ADAM11

ADAM metallopeptidase domain 11
Identifiers
Symbols	ADAM11 ; MDC
External IDs	OMIM: 155120 MGI: 1098667 HomoloGene: 7614 GeneCards: ADAM11 Gene
Gene ontology Molecular function • metalloendopeptidase activity • integrin binding • metallopeptidase activity • zinc ion binding Cellular component • plasma membrane • integral component of membrane • extracellular matrix Biological process • proteolysis • integrin-mediated signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4185	11488
Ensembl	ENSG00000073670	ENSMUSG00000020926
UniProt	O75078	Q9R1V4
RefSeq (mRNA)	NM_002390	NM_001110778
RefSeq (protein)	NP_002381	NP_001104248
Location (UCSC)	Chr 17: 44.76 – 44.78 Mb	Chr 11: 102.76 – 102.78 Mb
PubMed search

Disintegrin and metalloproteinase domain-containing protein 11 is an enzyme that in humans is encoded by the ADAM11 gene.^[1][2]

This gene encodes a member of the ADAM (a disintegrin and metalloprotease) protein 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 represents a candidate tumor suppressor gene for human breast cancer based on its location within a minimal region of chromosome 17q21 previously defined by tumor deletion mapping.^[2]

References

1. Emi M, Katagiri T, Harada Y, Saito H, Inazawa J, Ito I, Kasumi F, Nakamura Y (Jan 1994). "A novel metalloprotease/disintegrin-like gene at 17q21.3 is somatically rearranged in two primary breast cancers". Nat Genet 5 (2): 151–7. doi:10.1038/ng1093-151. PMID 8252040.
2. "Entrez Gene: ADAM11 ADAM metallopeptidase domain 11".

Further reading

• Wolfsberg TG, Primakoff P, Myles DG, White JM (1995). "ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell- matrix interactions". J. Cell Biol. 131 (2): 275–8. doi:10.1083/jcb.131.2.275. PMC 2199973. PMID 7593158.
• Katagiri T, Harada Y, Emi M, Nakamura Y (1994). "Human metalloprotease/disintegrin-like (MDC) gene: exon-intron organization and alternative splicing". Cytogenet. Cell Genet. 68 (1–2): 39–44. doi:10.1159/000133884. PMID 7956356.
• Sagane K, Ohya Y, Hasegawa Y, Tanaka I (1998). "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain". Biochem. J. 334 ( Pt 1) (Pt 1): 93–8. PMC 1219666. PMID 9693107.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
• Brandenberger R, Wei H, Zhang S; et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
• Fu GK, Wang JT, Yang J; et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics 84 (1): 205–10. doi:10.1016/j.ygeno.2004.01.011. PMID 15203218.

External links

• The MEROPS online database for peptidases and their inhibitors: M12.976