TPST1
Description
The TPST1 (tyrosylprotein sulfotransferase 1) is a protein-coding gene located on chromosome 7.
Tyrosylprotein sulfotransferase 1 (TPST1) is an enzyme that catalyzes the sulfation reaction of protein tyrosines, a post-translational modification of proteins. It utilizes 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) as the sulfonate donor and binds proteins with target tyrosine residues to eventually form the tyrosine O-sulfate ester group and the desulfonated 3’-phosphoadenosine-5’-phosphate (PAP). TPST and tyrosine sulfation are involved in various biological and physiological processes, including inflammation, leukocyte movement, viral cell entrance, and cell-cell and protein-protein interactions. The selection for specific tyrosine residues requires a generally accessible tyrosine residue and acidic residues within +5 or -5 residues of the target tyrosine. P-selectin glycoprotein ligand-1 (PSGL-1) is a well-studied substrate for TPST, highlighting the importance of sulfation in PSGL-1 and its ability to bind its receptor. Another TPST substrate, CC-chemokine Receptor 5 (CCR5), is crucial for HIV viral entry into cells. The significance of CCR5's sulfation for HIV invasion has spurred research on TPST and CCR5, including the characterization of the sulfation pattern of CCR5. Beyond these two proteins, other notable protein substrates include Cholecystokinin (CCK), Factor V and Factor VIII, gastrin, the leech enzyme hirudin, fibrinogen, Complement component 4, follicle-stimulating hormone receptor (FSHR), and other chemokine and G-protein coupled receptors.
TPST1 is also known as TANGO13A.
