Recombinant Dog GRP94 protein

Specifications

Form

Liquid

Additional notes

> 90% pure as determined by SDS-PAGE and Western Blot analysis

General info

Function

ATP-dependent chaperone involved in the processing of proteins in the endoplasmic reticulum, regulating their transport (PubMed : 17936703). Together with MESD, acts as a modulator of the Wnt pathway by promoting the folding of LRP6, a coreceptor of the canonical Wnt pathway (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Promotes folding and trafficking of TLR4 to the cell surface (By similarity). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (By similarity). May also function in endoplasmic reticulum associated degradation (ERAD); it is however unclear whether it participates to ERAD or is a target of ERAD (By similarity).

Sequence similarities

Belongs to the heat shock protein 90 family.

Post-translational modifications

Phosphorylated by CK2.. N-glycosylated cotranslationally at Asn-217 by STT3A-containing OST-A complex: this glycosylation is constitutive. In response to various stress, 5 additional facultative sites (Asn-62, Asn-107, Asn-445, Asn-481 and Asn-502) can be glycosylated post-translationally by STT3B-containing OST-B complex, leading to a hyperglycosylated form that is degraded by the ER-associated degradation (ERAD) pathway. In normal conditions, the OST-A complex together with CCDC134 prevent glycosylation at facultative sites during protein folding, thereby preventing hyperglycosylation. Mechanistically, nascent HSP90B1 is tethered during translation to a specialized CCDC134-containing translocon that forms a microenvironment for its folding, in which STT3A associates with the SRT pseudosubstrate motif, and prevents access to facultative glycosylation sites until folding is completed, rendering its facultative sites inaccessible to the OST-B complex.