Sele selectin, endothelial cell [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Seleprovided by MGI
Official Full Name: selectin, endothelial cellprovided by MGI
Primary source: MGI:MGI:98278
See related: Ensembl:ENSMUSG00000026582 AllianceGenome:MGI:98278
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Elam; CD62E; ELAM-1; LECAM2; E-selectin
Summary: Predicted to enable several functions, including oligosaccharide binding activity; phospholipase binding activity; and sialic acid binding activity. Involved in positive regulation of leukocyte tethering or rolling. Acts upstream of or within positive regulation of leukocyte migration. Predicted to be located in several cellular components, including caveola; clathrin-coated pit; and perinuclear region of cytoplasm. Predicted to be active in external side of plasma membrane and extracellular space. Is expressed in several structures, including adrenal gland; genitourinary system; incisor; integumental system; and limb segment. Human ortholog(s) of this gene implicated in IgA glomerulonephritis; brain ischemia; cerebrovascular disease; and coronary artery disease. Orthologous to human SELE (selectin E). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Biased expression in bladder adult (RPKM 5.9), placenta adult (RPKM 2.3) and 1 other tissue See more
Orthologs: human all
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Genomic context

Location:: 1 H2.2; 1 71.35 cM

Exon count:: 15

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	1	NC_000067.7 (163867200..163886056)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	1	NC_000067.6 (164039614..164058487)

Chromosome 1 - NC_000067.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

PDGFRalpha[+]ITGA11[+] fibroblasts foster early-stage cancer lymphovascular invasion and lymphatic metastasis via ITGA11-SELE interplay.
Title: PDGFRα(+)ITGA11(+) fibroblasts foster early-stage cancer lymphovascular invasion and lymphatic metastasis via ITGA11-SELE interplay.
Oxidative Stress Induces E-Selectin Expression through Repression of Endothelial Transcription Factor ERG.
Title: Oxidative Stress Induces E-Selectin Expression through Repression of Endothelial Transcription Factor ERG.
Vascular and blood-brain barrier-related changes underlie stress responses and resilience in female mice and depression in human tissue.
Title: Vascular and blood-brain barrier-related changes underlie stress responses and resilience in female mice and depression in human tissue.
Selectin Dependence of Allergic Skin Inflammation Is Diminished by Maternal Atopy.
Title: Selectin Dependence of Allergic Skin Inflammation Is Diminished by Maternal Atopy.
Adhesion to E-selectin primes macrophages for activation through AKT and mTOR.
Title: Adhesion to E-selectin primes macrophages for activation through AKT and mTOR.
SELE Downregulation Suppresses Mast Cell Accumulation to Protect against Inflammatory Response in Chronic Idiopathic Urticaria.
Title: SELE Downregulation Suppresses Mast Cell Accumulation to Protect against Inflammatory Response in Chronic Idiopathic Urticaria.
Functional binding of E-selectin to its ligands is enhanced by structural features beyond its lectin domain.
Title: Functional binding of E-selectin to its ligands is enhanced by structural features beyond its lectin domain.
Sele is a potential miR-21 target
Title: A protein-mRNA feedback exists in miR-21-associated E-selectin expression.
E-selectin binding activity mediated by the alpha1-3 fucosyltransferases Fut3/Fut6 and Glg1 are instrumental to the formation of bone metastasis. These findings provide unique insights into the functional role of E-selectin as a component of the vascular niche critical for metastatic colonization in bone.
Title: Bone vascular niche E-selectin induces mesenchymal-epithelial transition and Wnt activation in cancer cells to promote bone metastasis.
Study reports that stromal cell-derived factor-1alpha elevated or therapeutically administered in ischemic wounded tissue can stimulate both local endothelial cells (EC) and bone marrow-derived endothelial progenitor cells (EPC) to express reciprocally E-selectin/ligand pairs and thereby enhance EPC-EC interactions.
Title: SDF-1α-induced dual pairs of E-selectin/ligand mediate endothelial progenitor cell homing to critical ischemia.

