Glycoprotein 130

Glycoprotein 130 (also known as gp130, IL6ST, IL6R-beta or CD130) is a transmembrane protein which is the founding member of the class of tall cytokine receptors. It forms one subunit of the type I cytokine receptor within the IL-6 receptor family. It is often referred to as the common gp130 subunit, and is important for signal transduction following cytokine engagement. As with other type I cytokine receptors, gp130 possesses a WSXWS amino acid motif that ensures correct protein folding and ligand binding. It interacts with Janus kinases to elicit an intracellular signal following receptor interaction with its ligand. Structurally, gp130 is composed of five fibronectin type-III domains and one immunoglobulin-like C2-type (immunoglobulin-like) domain in its extracellular portion.

IL6ST
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesIL6ST, CD130, CDW130, GP130, IL-6RB, interleukin 6 signal transducer
External IDsOMIM: 600694 MGI: 96560 HomoloGene: 1645 GeneCards: IL6ST
Orthologs
SpeciesHumanMouse
Entrez

3572

16195

Ensembl

ENSG00000134352

ENSMUSG00000021756

UniProt

P40189
Q17RA0

Q00560

RefSeq (mRNA)

NM_001190981
NM_002184
NM_175767

NM_010560

RefSeq (protein)

NP_034690

Location (UCSC)Chr 5: 55.94 – 55.99 MbChr 13: 112.6 – 112.65 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse
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