Q95LG1 · LYAM2_HORSE
- ProteinE-selectin
- GeneSELE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids610 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 101 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 101-108 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: EPNNKQNE | ||||||
Binding site | 103 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 108 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 112-117 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: EIYIKR | ||||||
Binding site | 125 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 125-127 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: NDE | ||||||
Binding site | 126 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | external side of plasma membrane | |
Cellular Component | extracellular space | |
Molecular Function | calcium ion binding | |
Molecular Function | oligosaccharide binding | |
Molecular Function | sialic acid binding | |
Biological Process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules | |
Biological Process | leukocyte tethering or rolling | |
Biological Process | positive regulation of leukocyte tethering or rolling | |
Biological Process | response to cytokine |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameE-selectin
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Equidae > Equus
Accessions
- Primary accessionQ95LG1
Proteomes
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 | 22-555 | Extracellular | ||||
Sequence: WSYSASTTNMTFDEASAYCQQRYTHLVAIQNQEEIKYLNSIFNHSPSYYWIGIRKVNDKWVWIGTQKPLTEEAKNWAPGEPNNKQNEDCVEIYIKRYKDAGKWNDENCNKKKLALCYTAACTHTSCSGHGECVETINNYTCQCHPGFTGLRCEQVVTCQAQEAPEHGRLVCTHPLGNFSYNSSCSVSCEEGYLPSRTEAMQCTSSGEWSAPPPACHVVECDALTNPANGVMQCSQSPGSFPWNTTCTFDCQEGFELTGPQHLQCTPSGNWDNEKPTCKAVTCGAGGHPQNGFVNCSHSSAGEFTFNSSCNFTCEEGFVLQGPAQVECTAQGQWTQQVPVCKALQCKALSRPERGYMSCRPSTSGSFQSGSSCEFSCEQGFVLKGSKKLRCGPTGEWDSEKPTCEAVRCDAVRQPQGGLVRCTHSAAGEFTYKSSCAFSCEEGFELRGSAQLECTLQGQWTQEVPSCQVVQCASLAVPGKVSMSCSGEPVFGAVCTFACPEGWTLNGSAALTCGATGHWSGMLPTCEATAKSNIP | ||||||
Transmembrane | 556-577 | Helical | ||||
Sequence: LTVGLSAAGTSLLTLASFLFWL | ||||||
Topological domain | 578-610 | Cytoplasmic | ||||
Sequence: LKRLRRKAKKFVPASSYQSLQSDGSYQMPSESA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MIASQFLSALTLVLLIKESGA | ||||||
Chain | PRO_0000017491 | 22-610 | E-selectin | |||
Sequence: WSYSASTTNMTFDEASAYCQQRYTHLVAIQNQEEIKYLNSIFNHSPSYYWIGIRKVNDKWVWIGTQKPLTEEAKNWAPGEPNNKQNEDCVEIYIKRYKDAGKWNDENCNKKKLALCYTAACTHTSCSGHGECVETINNYTCQCHPGFTGLRCEQVVTCQAQEAPEHGRLVCTHPLGNFSYNSSCSVSCEEGYLPSRTEAMQCTSSGEWSAPPPACHVVECDALTNPANGVMQCSQSPGSFPWNTTCTFDCQEGFELTGPQHLQCTPSGNWDNEKPTCKAVTCGAGGHPQNGFVNCSHSSAGEFTFNSSCNFTCEEGFVLQGPAQVECTAQGQWTQQVPVCKALQCKALSRPERGYMSCRPSTSGSFQSGSSCEFSCEQGFVLKGSKKLRCGPTGEWDSEKPTCEAVRCDAVRQPQGGLVRCTHSAAGEFTYKSSCAFSCEEGFELRGSAQLECTLQGQWTQEVPSCQVVQCASLAVPGKVSMSCSGEPVFGAVCTFACPEGWTLNGSAALTCGATGHWSGMLPTCEATAKSNIPLTVGLSAAGTSLLTLASFLFWLLKRLRRKAKKFVPASSYQSLQSDGSYQMPSESA | ||||||
Glycosylation | 30 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 40↔137 | |||||
Sequence: CQQRYTHLVAIQNQEEIKYLNSIFNHSPSYYWIGIRKVNDKWVWIGTQKPLTEEAKNWAPGEPNNKQNEDCVEIYIKRYKDAGKWNDENCNKKKLALC | ||||||
Disulfide bond | 110↔129 | |||||
