SELE (selectin E, endothelial adhesion molecule 1)

Alias_names	ELAM1
	ELAM
	endothelial adhesion molecule 1
Alias_symbol (synonym)	ESEL
	CD62E
Other alias	ELAM-1
	LECAM2
HGNC (Hugo)	SELE
LocusID (NCBI)	6401
Atlas_Id	42247
Location	1q24.2  [Link to chromosome band 1q24]
Location_base_pair	Starts at 169722640 and ends at 169734079 bp from pter ( according to hg19-Feb_2009)  [Mapping SELE.png]
Local_order	centromere....SELP - SELL - SELE - C1orf156 - C1orf112.....telomere

Note	Member of the Selectin family. ELAM and CD62E, two of the alternative gene names, have continued to be used in the literature for this gene.
	Exons are represented by solid blue rectangles and introns by black lines.The drawing is in scale.
Description	This gene can be found on Chromosome 1 at location 167,958,406-167,969,803. The gene is composed of 14 exons, spanning approximately 12 kb of genomic DNA in the telomere-to-centromere orientation on chromosome region 1q22-1q25. The promoter region is not included.
Transcription	NM_000450 3834 bp mRNA. The sequence is supported by several sequences (cDNA clones) and produces, by alternative splicing, 5 different protein isoforms (6 transcripts). The transcripts differ by truncation of the N-terminus, truncation of the C-terminus, presence or absence of an exon.
Pseudogene	None

Description	Selectin E precursor is composed of 610 amino acids (66655 Da). Subcellular location: Membrane; Single-pass type I membrane protein. It exhibits structural features such as the presence of lectin- and EGF-like domains followed by short consensus repeat (SCR) domains that contain 6 conserved cysteine residues (Sushi domains). E-Selectin belongs to the selectin family of proteins. Amino acids: 610; Molecular Weight: 66655 Dalton. The phosphorylation on Tyr-603 (cytoplasmic domain) is required for the E-selectin-dependent ERK1 / ERK2 activation.
Expression	The endothelial leukocyte adhesion molecule-1 is ubiquitously expressed in normal tissues. SELE is expressed at high level in cytokine-stimulated endothelial cells.
Localisation	Single-pass type I membrane protein.
Function	E-Selectin is thought to be responsible for the accumulation of blood leukocytes at sites of inflammation by mediating the adhesion of cells to the vascular lining. Adhesion molecules participate in the interaction between leukocytes and the endothelium and appear to be involved in the pathogenesis of atherosclerosis.
Homology	Using pairwise alignment function of ClustalW2, the corresponding sequences from Mus musculus and Rattus norvegicus match with a score of 72 and 73 respectively.

Note	Since adhesion molecules such as members of the selectin family participate in the interaction between leukocytes and the endothelium and appear to be involved in the pathogenesis of atherosclerosis, Wenzel et al. (1994) sought DNA polymorphisms in the ELAM1 gene, which appears to be expressed only in activated endothelium. They identified an A-to-C transversion at cDNA nucleotide 561, resulting in an amino acid exchange from serine to arginine at codon 128 (S128R) in the epidermal growth factor-like domain. They found a significantly higher frequency of the mutation in 97 patients aged 50 years or less with angiographically proven severe atherosclerosis (arginine allele frequency, 0.155) compared with an unselected population (arginine allele frequency, 0.088), as well as in 40 patients aged 40 years or less (arginine allele frequency, 0.21). Mutations of the gene may be a risk factor in atherosclerosis. A polymorphism in position 149 is associated with a higher risk of coronary artery disease (CAD). A significantly higher mutation frequency (Arg-149) is observed in patients with angiographically proven severe atherosclerosis compared with an unselected population (Ser-149).Genomewide linkage and candidate gene-based association studies demonstrated that variation in 3 genes on 1q23 is important in the determination of differences in blood pressure levels: ATP1B1 (182330), RGS5 (603276), and SELE (Takei et al, 2002; 131210). E-selectin S128R polymorphism can functionally affect tumor-endothelial interactions as well as motility and signaling properties of neoplastic cells that may modulate the metastatic phenotype (Alessandro et al, 2007).

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