ADAM28

ADAM metallopeptidase domain 28
Identifiers
Symbols	ADAM28; ADAM 28; ADAM23; MDC-L; MDC-Lm; MDC-Ls; MDCL; eMDC II; eMDCII
External IDs	OMIM: 606188 MGI: 105988 HomoloGene: 40705 GeneCards: ADAM28 Gene
Gene Ontology Molecular function • metalloendopeptidase activity • peptidase activity • metallopeptidase activity • zinc ion binding • metal ion binding Cellular component • extracellular region • plasma membrane • integral to membrane Biological process • proteolysis • spermatogenesis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10863	13522
Ensembl	ENSG00000042980	ENSMUSG00000014725
UniProt	Q9UKQ2	Q9JLN6
RefSeq (mRNA)	NM_014265.4	NM_001048175.1
RefSeq (protein)	NP_055080.2	NP_001041640.1
Location (UCSC)	Chr 8: 24.15 – 24.22 Mb	Chr 14: 69.22 – 69.27 Mb
PubMed search	[1]	[2]

Disintegrin and metalloproteinase domain-containing protein 28 is an enzyme that in humans is encoded by the ADAM28 gene.

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. The protein encoded by this gene is a lymphocyte-expressed ADAM protein. Alternative splicing results in two transcript variants. The shorter version encodes a secreted isoform, while the longer version encodes a transmembrane isoform.

Further reading

• Roberts CM, Tani PH, Bridges LC, et al. (1999). "MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes.". J. Biol. Chem. 274 (41): 29251–9. doi:10.1074/jbc.274.41.29251. PMID 10506182. 
• Jury JA, Perry AC, Hall L (2000). "Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymis.". Mol. Hum. Reprod. 5 (12): 1127–34. doi:10.1093/molehr/5.12.1127. PMID 10587367. 
• Howard L, Maciewicz RA, Blobel CP (2000). "Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28". Biochem. J. 348 Pt 1 (Pt 1): 21–7. doi:10.1042/0264-6021:3480021. PMC 1221031. PMID 10794709. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1221031. 
• Bridges LC, Tani PH, Hanson KR, et al. (2002). "The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1". J. Biol. Chem. 277 (5): 3784–92. doi:10.1074/jbc.M109538200. PMID 11724793. 
• Bridges LC, Hanson KR, Tani PH, et al. (2003). "Integrin alpha4beta1-dependent adhesion to ADAM 28 (MDC-L) requires an extended surface of the disintegrin domain". Biochemistry 42 (13): 3734–41. doi:10.1021/bi026871y. PMID 12667064. 
• Fourie AM, Coles F, Moreno V, Karlsson L (2003). "Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23". J. Biol. Chem. 278 (33): 30469–77. doi:10.1074/jbc.M213157200. PMID 12777399. 
• Mochizuki S, Shimoda M, Shiomi T, et al. (2004). "ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3". Biochem. Biophys. Res. Commun. 315 (1): 79–84. doi:10.1016/j.bbrc.2004.01.022. PMID 15013428. 
• Ohtsuka T, Shiomi T, Shimoda M, et al. (2006). "ADAM28 is overexpressed in human non-small cell lung carcinomas and correlates with cell proliferation and lymph node metastasis". Int. J. Cancer 118 (2): 263–73. doi:10.1002/ijc.21324. PMID 16052521. 
• Mitsui Y, Mochizuki S, Kodama T, et al. (2006). "ADAM28 is overexpressed in human breast carcinomas: implications for carcinoma cell proliferation through cleavage of insulin-like growth factor binding protein-3". Cancer Res. 66 (20): 9913–20. doi:10.1158/0008-5472.CAN-06-0377. PMID 17047053. 
• Shimoda M, Hashimoto G, Mochizuki S, et al. (2007). "Binding of ADAM28 to P-selectin glycoprotein ligand-1 enhances P-selectin-mediated leukocyte adhesion to endothelial cells". J. Biol. Chem. 282 (35): 25864–74. doi:10.1074/jbc.M702414200. PMID 17597069. 

External links

• The MEROPS online database for peptidases and their inhibitors: M12.224