TULP1 Human

The tubby-like proteins were first identified through a mutation at the tubby (Tub) locus, which causes obesity and neurosensory degeneration . This discovery led to the identification of the TULP family, which is conserved across various species, including humans, mice, Drosophila, and C. elegans . The strong conservation of these proteins suggests they perform essential cellular functions.

TULP1, like other tubby-like proteins, is characterized by a specific signature of a carboxyl-terminal tubby domain, which is required for plasma membrane tethering, and an amino-terminal F-box domain, which functions as SCF-type E3 ligases . These structural features enable TULP1 to participate in various cellular processes, including vesicular trafficking, insulin signaling, and gene transcription .

TULP1 is particularly important in the context of neuronal development. It plays a role in the maintenance and function of neuronal cells, and mutations in TULP1 have been associated with retinal degeneration and other neurosensory defects . Experimental evidence suggests that TULP1 is involved in vesicular trafficking, which is crucial for the proper functioning of neurons .

Human recombinant TULP1 is produced in E. coli and consists of a single polypeptide chain containing 276 amino acids, with a molecular mass of 31.1 kDa . It is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques . This recombinant form is used in various research applications to study the function and mechanisms of TULP1 in cellular processes.