A Disintegrin And Metalloprotease 22 (ADAM22)

MDC2; Disintegrin And Metalloproteinase Domain-Containing Protein 22; Metalloproteinase-Like,Disintegrin-Like,And Cysteine-Rich Protein 2

SPN	N570
HGNC	201
MGI	1340046
PubMed	20089912
UniProt	Q9P0K1
Wiki	ADAM22

ADAM22 is a member of the ADAM 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.

Three-prime RACE yielded products corresponding to 2 MDC2 mRNAs, MDC2-alpha and -beta, in both mouse and human. MDC2-alpha encodes a predicted 859-amino acid protein. The shorter transcript, MDC2-beta, results from exon skipping and encodes an 823-amino acid protein. The MDC2-alpha protein shares 56% and 51% sequence similarity with MDC and MDC3, respectively.

Reference

"Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain."
Biochem. J. 334:93-98(1998) [PubMed] [Europe PMC] [Abstract]

"The specific expression of three novel splice variant forms of human metalloprotease-like disintegrin-like cysteine-rich protein 2 gene in brain tissues and gliomas."
Jpn. J. Cancer Res. 91:1001-1006(2000) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence of human chromosome 7."
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]

"The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries."
Gene 237:61-70(1999) [PubMed] [Europe PMC] [Abstract]

"The interaction between ADAM 22 and 14-3-3zeta: regulation of cell adhesion and spreading."
Biochem. Biophys. Res. Commun. 301:991-999(2003) [PubMed] [Europe PMC] [Abstract]

"An unappreciated role for RNA surveillance."
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]

"ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3."
Biochem. Biophys. Res. Commun. 331:938-946(2005) [PubMed] [Europe PMC] [Abstract]

"ADAM22, expressed in normal brain but not in high-grade gliomas, inhibits cellular proliferation via the disintegrin domain."
Neurosurgery 58:179-186(2006) [PubMed] [Europe PMC] [Abstract]

"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]

"Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function."
J. Biol. Chem. 284:29077-29086(2009) [PubMed] [Europe PMC] [Abstract]