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ICAM3

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ICAM3
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesICAM3, CD50, CDW50, ICAM-R, intercellular adhesion molecule 3
External IDsOMIM: 146631; HomoloGene: 88479; GeneCards: ICAM3; OMA:ICAM3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

RefSeq (protein)

NP_001307534
NP_001307535
NP_001307537
NP_002153

n/a

Location (UCSC)Chr 19: 10.33 – 10.34 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Intercellular adhesion molecule 3 (ICAM3) also known as CD50 (Cluster of Differentiation 50), is a protein that in humans is encoded by the ICAM3 gene.

Function

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 leukocytes and may be the most important ligand for LFA-1 in the initiation of the immune response.[3] It functions not only as an adhesion molecule, but also as a potent signalling molecule.[4]

Interactions

ICAM3 has been shown to interact with EZR[5][6] and Moesin.[6][7]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000076662Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ de Fougerolles AR, Springer TA (Jan 1992). "Intercellular adhesion molecule 3, a third adhesion counter-receptor for lymphocyte function-associated molecule 1 on resting lymphocytes". The Journal of Experimental Medicine. 175 (1): 185–90. doi:10.1084/jem.175.1.185. PMC 2119096. PMID 1730916.
  4. ^ "Entrez Gene: ICAM3 intercellular adhesion molecule 3".
  5. ^ Heiska L, Alfthan K, Grönholm M, Vilja P, Vaheri A, Carpén O (Aug 1998). "Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4, 5-bisphosphate". The Journal of Biological Chemistry. 273 (34): 21893–900. doi:10.1074/jbc.273.34.21893. PMID 9705328.
  6. ^ a b Serrador JM, Vicente-Manzanares M, Calvo J, Barreiro O, Montoya MC, Schwartz-Albiez R, Furthmayr H, Lozano F, Sánchez-Madrid F (Mar 2002). "A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting". The Journal of Biological Chemistry. 277 (12): 10400–9. doi:10.1074/jbc.M110694200. PMID 11784723.
  7. ^ Serrador JM, Alonso-Lebrero JL, del Pozo MA, Furthmayr H, Schwartz-Albiez R, Calvo J, Lozano F, Sánchez-Madrid F (Sep 1997). "Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization" (PDF). The Journal of Cell Biology. 138 (6): 1409–23. doi:10.1083/jcb.138.6.1409. PMC 2132557. PMID 9298994.

Further reading

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