulation of acute inflammatory response
  • cell morphogenesis
  • positive regulation of thymocyte apoptotic process
  • positive regulation of bone resorption
  • negative regulation of neuron apoptotic process
  • positive regulation of fibronectin-dependent thymocyte migration
  • positive regulation of eosinophil migration
  • positive regulation of NF-kappaB transcription factor activity
  • leukocyte migration involved in inflammatory response
  • positive regulation of membrane protein ectodomain proteolysis
  • positive regulation of protein kinase B signaling
  • positive regulation of T cell differentiation in thymus
  • lymphocyte chemotaxis
  • positive regulation of cell adhesion
  • angiogenesis
  • neutrophil degranulation
  • cell-cell adhesion
  • positive regulation of MAP kinase activity
  • positive regulation of innate immune response
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

101

11501

Ensembl

ENSG00000151651

ENSMUSG00000025473

UniProt

P78325

Q05910

RefSeq (mRNA)

NM_001109
NM_001164489
NM_001164490

NM_001291066
NM_007403

RefSeq (protein)

NP_001100
NP_001157961
NP_001157962

NP_001277995
NP_031429

Location (UCSC)Chr 10: 133.26 – 133.28 MbChr 7: 139.56 – 139.57 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

A Disintegrin and metalloproteinase domain-containing protein 8 is an enzyme that in humans is encoded by the ADAM8 gene.[5][6]

Function

This gene encodes a member of the ADAM (a disintegrin and metalloproteinase 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. The protein encoded by this gene may be involved in cell adhesion during neurodegeneration.[6]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000151651 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025473 – 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. ^ Yoshiyama K, Higuchi Y, Kataoka M, Matsuura K, Yamamoto S (April 1997). "CD156 (human ADAM8): expression, primary amino acid sequence, and gene location". Genomics. 41 (1): 56–62. doi:10.1006/geno.1997.4607. PMID 9126482.
  6. ^ a b "Entrez Gene: ADAM8 ADAM metallopeptidase domain 8".

Further reading

  • Yamamoto S, Higuchi Y, Yoshiyama K, Shimizu E, Kataoka M, Hijiya N, Matsuura K (June 1999). "ADAM family proteins in the immune system". Immunology Today. 20 (6): 278–84. doi:10.1016/S0167-5699(99)01464-4. PMID 10354553.
  • Schlomann U, Rathke-Hartlieb S, Yamamoto S, Jockusch H, Bartsch JW (November 2000). "Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): implications for neuron-glia interactions during neurodegeneration". The Journal of Neuroscience. 20 (21): 7964–71. doi:10.1523/JNEUROSCI.20-21-07964.2000. PMC 6772711. PMID 11050116.
  • Amour A, Knight CG, English WR, Webster A, Slocombe PM, Knäuper V, Docherty AJ, Becherer JD, Blobel CP, Murphy G (July 2002). "The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs". FEBS Letters. 524 (1–3): 154–8. doi:10.1016/S0014-5793(02)03047-8. PMID 12135759. S2CID 37423323.
  • Ishikawa N, Daigo Y, Yasui W, Inai K, Nishimura H, Tsuchiya E, Kohno N, Nakamura Y (December 2004). "ADAM8 as a novel serological and histochemical marker for lung cancer". Clinical Cancer Research. 10 (24): 8363–70. doi:10.1158/1078-0432.CCR-04-1436. PMID 15623614.
  • Foley SC, Mogas AK, Olivenstein R, Fiset PO, Chakir J, Bourbeau J, Ernst P, Lemière C, Martin JG, Hamid Q (April 2007). "Increased expression of ADAM33 and ADAM8 with disease progression in asthma". The Journal of Allergy and Clinical Immunology. 119 (4): 863–71. doi:10.1016/j.jaci.2006.12.665. PMID 17339047.
  • Gómez-Gaviro M, Domínguez-Luis M, Canchado J, Calafat J, Janssen H, Lara-Pezzi E, Fourie A, Tugores A, Valenzuela-Fernández A, Mollinedo F, Sánchez-Madrid F, Díaz-González F (June 2007). "Expression and regulation of the metalloproteinase ADAM-8 during human neutrophil pathophysiological activation and its catalytic activity on L-selectin shedding". Journal of Immunology. 178 (12): 8053–63. doi:10.4049/jimmunol.178.12.8053. PMID 17548643.
  • Valkovskaya N, Kayed H, Felix K, Hartmann D, Giese NA, Osinsky SP, Friess H, Kleeff J (2008). "ADAM8 expression is associated with increased invasiveness and reduced patient survival in pancreatic cancer". Journal of Cellular and Molecular Medicine. 11 (5): 1162–74. doi:10.1111/j.1582-4934.2007.00082.x. PMC 4401277. PMID 17979891.

External links

  • The MEROPS online database for peptidases and their inhibitors: M12.208
  • ADAM8 human gene location in the UCSC Genome Browser.
  • ADAM8 human gene details in the UCSC Genome Browser.
  • PDBe-KB provides an overview of all the structure information available in the PDB for Human Disintegrin and metalloproteinase domain-containing protein 8 (ADAM8)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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