Sequence: CVEIYIKRYKDAGKWNDENC | ||||||
Disulfide bond | 142↔153 | |||||
Sequence: CTHTSCSGHGEC | ||||||
Disulfide bond | 147↔162 | |||||
Sequence: CSGHGECVETINNYTC | ||||||
Glycosylation | 159 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 164↔173 | |||||
Sequence: CHPGFTGLRC | ||||||
Disulfide bond | 179↔223 | |||||
Sequence: CQAQEAPEHGRLVCTHPLGNFSYNSSCSVSCEEGYLPSRTEAMQC | ||||||
Disulfide bond | 192↔205 | |||||
Sequence: CTHPLGNFSYNSSC | ||||||
Glycosylation | 198 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 202 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 209↔236 | |||||
Sequence: CEEGYLPSRTEAMQCTSSGEWSAPPPAC | ||||||
Disulfide bond | 241↔285 | |||||
Sequence: CDALTNPANGVMQCSQSPGSFPWNTTCTFDCQEGFELTGPQHLQC | ||||||
Disulfide bond | 254↔267 | |||||
Sequence: CSQSPGSFPWNTTC | ||||||
Glycosylation | 264 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 271↔298 | |||||
Sequence: CQEGFELTGPQHLQCTPSGNWDNEKPTC | ||||||
Disulfide bond | 303↔348 | |||||
Sequence: CGAGGHPQNGFVNCSHSSAGEFTFNSSCNFTCEEGFVLQGPAQVEC | ||||||
Glycosylation | 315 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 327 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 331 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 334↔361 | |||||
Sequence: CEEGFVLQGPAQVECTAQGQWTQQVPVC | ||||||
Disulfide bond | 366↔411 | |||||
Sequence: CKALSRPERGYMSCRPSTSGSFQSGSSCEFSCEQGFVLKGSKKLRC | ||||||
Disulfide bond | 397↔424 | |||||
Sequence: CEQGFVLKGSKKLRCGPTGEWDSEKPTC | ||||||
Disulfide bond | 429↔474 | |||||
Sequence: CDAVRQPQGGLVRCTHSAAGEFTYKSSCAFSCEEGFELRGSAQLEC | ||||||
Disulfide bond | 460↔487 | |||||
Sequence: CEEGFELRGSAQLECTLQGQWTQEVPSC | ||||||
Disulfide bond | 492↔533 | |||||
Sequence: CASLAVPGKVSMSCSGEPVFGAVCTFACPEGWTLNGSAALTC | ||||||
Disulfide bond | 519↔546 | |||||
Sequence: CPEGWTLNGSAALTCGATGHWSGMLPTC | ||||||
Glycosylation | 526 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-138 | C-type lectin | ||||
Sequence: WSYSASTTNMTFDEASAYCQQRYTHLVAIQNQEEIKYLNSIFNHSPSYYWIGIRKVNDKWVWIGTQKPLTEEAKNWAPGEPNNKQNEDCVEIYIKRYKDAGKWNDENCNKKKLALCY | ||||||
Domain | 139-174 | EGF-like | ||||
Sequence: TAACTHTSCSGHGECVETINNYTCQCHPGFTGLRCE | ||||||
Domain | 177-238 | Sushi 1 | ||||
Sequence: VTCQAQEAPEHGRLVCTHPLGNFSYNSSCSVSCEEGYLPSRTEAMQCTSSGEWSAPPPACHV | ||||||
Domain | 239-300 | Sushi 2 | ||||
Sequence: VECDALTNPANGVMQCSQSPGSFPWNTTCTFDCQEGFELTGPQHLQCTPSGNWDNEKPTCKA | ||||||
Domain | 314-363 | Sushi 3 | ||||
Sequence: VNCSHSSAGEFTFNSSCNFTCEEGFVLQGPAQVECTAQGQWTQQVPVCKA | ||||||
Domain | 365-426 | Sushi 4 | ||||
Sequence: QCKALSRPERGYMSCRPSTSGSFQSGSSCEFSCEQGFVLKGSKKLRCGPTGEWDSEKPTCEA | ||||||
Domain | 428-489 | Sushi 5 | ||||
Sequence: RCDAVRQPQGGLVRCTHSAAGEFTYKSSCAFSCEEGFELRGSAQLECTLQGQWTQEVPSCQV | ||||||
Domain | 490-548 | Sushi 6 | ||||
Sequence: VQCASLAVPGKVSMSCSGEPVFGAVCTFACPEGWTLNGSAALTCGATGHWSGMLPTCEA |
Sequence similarities
Belongs to the selectin/LECAM family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length610
- Mass (Da)66,191
- Last updated2001-12-01 v1
- ChecksumF9D3DED12C445382
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF307972 EMBL· GenBank· DDBJ | AAK48712.1 EMBL· GenBank· DDBJ | mRNA |