Discover millions of predesigned assays for gene expression, mutation detection, microbial ID, and more — all optimized for real-time and digital PCR platforms.
Explore intuitive guides and resources designed to help you get the most out of GeneGlobe. Whether you're designing assays, browsing curated panels, or diving into analysis tools—find practical help to accelerate your research journey.
Predicted to enable enzyme regulator activity. Predicted to be involved in several processes, including negative regulation of ATPase-coupled calcium transmembrane transporter activity; positive regulation of cold-induced thermogenesis; and sarcoplasmic reticulum calcium ion transport. Predicted to be located in sarcoplasmic reticulum membrane. Orthologous to human SLN (sarcolipin). [provided by Alliance of Genome Resources, Jul 2025]
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in rat Sln often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
ATPase binding
Sarcolipin
carboxy-terminal luminal tail domain
phospholamban, sarcolipin, and sarcolamban family of bioactive peptides
enzyme inhibitor activity
protein binding
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
Cytoplasm
cellular membrane
sarcoplasmic reticulum
endoplasmic reticulum membrane
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the rat Sln gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
negative regulation of catalytic activity
sarcoplasmic reticulum calcium ion transport
negative regulation of protein complex disassembly