Nprl3

Nitrogen permease regulator-like 3 is a is_associated_with::protein that in humans is encoded by the NPRL3 is_associated_with::gene.

Function
NPRL3 is a human is_associated_with::protein of poorly understood function but has been associated with is_associated_with::cancer.

The most prominent function ascribed to Nprl3 to date is as part of the GATOR1 complex (with is_associated_with::Nprl2 and is_associated_with::DEPDC5) that inhibits the is_associated_with::mechanistic target of rapamycin (mTOR) kinase-complex-1 (is_associated_with::mTORC1) on the surface of the is_associated_with::lysosome (equivalent of degradative is_associated_with::vacuole in yeast) via an effect on the is_associated_with::Rag GTPase complex. Additionally, Nprl3 has been shown to adjust cell metabolism via the TOR pathway, and this is important for development of the cardiovascular system in mammals. Without this effect, spontaneous cell apoptosis would occur. A similar function for Nprl3 has been identified in the female reproductive system of Drosophila during times of protein scarcity.

Gene
In is_associated_with::Homo sapiens, the NPRL3 gene is located at C16orf35. The gene is composed of 14 exons at 53 kbp in length. This gene is highly conserved in vertebrates which is upstream from the is_associated_with::alpha globin gene cluster. Within the fifth intron of the gene there is a regulatory section of DNA is_associated_with::HS-40 which regulates the expression of the alpha globin. This means that the gene C16orf35 is expressed in early is_associated_with::erythrocytes accompanying hemoglobin production.

Structure
The human Nprl3 protein has 569 is_associated_with::amino acids.

Domains
There is a predicted N-terminal longin is_associated_with::domain within the Nprl3 protein (amino acids 4-168). At the C terminus there are three consecutive winged is_associated_with::helix turn helix (HTH) domains. These regions are predicted bind to another macromolecule, which could be DNA, RNA or protein.