Q95235 · LYAM1_PONPY
- ProteinL-selectin
- GeneSELL
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids372 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | calcium ion binding | |
Molecular Function | oligosaccharide binding | |
Biological Process | calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules | |
Biological Process | leukocyte tethering or rolling |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameL-selectin
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pongo
Accessions
- Primary accessionQ95235
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 39-332 | Extracellular | ||||
Sequence: WTYHYSEKPMNWQRARRFCRENYTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPNNKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALCYTASCQPWSCSGHGECVEIINNYTCNCDVGYYGPQCQFVIQCEPLEAPELGTMDCTHPLGNFSFSSQCAFNCSEGTNLTGIEETTCGPFGNWSSPEPTCQVIQCEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKKTICESSGIWSNPSPICQKLDKSFSMIKEGDYN | ||||||
Transmembrane | 333-355 | Helical | ||||
Sequence: PLFIPVAVMVTAFSGLAFIIWLA | ||||||
Topological domain | 356-372 | Cytoplasmic | ||||
Sequence: RRLKKGKKSKKSMDDPY |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-28 | |||||
Sequence: MIFPWKCQSTQRDLCNIFKLWGWTMLCC | ||||||
Propeptide | PRO_0000017485 | 29-38 | ||||
Sequence: DFLAHHGTDC | ||||||
Chain | PRO_0000017486 | 39-372 | L-selectin | |||
Sequence: WTYHYSEKPMNWQRARRFCRENYTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPNNKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALCYTASCQPWSCSGHGECVEIINNYTCNCDVGYYGPQCQFVIQCEPLEAPELGTMDCTHPLGNFSFSSQCAFNCSEGTNLTGIEETTCGPFGNWSSPEPTCQVIQCEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKKTICESSGIWSNPSPICQKLDKSFSMIKEGDYNPLFIPVAVMVTAFSGLAFIIWLARRLKKGKKSKKSMDDPY | ||||||
Disulfide bond | 57↔155 | |||||
Sequence: CRENYTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPNNKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALC | ||||||
Glycosylation | 60 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 104 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 128↔147 | |||||
Sequence: CVEIYIKRNKDAGKWNDDAC | ||||||
Disulfide bond | 128↔160 | |||||
Sequence: CVEIYIKRNKDAGKWNDDACHKLKAALCYTASC | ||||||
Disulfide bond | 160↔171 | |||||
Sequence: CQPWSCSGHGEC | ||||||
Disulfide bond | 165↔180 | |||||
Sequence: CSGHGECVEIINNYTC | ||||||
Glycosylation | 177 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 182↔191 | |||||
Sequence: CDVGYYGPQC | ||||||
Disulfide bond | 197↔241 | |||||
Sequence: CEPLEAPELGTMDCTHPLGNFSFSSQCAFNCSEGTNLTGIEETTC | ||||||
Glycosylation | 216 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 226 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 227↔254 | |||||
Sequence: CSEGTNLTGIEETTCGPFGNWSSPEPTC | ||||||
Glycosylation | 232 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 246 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 259↔303 | |||||
Sequence: CEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKKTIC | ||||||
Glycosylation | 271 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 289↔316 | |||||
Sequence: CSEGTELIGKKKTICESSGIWSNPSPIC |
Post-translational modification
N-glycosylated.
Keywords
- PTM
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.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 55-155 | C-type lectin | ||||
Sequence: RFCRENYTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPNNKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALC | ||||||
Domain | 156-192 | EGF-like | ||||
Sequence: YTASCQPWSCSGHGECVEIINNYTCNCDVGYYGPQCQ | ||||||
Domain | 195-256 | Sushi 1 | ||||
Sequence: IQCEPLEAPELGTMDCTHPLGNFSFSSQCAFNCSEGTNLTGIEETTCGPFGNWSSPEPTCQV | ||||||
Domain | 257-318 | Sushi 2 | ||||
Sequence: IQCEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKKTICESSGIWSNPSPICQK |
Sequence similarities
Belongs to the selectin/LECAM family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length372
- Mass (Da)42,118
- Last updated1997-02-01 v1
- Checksum6517DD22213FF15E