ICAM3

Intercellular adhesion molecule 3
PDB rendering based on 1t0p.
Available structures PDB 1T0P
Identifiers
Symbols	ICAM3; CD50; CDW50; ICAM-R
External IDs	OMIM: 146631 HomoloGene: 88479 GeneCards: ICAM3 Gene
Gene Ontology Molecular function • receptor binding • integrin binding • protein binding Cellular component • plasma membrane • integral to plasma membrane Biological process • cell-cell adhesion • regulation of immune response Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3385	n/a
Ensembl	ENSG00000076662	n/a
UniProt	P32942	n/a
RefSeq (mRNA)	NM_002162.3	n/a
RefSeq (protein)	NP_002153.2	n/a
Location (UCSC)	Chr 19: 10.44 – 10.45 Mb	n/a
PubMed search	[1]	n/a

Intercellular adhesion molecule 3 (ICAM3) also known as CD50 (Cluster of Differentiation 50), is a human gene.

The protein encoded by this gene is a member of the intercellular adhesion molecule (ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 2-9 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein. This protein is constitutively and abundantly expressed by all leucocytes and may be the most important ligand for LFA-1 in the initiation of the immune response. It functions not only as an adhesion molecule, but also as a potent signalling molecule.

Interactions

ICAM3 has been shown to interact with EZR and Moesin.

See also

• Cluster of differentiation

Further reading

• Simmons DL (1995). "The role of ICAM expression in immunity and disease.". Cancer Surv. 24: 141–55. PMID 7553659. 
• Hayflick JS, Kilgannon P, Gallatin WM (1998). "The intercellular adhesion molecule (ICAM) family of proteins. New members and novel functions.". Immunol. Res. 17 (3): 313–27. doi:10.1007/BF02786454. PMID 9638475. 
• Fawcett J, Holness CL, Needham LA, et al. (1992). "Molecular cloning of ICAM-3, a third ligand for LFA-1, constitutively expressed on resting leukocytes.". Nature 360 (6403): 481–4. doi:10.1038/360481a0. PMID 1448173. 
• Vazeux R, Hoffman PA, Tomita JK, et al. (1992). "Cloning and characterization of a new intercellular adhesion molecule ICAM-R.". Nature 360 (6403): 485–8. doi:10.1038/360485a0. PMID 1448174. 
• Pino-Otín MR, Juan M, de la Fuente MA, et al. (1995). "CD50 (intercellular adhesion molecule-3) is expressed at higher levels on memory than on naive human T cells but induces a similar calcium mobilization on both subsets.". Tissue Antigens 46 (1): 32–44. doi:10.1111/j.1399-0039.1995.tb02473.x. PMID 7482494. 
• Marazuela M, Postigo AA, Acevedo A, et al. (1994). "Adhesion molecules from the LFA-1/ICAM-1,3 and VLA-4/VCAM-1 pathways on T lymphocytes and vascular endothelium in Graves' and Hashimoto's thyroid glands.". Eur. J. Immunol. 24 (10): 2483–90. doi:10.1002/eji.1830241034. PMID 7523142. 
• Holness CL, Bates PA, Little AJ, et al. (1995). "Analysis of the binding site on intercellular adhesion molecule 3 for the leukocyte integrin lymphocyte function-associated antigen 1.". J. Biol. Chem. 270 (2): 877–84. doi:10.1074/jbc.270.2.877. PMID 7822326. 
• Martin S, Rieckmann P, Melchers I, et al. (1995). "Circulating forms of ICAM-3 (cICAM-3). Elevated levels in autoimmune diseases and lack of association with cICAM-1.". J. Immunol. 154 (4): 1951–5. PMID 7836774. 
• Bossy D, Mattei MG, Simmons DL (1995). "The human intercellular adhesion molecule 3 (ICAM3) gene is located in the 19p13.2-p13.3 region, close to the ICAM1 gene.". Genomics 23 (3): 712–3. doi:10.1006/geno.1994.1565. PMID 7851905. 
• Skubitz KM, Ahmed K, Campbell KD, Skubitz AP (1995). "CD50 (ICAM-3) is phosphorylated on tyrosine and is associated with tyrosine kinase activity in human neutrophils.". J. Immunol. 154 (6): 2888–95. PMID 7876557. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Juan M, Vilella R, Mila J, et al. (1993). "CDw50 and ICAM-3: two names for the same molecule". Eur. J. Immunol. 23 (7): 1508–12. doi:10.1002/eji.1830230717. PMID 8325327. 
• de Fougerolles AR, Klickstein LB, Springer TA (1993). "Cloning and expression of intercellular adhesion molecule 3 reveals strong homology to other immunoglobulin family counter-receptors for lymphocyte function-associated antigen 1". J. Exp. Med. 177 (4): 1187–92. doi:10.1084/jem.177.4.1187. PMC 2190956. PMID 8459213. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2190956. 
• Hosaka S, Shah MR, Pope RM, Koch AE (1996). "Soluble forms of P-selectin and intercellular adhesion molecule-3 in synovial fluids". Clin. Immunol. Immunopathol. 78 (3): 276–82. doi:10.1006/clin.1996.0039. PMID 8605703. 
• Van der Vieren M, Le Trong H, Wood CL, et al. (1996). "A novel leukointegrin, alpha d beta 2, binds preferentially to ICAM-3". Immunity 3 (6): 683–90. doi:10.1016/1074-7613(95)90058-6. PMID 8777714. 
• Hayflick JS, Stine J, Fox R, et al. (1997). "Functional mapping of the cytoplasmic region of intercellular adhesion molecule-3 reveals important roles for serine residues". J. Biol. Chem. 272 (35): 22207–14. doi:10.1074/jbc.272.35.22207. PMID 9268366. 
• Serrador JM, Alonso-Lebrero JL, del Pozo MA, et al. (1997). "Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization". J. Cell Biol. 138 (6): 1409–23. doi:10.1083/jcb.138.6.1409. PMC 2132557. PMID 9298994. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2132557. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Bernstein CN, Sargent M, Gallatin WM (1998). "Beta2 integrin/ICAM expression in Crohn's disease". Clin. Immunol. Immunopathol. 86 (2): 147–60. doi:10.1006/clin.1997.4462. PMID 9473377. 

External links

• MeSH ICAM3+protein,+human

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