Q95LG1 · LYAM2_HORSE

Function

function

Cell-surface glycoprotein having a role in immunoadhesion (PubMed:11529941).
Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis (By similarity).

Features

Showing features for binding site.

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TypeIDPosition(s)Description
Binding site101Ca2+ (UniProtKB | ChEBI)
Binding site101-108a carbohydrate (UniProtKB | ChEBI)
Binding site103Ca2+ (UniProtKB | ChEBI)
Binding site108Ca2+ (UniProtKB | ChEBI)
Binding site112-117a carbohydrate (UniProtKB | ChEBI)
Binding site125Ca2+ (UniProtKB | ChEBI)
Binding site125-127a carbohydrate (UniProtKB | ChEBI)
Binding site126Ca2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentexternal side of plasma membrane
Cellular Componentextracellular space
Molecular Functioncalcium ion binding
Molecular Functionoligosaccharide binding
Molecular Functionsialic acid binding
Biological Processheterophilic cell-cell adhesion via plasma membrane cell adhesion molecules
Biological Processleukocyte tethering or rolling
Biological Processpositive regulation of leukocyte tethering or rolling
Biological Processresponse to cytokine

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    E-selectin
  • Alternative names
    • CD62 antigen-like family member E
    • Endothelial leukocyte adhesion molecule 1 (ELAM-1)
    • Leukocyte-endothelial cell adhesion molecule 2 (LECAM2)
  • CD Antigen Name
    • CD62E

Gene names

    • Name
      SELE

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Equidae > Equus

Accessions

  • Primary accession
    Q95LG1

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain22-555Extracellular
Transmembrane556-577Helical
Topological domain578-610Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_000001749122-610E-selectin
Glycosylation30N-linked (GlcNAc...) asparagine
Disulfide bond40↔137
Disulfide bond110↔129
Disulfide bond142↔153
Disulfide bond147↔162
Glycosylation159N-linked (GlcNAc...) asparagine
Disulfide bond164↔173
Disulfide bond179↔223
Disulfide bond192↔205
Glycosylation198N-linked (GlcNAc...) asparagine
Glycosylation202N-linked (GlcNAc...) asparagine
Disulfide bond209↔236
Disulfide bond241↔285
Disulfide bond254↔267
Glycosylation264N-linked (GlcNAc...) asparagine
Disulfide bond271↔298
Disulfide bond303↔348
Glycosylation315N-linked (GlcNAc...) asparagine
Glycosylation327N-linked (GlcNAc...) asparagine
Glycosylation331N-linked (GlcNAc...) asparagine
Disulfide bond334↔361
Disulfide bond366↔411
Disulfide bond397↔424
Disulfide bond429↔474
Disulfide bond460↔487
Disulfide bond492↔533
Disulfide bond519↔546
Glycosylation526N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Induction

Up-regulated in endothelial cells after exposure to bacterial lipopolysaccharide (LPS).

Interaction

Subunit

Interacts with SELPLG/PSGL1 and PODXL2 through the sialyl Lewis X epitope. SELPLG sulfation appears not to be required for this interaction.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain22-138C-type lectin
Domain139-174EGF-like
Domain177-238Sushi 1
Domain239-300Sushi 2
Domain314-363Sushi 3
Domain365-426Sushi 4
Domain428-489Sushi 5
Domain490-548Sushi 6

Sequence similarities

Belongs to the selectin/LECAM family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    610
  • Mass (Da)
    66,191
  • Last updated
    2001-12-01 v1
  • Checksum
    F9D3DED12C445382
MIASQFLSALTLVLLIKESGAWSYSASTTNMTFDEASAYCQQRYTHLVAIQNQEEIKYLNSIFNHSPSYYWIGIRKVNDKWVWIGTQKPLTEEAKNWAPGEPNNKQNEDCVEIYIKRYKDAGKWNDENCNKKKLALCYTAACTHTSCSGHGECVETINNYTCQCHPGFTGLRCEQVVTCQAQEAPEHGRLVCTHPLGNFSYNSSCSVSCEEGYLPSRTEAMQCTSSGEWSAPPPACHVVECDALTNPANGVMQCSQSPGSFPWNTTCTFDCQEGFELTGPQHLQCTPSGNWDNEKPTCKAVTCGAGGHPQNGFVNCSHSSAGEFTFNSSCNFTCEEGFVLQGPAQVECTAQGQWTQQVPVCKALQCKALSRPERGYMSCRPSTSGSFQSGSSCEFSCEQGFVLKGSKKLRCGPTGEWDSEKPTCEAVRCDAVRQPQGGLVRCTHSAAGEFTYKSSCAFSCEEGFELRGSAQLECTLQGQWTQEVPSCQVVQCASLAVPGKVSMSCSGEPVFGAVCTFACPEGWTLNGSAALTCGATGHWSGMLPTCEATAKSNIPLTVGLSAAGTSLLTLASFLFWLLKRLRRKAKKFVPASSYQSLQSDGSYQMPSESA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF307972
EMBL· GenBank· DDBJ
AAK48712.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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