Submit: New GeneRIF Correction See all GeneRIFs (84)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Targeted (6) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Sele (e-PCR), detects polymorphism
- UniSTS:144389

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables calcium ion binding	IEA Inferred from Electronic Annotation more info
enables oligosaccharide binding	IBA Inferred from Biological aspect of Ancestor more info
enables oligosaccharide binding	IEA Inferred from Electronic Annotation more info
enables oligosaccharide binding	ISO Inferred from Sequence Orthology more info
enables phospholipase binding	IEA Inferred from Electronic Annotation more info
enables phospholipase binding	ISO Inferred from Sequence Orthology more info
enables sialic acid binding	IBA Inferred from Biological aspect of Ancestor more info
enables sialic acid binding	IEA Inferred from Electronic Annotation more info
enables sialic acid binding	ISO Inferred from Sequence Orthology more info
enables transmembrane signaling receptor activity	IEA Inferred from Electronic Annotation more info
enables transmembrane signaling receptor activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in actin filament-based process	IEA Inferred from Electronic Annotation more info
involved_in actin filament-based process	ISO Inferred from Sequence Orthology more info
involved_in heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules	IBA Inferred from Biological aspect of Ancestor more info
involved_in heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules	IEA Inferred from Electronic Annotation more info
involved_in heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules	ISO Inferred from Sequence Orthology more info
involved_in leukocyte cell-cell adhesion	ISO Inferred from Sequence Orthology more info
acts_upstream_of leukocyte migration	IGI Inferred from Genetic Interaction more info	PubMed
involved_in leukocyte tethering or rolling	IBA Inferred from Biological aspect of Ancestor more info
involved_in leukocyte tethering or rolling	IEA Inferred from Electronic Annotation more info
involved_in leukocyte tethering or rolling	ISO Inferred from Sequence Orthology more info
involved_in phospholipase C-activating G protein-coupled receptor signaling pathway	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within positive regulation of leukocyte migration	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of leukocyte tethering or rolling	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of receptor internalization	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of receptor internalization	ISO Inferred from Sequence Orthology more info
involved_in response to cytokine	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to interleukin-1	IEA Inferred from Electronic Annotation more info
involved_in response to interleukin-1	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in caveola	IEA Inferred from Electronic Annotation more info
located_in caveola	ISO Inferred from Sequence Orthology more info
located_in clathrin-coated pit	IEA Inferred from Electronic Annotation more info
located_in clathrin-coated pit	ISO Inferred from Sequence Orthology more info
located_in cortical cytoskeleton	IEA Inferred from Electronic Annotation more info
located_in cortical cytoskeleton	ISO Inferred from Sequence Orthology more info
is_active_in external side of plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular space	IEA Inferred from Electronic Annotation more info
located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in membrane raft	ISO Inferred from Sequence Orthology more info
located_in perinuclear region of cytoplasm	IEA Inferred from Electronic Annotation more info
located_in perinuclear region of cytoplasm	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: E-selectin

Names: CD62 antigen-like family member E; endothelial leukocyte adhesion molecule 1; leukocyte-endothelial cell adhesion molecule 2

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_011345.3 → NP_035475.2 E-selectin precursor

Status: VALIDATED

Source sequence(s)

AC110499

Consensus CDS

CCDS15432.1

UniProtKB/Swiss-Prot

Q00690

Related

ENSMUSP00000027874.7, ENSMUST00000027874.7

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000067.7 Reference GRCm39 C57BL/6J

Range

163867200..163886056

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_017319404.3 → XP_017174893.1 E-selectin isoform X2

Conserved Domains (4) summary

cd00033
Location:501 → 556

CCP; Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system

cd03592
Location:29 → 147

CLECT_selectins_like; C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels)

PHA02927
Location:269 → 496

PHA02927; secreted complement-binding protein; Provisional

cd00054
Location:155 → 182

EGF_CA; Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the ...
XM_006496715.4 → XP_006496778.1 E-selectin isoform X1

See identical proteins and their annotated locations for XP_006496778.1

UniProtKB/TrEMBL

Q3U5F6

Conserved Domains (4) summary

cd00033
Location:501 → 556

CCP; Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system

cd03592
Location:29 → 147

CLECT_selectins_like; C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels)

PHA02927
Location:269 → 496

PHA02927; secreted complement-binding protein; Provisional

cd00054
Location:155 → 182

EGF_CA; Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the ...