ADAM12

For the television show, see Adam 12

ADAM metallopeptidase domain 12
Identifiers
Symbols	ADAM12; MCMP; MCMPMltna; MLTN; MLTNA
External IDs	OMIM: 602714 MGI: 105378 HomoloGene: 74862 GeneCards: ADAM12 Gene
Gene Ontology Molecular function • metalloendopeptidase activity • protein binding • peptidase activity • metallopeptidase activity • zinc ion binding • SH3 domain binding • metal ion binding Cellular component • extracellular region • plasma membrane • integral to membrane Biological process • proteolysis • cell adhesion • epidermal growth factor receptor signaling pathway • myoblast fusion Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8038	11489
Ensembl	ENSG00000148848	ENSMUSG00000054555
UniProt	O43184	n/a
RefSeq (mRNA)	NM_003474.4	NM_007400.2
RefSeq (protein)	NP_003465.3	NP_031426.2
Location (UCSC)	Chr 10: 127.7 – 128.08 Mb	Chr 7: 141.07 – 141.42 Mb
PubMed search	[1]	[2]

Disintegrin and metalloproteinase domain-containing protein 12 is an enzyme that in humans is encoded by the ADAM12 gene.

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 has two alternatively spliced transcripts: a shorter secreted form and a longer membrane-bound form. The shorter form is found to stimulate myogenesis.

Interactions

ADAM12 has been shown to interact with PIK3R1, IGFBP3 and Actinin, alpha 2.

Further reading

• Kang Q, Cao Y, Zolkiewska A (2001). "Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85alpha activates phosphatidylinositol 3-kinase in C2C12 cells.". J. Biol. Chem. 276 (27): 24466–72. doi:10.1074/jbc.M101162200. PMID 11313349. 
• Yagami-Hiromasa T, Sato T, Kurisaki T, et al. (1995). "A metalloprotease-disintegrin participating in myoblast fusion.". Nature 377 (6550): 652–6. doi:10.1038/377652a0. PMID 7566181. 
• Loechel F, Gilpin BJ, Engvall E, et al. (1998). "Human ADAM 12 (meltrin alpha) is an active metalloprotease.". J. Biol. Chem. 273 (27): 16993–7. doi:10.1074/jbc.273.27.16993. PMID 9642263. 
• Howard L, Nelson KK, Maciewicz RA, Blobel CP (1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1.". J. Biol. Chem. 274 (44): 31693–9. doi:10.1074/jbc.274.44.31693. PMID 10531379. 
• Galliano MF, Huet C, Frygelius J, et al. (2000). "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion.". J. Biol. Chem. 275 (18): 13933–9. doi:10.1074/jbc.275.18.13933. PMID 10788519. 
• Iba K, Albrechtsen R, Gilpin B, et al. (2000). "The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading.". J. Cell Biol. 149 (5): 1143–56. doi:10.1083/jcb.149.5.1143. PMC 2174829. PMID 10831617. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2174829. 
• Shi Z, Xu W, Loechel F, et al. (2000). "ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3.". J. Biol. Chem. 275 (24): 18574–80. doi:10.1074/jbc.M002172200. PMID 10849447. 
• Eto K, Puzon-McLaughlin W, Sheppard D, et al. (2001). "RGD-independent binding of integrin alpha9beta1 to the ADAM-12 and -15 disintegrin domains mediates cell-cell interaction.". J. Biol. Chem. 275 (45): 34922–30. doi:10.1074/jbc.M001953200. PMID 10944520. 
• Loechel F, Fox JW, Murphy G, et al. (2001). "ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3.". Biochem. Biophys. Res. Commun. 278 (3): 511–5. doi:10.1006/bbrc.2000.3835. PMID 11095942. 
• Suzuki A, Kadota N, Hara T, et al. (2000). "Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src.". Oncogene 19 (51): 5842–50. doi:10.1038/sj.onc.1203986. PMID 11127814. 
• Kawaguchi N, Xu X, Tajima R, et al. (2002). "ADAM 12 protease induces adipogenesis in transgenic mice.". Am. J. Pathol. 160 (5): 1895–903. doi:10.1016/S0002-9440(10)61136-4. PMC 1850877. PMID 12000741. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1850877. 
• Cao Y, Kang Q, Zhao Z, Zolkiewska A (2002). "Intracellular processing of metalloprotease disintegrin ADAM12". J. Biol. Chem. 277 (29): 26403–11. doi:10.1074/jbc.M110814200. PMID 12000744. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Abram CL, Seals DF, Pass I, et al. (2003). "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells". J. Biol. Chem. 278 (19): 16844–51. doi:10.1074/jbc.M300267200. PMID 12615925. 
• Le Pabic H, Bonnier D, Wewer UM, et al. (2003). "ADAM12 in human liver cancers: TGF-beta-regulated expression in stellate cells is associated with matrix remodeling". Hepatology 37 (5): 1056–66. doi:10.1053/jhep.2003.50205. PMID 12717386. 
• Kawaguchi N, Sundberg C, Kveiborg M, et al. (2004). "ADAM12 induces actin cytoskeleton and extracellular matrix reorganization during early adipocyte differentiation by regulating beta1 integrin function". J. Cell. Sci. 116 (Pt 19): 3893–904. doi:10.1242/jcs.00699. PMID 12915587. 
• Mori S, Tanaka M, Nanba D, et al. (2003). "PACSIN3 binds ADAM12/meltrin alpha and up-regulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor". J. Biol. Chem. 278 (46): 46029–34. doi:10.1074/jbc.M306393200. PMID 12952982. 
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=403697. 
• Laigaard J, Sørensen T, Fröhlich C, et al. (2004). "ADAM12: a novel first-trimester maternal serum marker for Down syndrome". Prenat. Diagn. 23 (13): 1086–91. doi:10.1002/pd.762. PMID 14691998. 

External links

• The MEROPS online database for peptidases and their inhibitors: M12.212
• ADAM12 on the Atlas of Genetics and Oncology