PADI4
Description
The PADI4 (peptidyl arginine deiminase 4) is a protein-coding gene located on chromosome 1.
PADI4, also known as protein-arginine deiminase type-4, is a human enzyme that converts arginine to citrulline residues in proteins (citrullination). This gene is located on chromosome 1 and encodes a protein of 663 amino acids. PADI4 plays a crucial role in inflammation and immune response by influencing granulocyte and macrophage development. It also contributes to epigenetics by deimination of arginines on histones, opposing arginine methylation. PADI4 binds calcium ions and exists as an oligomer. It catalyzes the reaction: Protein L-arginine + H2O = protein L-citrulline + NH3. PADI4 is found in the cytoplasm, nucleus, and cytoplasmic granules of eosinophils and neutrophils.
PADI4 is an enzyme that catalyzes the conversion of arginine to citrulline residues in proteins, a process called citrullination or deimination. This enzyme plays a crucial role in regulating histone modifications, particularly by citrullinating histones H1, H3, and H4. Citrullination of histone H1, specifically at arginine 54, leads to its displacement from chromatin and subsequent chromatin decondensation, which promotes stem cell maintenance and pluripotency. PADI4 also contributes to the innate immune response by facilitating chromatin decondensation in neutrophils during infection. Furthermore, citrullination of histone H3 by PADI4 prevents methylation by CARM1 and HRMT1L2/PRMT1, ultimately repressing transcription. Additionally, PADI4 citrullinates EP300/P300 at arginine 2142, promoting its interaction with NCOA2/GRIP1.
PADI4 is also known as PAD, PAD4, PADI5, PDI4, PDI5.
