A0A2K5F4L1 · A0A2K5F4L1_AOTNA

Function

function

Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for binding site.

138550100150200250300350
TypeIDPosition(s)Description
Binding site131Ca2+ (UniProtKB | ChEBI)
Binding site133Ca2+ (UniProtKB | ChEBI)
Binding site139Ca2+ (UniProtKB | ChEBI)
Binding site156Ca2+ (UniProtKB | ChEBI)
Binding site157Ca2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functioncalcium ion binding
Molecular Functionoligosaccharide binding
Molecular Functionprotease binding
Biological Processcalcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules
Biological Processleukocyte tethering or rolling

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    L-selectin

Gene names

    • Name
      SELL

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Platyrrhini > Aotidae > Aotus

Accessions

  • Primary accession
    A0A2K5F4L1

Proteomes

Subcellular Location

Cell membrane
; Single-pass type I membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane347-368Helical

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond70↔168
Disulfide bond141↔160
Disulfide bond173↔184
Disulfide bond178↔193
Disulfide bond195↔204
Disulfide bond210↔254
Disulfide bond240↔267
Disulfide bond272↔316
Disulfide bond302↔329

Keywords

Interaction

Subunit

Interaction with SELPLG/PSGL1 and PODXL2 is required for promoting recruitment and rolling of leukocytes. This interaction is dependent on the sialyl Lewis X glycan modification of SELPLG and PODXL2, and tyrosine sulfation modifications of SELPLG. Sulfation on 'Tyr-51' of SELPLG is important for L-selectin binding.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain47-169C-type lectin
Domain169-205EGF-like
Domain208-269Sushi
Domain270-331Sushi

Sequence similarities

Belongs to the selectin/LECAM family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    385
  • Mass (Da)
    43,255
  • Last updated
    2018-03-28 v1
  • Checksum
    F2C82016E6D3E018
MGCRRAREGPSKAMIFPWKCQSIQRDLWNIFKLWGWIMLCCDFLAHHGADCWTYHYSEKAMNWQRARRFCQESYTDLVAIQNKAEIEYLNKTLPFSHSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGAGEPNNKKNKEDCVEIYIKRAKDAGKWNDDSCHKPKAALCYTASCQPWSCSGHGECVEIINNYTCNCDVGYYGPQCQFVIQCEPLEAPELGTMACTHPLGDFSFSSQCAFNCSEGTNLTGIEETTCGPFGNWSSPEPSCQVIQCEPLSAPDLGTMGCSHPLASFSFTSACTFSCSEGTELIGEKKTVCESSGIWSNPSPICQKLDRSFSMIKKGDYNPLFIPVAVMVTAFSGLAFIIWLARRLKKGKKSQKSMDDPY

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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