Anti-ERLEC1 antibody [EPR13849]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

ERLEC1 also known as Endoplasmic Reticulum Lectin 1 or XTP3-B is a protein involved in maintaining protein quality control in the endoplasmic reticulum (ER). ERLEC1 has a molecular mass of about 38 kDa. The protein localizes in the ER where it participates in the calnexin/calreticulin cycle and binds to misfolded glycoproteins. Its role as a lectin allows it to recognize specific glycan structures on proteins aiding in their proper folding and maturation.

Biological function summary

ERLEC1 contributes to the ER-associated degradation (ERAD) pathway by interacting with other ER chaperones and lectin-like proteins. ERLEC1 forms part of a protein complex that identifies misfolded glycoproteins and targets them for degradation. Its function is important for relieving the ER of protein overload therefore maintaining cellular homeostasis. This role is particularly significant in tissues with high protein synthesis rates such as the liver and pancreas.

Pathways

ERLEC1 plays an important role in the unfolded protein response (UPR) by assisting in the degradation of malfunctioning proteins. It interacts with other proteins such as HRD1 and SEL1L which are part of the ERAD pathway to achieve this function. ERLEC1 contributes to maintaining cellular health by ensuring only correctly folded proteins proceed to their destination therefore preventing stress induced by protein aggregation.

Associated diseases and disorders

ERLEC1's role in protein degradation links it to neurodegenerative diseases like Parkinson's and Alzheimer's. Misfolded protein accumulation which ERLEC1 helps prevent is a hallmark of these diseases. Disruption of ERLEC1 function may also relate to conditions like cystic fibrosis where improper protein folding and processing are involved. Protein connections to disorders include interactions with well-studied pathological proteins like alpha-synuclein and amyloid-beta highlighting its therapeutic potential.