Q95235 · LYAM1_PONPY

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.

Features

Showing features for binding site.

137250100150200250300350
TypeIDPosition(s)Description
Binding site118Ca2+ (UniProtKB | ChEBI)
Binding site120Ca2+ (UniProtKB | ChEBI)
Binding site126Ca2+ (UniProtKB | ChEBI)
Binding site143Ca2+ (UniProtKB | ChEBI)
Binding site144Ca2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular Functioncalcium ion binding
Molecular Functionoligosaccharide 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
  • Alternative names
    • CD62 antigen-like family member L
    • Leukocyte adhesion molecule 1 (LAM-1)
    • Leukocyte-endothelial cell adhesion molecule 1 (LECAM1)
    • Lymph node homing receptor
  • CD Antigen Name
    • CD62L

Gene names

    • Name
      SELL

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pongo

Accessions

  • Primary accession
    Q95235

Subcellular Location

Cell membrane
; Single-pass type I membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain39-332Extracellular
Transmembrane333-355Helical
Topological domain356-372Cytoplasmic

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-28
PropeptidePRO_000001748529-38
ChainPRO_000001748639-372L-selectin
Disulfide bond57↔155
Glycosylation60N-linked (GlcNAc...) asparagine
Glycosylation104N-linked (GlcNAc...) asparagine
Disulfide bond128↔147
Disulfide bond128↔160
Disulfide bond160↔171
Disulfide bond165↔180
Glycosylation177N-linked (GlcNAc...) asparagine
Disulfide bond182↔191
Disulfide bond197↔241
Glycosylation216N-linked (GlcNAc...) asparagine
Glycosylation226N-linked (GlcNAc...) asparagine
Disulfide bond227↔254
Glycosylation232N-linked (GlcNAc...) asparagine
Glycosylation246N-linked (GlcNAc...) asparagine
Disulfide bond259↔303
Glycosylation271N-linked (GlcNAc...) asparagine
Disulfide bond289↔316

Post-translational modification

N-glycosylated.

Keywords

PTM databases

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.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain55-155C-type lectin
Domain156-192EGF-like
Domain195-256Sushi 1
Domain257-318Sushi 2

Sequence similarities

Belongs to the selectin/LECAM family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    372
  • Mass (Da)
    42,118
  • Last updated
    1997-02-01 v1
  • Checksum
    6517DD22213FF15E
MIFPWKCQSTQRDLCNIFKLWGWTMLCCDFLAHHGTDCWTYHYSEKPMNWQRARRFCRENYTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPNNKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALCYTASCQPWSCSGHGECVEIINNYTCNCDVGYYGPQCQFVIQCEPLEAPELGTMDCTHPLGNFSFSSQCAFNCSEGTNLTGIEETTCGPFGNWSSPEPTCQVIQCEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKKTICESSGIWSNPSPICQKLDKSFSMIKEGDYNPLFIPVAVMVTAFSGLAFIIWLARRLKKGKKSKKSMDDPY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U73729
EMBL· GenBank· DDBJ
AAB18247.1
EMBL· GenBank· DDBJ
mRNA

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Disclaimer

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