|GLG1||GLG1 (golgi apparatus protein 1), ESL-1 (E-selectin ligand 1), MG-160|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 1 glycoprotein
|GLG1 is widely expressed with highest levels in pancreas, skeletal muscle, placenta, heart, testis and ovary. Expression is also in the kidney, liver, lung and brain. Expression is in both adulat and fetal tissues. ESL-1 is expressed on virtually all cells. However, the glycoform which binds to E-selectin has only been detected on cells of the myeloid lineage.|
|MOLECULAR FAMILY NAME|
GLG1, ESL-1, is a single-pass type-1 1,179 aa glycoprotein. It is contains a signal sequence, an extracellular domain which contains a ~70 aa proline and glutamine-rich domain, 16 repeats 50 aa-60 aa long cysteine-rich motif and 5 potential asparagine-linked glycosylation sites, a hydrophobic transmembrane region, and a short cytoplasmic region domain. The proline and glutamine-rich segment contains a polyglutamine stretch which is encoded by an uninterruped exonic sequence. Mouse ESL-1 is likely to be the homologue which is 98% identical to the rat Golgi glycoprotein MG-160. ESL-1 may also be a splice variant of the cysteine-rich fibroblast growth factor (FGF) receptor, identified in the chicken and the human. Apart from the glutamine-rich N-terminal segment, ESL-1 is >98% identical to the human cysteine-rich FGF receptor.
POST-TRANSCRIPTIONAL MODIFICATION: No information.
GLG1 has N-linked glycosylation sites. It contains sialic acid residues and fucosylation which is essential for binding to E-selectin.
|LIGANDS AND MOLECULES ASSOCIATED WITH GLG1|
E-selectin, CD62E, binds to a glycoform of ESL-1 expressed on myeloid cells but not other cells. Binding requires N-linked carbohydrates on ESL-1 containing both sialic acid and fucose. MG-160 cysteine-rich FGF receptor proteins may be species orthologues of ESL-1 which bind to the fibroblast growth factor.
|GLG1 is a Golgi apparatus protein 1 which binds fibroblast growth factor and E-selection , a cell adhesion lectin on endothelial cells mediating the binding of neutrophils. Studies in vitro suggest that ESL-1 is a major E-selectin ligand on myeloid cells but the functional significance of this interaction has not been tested in vivo. It is not known what |
role, if any, the protein has in Golgi function.
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF GLG1 IN INTACT ANIMAL: No information.
Database accession numbers
Revised June 25, 2008