Polyamine Modulated Factor 1 (PMF1)

Polyamine Modulated Factor 1 (PMF1)
Cotransfection of PMF1 and NRF2 activated transcription from the polyamine-responsive element of the SSAT promoter in a reporter assay, and PMF1 was the rate-limiting component.
The deduced 165-amino acid protein has a calculated molecular mass of 19.2 kD. The N-terminal region contains a leucine zipper-like structure. Northern blot analysis detected a 1.2-kb transcript in nearly all tissues examined, with highest expression in heart and skeletal muscle and significant levels in kidney and liver. In vitro translated PMF1 had an apparent molecular mass of about 20 kD.The deduced proteins contain 202 and 133 amino acids, and both have a C-terminal coiled-coil domain. The shorter protein lacks the N-terminal coiled-coil region found in the longer mouse protein and in human PMF1.

Organism species: Homo sapiens (Human)

Organism species: Mus musculus (Mouse)

Organism species: Rattus norvegicus (Rat)