Recombinant Human Mesencephalic astrocyte-derived neurotrophic factor (MANF)

Uniprot Id

P55145

Target Species

Human

Target Name

MANF

Target Full Name

Mesencephalic astrocyte-derived neurotrophic factor

Target Function

Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. Retained in the ER/sarcoplasmic reticulum (SR) through association with the endoplasmic reticulum chaperone protein HSPA5 under normal conditions. Up-regulated and secreted by the ER/SR in response to ER stress and hypoxia. Following secretion by the ER/SR, directly binds to 3-O-sulfogalactosylceramide, a lipid sulfatide in the outer cell membrane of target cells. Sulfatide binding promotes its cellular uptake by endocytosis, and is required for its role in alleviating ER stress and cell toxicity under hypoxic and ER stress conditions.

Target Subcellular Location

Secreted. Endoplasmic reticulum lumen. Sarcoplasmic reticulum lumen.

Target Protein Families

ARMET family

Target Synonyms

Arginine rich mutated in early stage tumors; Arginine rich protein; Arginine-rich protein; ARMET; ARMET protein; ARP; Manf; MANF_HUMAN; Mesencephalic astrocyte derived neurotrophic factor; Mesencephalic astrocyte-derived neurotrophic factor; MGC142148; MGC142150; Protein ARMET

Target Background

The protein encoded by this gene is localized in the endoplasmic reticulum (ER) and golgi, and is also secreted. Reducing expression of this gene increases susceptibility to ER stress-induced death and results in cell proliferation. Activity of this protein is important in promoting the survival of dopaminergic neurons. The presence of polymorphisms in the N-terminal arginine-rich region, including a specific mutation that changes an ATG start codon to AGG, have been reported in a variety of solid tumors; however, these polymorphisms were later shown to exist in normal tissues and are thus no longer thought to be tumor-related.