| Intercellular adhesion molecule 5, telencephalin | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | ICAM5; TLCN; TLN | ||||||||||||
| External IDs | OMIM: 601852 MGI: 109430 HomoloGene: 2447 GeneCards: ICAM5 Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 7087 | 15898 | |||||||||||
| Ensembl | ENSG00000105376 | ENSMUSG00000032174 | |||||||||||
| UniProt | Q9UMF0 | Q2KHL7 | |||||||||||
| RefSeq (mRNA) | NM_003259.3 | NM_008319.2 | |||||||||||
| RefSeq (protein) | NP_003250.3 | NP_032345.2 | |||||||||||
| Location (UCSC) | Chr 19: 10.4 – 10.41 Mb |
Chr 9: 20.84 – 20.84 Mb |
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| PubMed search | [1] | [2] | |||||||||||
Intercellular adhesion molecule 5 is a protein that in humans is encoded by the ICAM5 gene.[1][2][3]
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 expressed on the surface of telencephalic neurons and displays two types of adhesion activity, homophilic binding between neurons and heterophilic binding between neurons and leukocytes. It may be a critical component in neuron-microglial cell interactions in the course of normal development or as part of neurodegenerative diseases.[3]
Interactions [link]
ICAM5 has been shown to interact with PSEN1.[4]
References [link]
- ^ Mizuno T, Yoshihara Y, Inazawa J, Kagamiyama H, Mori K (Feb 1997). "cDNA cloning and chromosomal localization of the human telencephalin and its distinctive interaction with lymphocyte function-associated antigen-1". J Biol Chem 272 (2): 1156–63. DOI:10.1074/jbc.272.2.1156. PMID 8995416.
- ^ Kilgannon P, Turner T, Meyer J, Wisdom W, Gallatin WM (Jan 1999). "Mapping of the ICAM-5 (telencephalin) gene, a neuronal member of the ICAM family, to a location between ICAM-1 and ICAM-3 on human chromosome 19p13.2". Genomics 54 (2): 328–30. DOI:10.1006/geno.1998.5565. PMID 9828136.
- ^ a b "Entrez Gene: ICAM5 intercellular adhesion molecule 5, telencephalin". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7087.
- ^ Annaert, W G; Esselens C, Baert V, Boeve C, Snellings G, Cupers P, Craessaerts K, De Strooper B (Nov. 2001). "Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins". Neuron (United States) 32 (4): 579–89. DOI:10.1016/S0896-6273(01)00512-8. ISSN 0896-6273. PMID 11719200.
Further reading [link]
- Yoshihara Y, Mori K (1995). "Telencephalin: a neuronal area code molecule?". Neurosci. Res. 21 (2): 119–24. DOI:10.1016/0168-0102(94)90153-8. PMID 7724062.
- 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.
- Benson DL, Yoshihara Y, Mori K (1998). "Polarized distribution and cell type-specific localization of telencephalin, an intercellular adhesion molecule.". J. Neurosci. Res. 52 (1): 43–53. DOI:10.1002/(SICI)1097-4547(19980401)52:1<43::AID-JNR5>3.0.CO;2-K. PMID 9556028.
- Rieckmann P, Turner T, Kligannon P, Steinhoff BJ (1998). "Telencephalin as an indicator for temporal-lobe dysfunction.". Lancet 352 (9125): 370–1. DOI:10.1016/S0140-6736(05)60469-2. PMID 9717930.
- Arii N, Mizuguchi M, Mori K, Takashima S (1999). "Development of telencephalin in the human cerebrum.". Microsc. Res. Tech. 46 (1): 18–23. DOI:10.1002/(SICI)1097-0029(19990701)46:1<18::AID-JEMT2>3.0.CO;2-G. PMID 10402269.
- Mizuno T, Yoshihara Y, Kagamiyama H, et al. (2000). "Neuronal adhesion molecule telencephalin induces rapid cell spreading of microglia.". Brain Res. 849 (1-2): 58–66. DOI:10.1016/S0006-8993(99)01984-8. PMID 10592287.
- Tian L, Kilgannon P, Yoshihara Y, et al. (2000). "Binding of T lymphocytes to hippocampal neurons through ICAM-5 (telencephalin) and characterization of its interaction with the leukocyte integrin CD11a/CD18.". Eur. J. Immunol. 30 (3): 810–8. DOI:10.1002/1521-4141(200003)30:3<810::AID-IMMU810>3.0.CO;2-X. PMID 10741396.
- Tian L, Nyman H, Kilgannon P, et al. (2000). "Intercellular adhesion molecule-5 induces dendritic outgrowth by homophilic adhesion.". J. Cell Biol. 150 (1): 243–52. DOI:10.1083/jcb.150.1.243. PMC 2185561. PMID 10893271. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2185561.
- Annaert WG, Esselens C, Baert V, et al. (2002). "Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins.". Neuron 32 (4): 579–89. DOI:10.1016/S0896-6273(01)00512-8. PMID 11719200.
- 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. DOI:10.1038/nbt810. PMID 12665801.
- Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.". Anal. Chem. 76 (10): 2763–72. DOI:10.1021/ac035352d. PMID 15144186.
- Cox DG, Hankinson SE, Hunter DJ (2006). "Polymorphisms in the ICAM gene locus are not associated with breast cancer Risk.". Cancer Epidemiol. Biomarkers Prev. 15 (1): 178–9. DOI:10.1158/1055-9965.EPI-05-0790. PMID 16434609.
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ICAM3
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 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
References
Further reading
External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
ICAM-1
ICAM-1 (Intercellular Adhesion Molecule 1) also known as CD54 (Cluster of Differentiation 54) is a protein that in humans is encoded by the ICAM1 gene. This gene encodes a cell surface glycoprotein which is typically expressed on endothelial cells and cells of the immune system. It binds to integrins of type CD11a / CD18, or CD11b / CD18 and is also exploited by rhinovirus as a receptor.
Structure
ICAM-1 is a member of the immunoglobulin superfamily, the superfamily of proteins including antibodies and T-cell receptors. ICAM-1 is a transmembrane protein possessing an amino-terminus extracellular domain, a single transmembrane domain, and a carboxy-terminus cytoplasmic domain. The structure of ICAM-1 is characterized by heavy glycosylation, and the protein’s extracellular domain is composed of multiple loops created by disulfide bridges within the protein. The dominant secondary structure of the protein is the beta sheet, leading researchers to hypothesize the presence of dimerization domains within ICAM-1.
