Anti-SSR3 antibody

Supplementary info

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

Activity summary

SSR3 also known as the signal sequence receptor subunit 3 or translocon-associated protein delta subunit is a component of the protein translocon complex located in the endoplasmic reticulum (ER) membrane. The protein has a mass of approximately 18-20 kDa. SSR3 is expressed in various tissues with significant levels in metabolically active tissues such as the liver and kidney. As a membrane-associated protein it functions as part of a larger complex that assists in the translocation of nascent polypeptides into the ER lumen.

Biological function summary

The involvement of SSR3 in the protein translocation process emphasizes its role in maintaining ER function and protein handling. It forms part of the heterotetrameric translocon-associated protein (TRAP) complex which includes SSR1 SSR2 and SSR4. This complex operates in the early stages of the secretory pathway assisting in the proper insertion and folding of nascent proteins into the ER. Consequently SSR3 plays a direct role in the synthesis of secretory and membrane-bound proteins ensuring the fidelity of protein modification and trafficking within the cell.

Pathways

SSR3 is intricately linked with the secretory pathway important for cell function and communication. The protein directly interacts with the translocon machinery which is responsible for mediating the transfer of nascent polypeptides through the ER membrane. SSR3's function in conjunction with TRAP and other components such as the signal recognition particle receptor allow transition into additional cellular pathways like the unfolded protein response (UPR). This relationship maintains ER homeostasis and cellular adaptability situating SSR3 within a network of proteins that respond to ER stress conditions.

Associated diseases and disorders

SSR3 has connections to conditions related to ER stress such as neurodegenerative diseases and certain forms of diabetes. Given its role in protein folding and quality control disruptions in SSR3 function can contribute to the accumulation of misfolded proteins possibly linking it to disorders like Alzheimer's disease. In these scenarios interactions with proteins involved in the UPR like ATF6 and PERK indicate SSR3's contribution to the cellular attempt to rectify protein misfolding and restore ER capacity. Therefore understanding SSR3's function and regulation provides insight into the cellular response to stress that could influence therapeutic strategies for related diseases.