Protein-arginine deiminase (PAD), N-terminal

Definition

This entry represents the first immunoglobulin-like non-catalytic domain of protein-arginine deiminase. Protein arginine deiminases (PADs) use a nucleophilic cysteine to hydrolyze guanidinium groups on arginine residues to form citrulline. This reaction, known as citrullination or deimination, results in the loss of positive charge, thereby affecting protein function and altering protein-protein and protein-nucleic acid interactions. Humans encode five PADs, designated PADs 1-4 and PAD6, which regulate numerous cellular processes. PADs are dysregulated in inflammatory diseases and cancer PMID:25621824. PAD6 does not bind Ca2+ and is inactive in vitro assays against standard PADs substrate PMID:39286527. The PAD2 monomer consists of two immunoglobulin-like domains, IgG1 (residues 1-115) and IgG2 (residues 116-295), as well as a C-terminal catalytic domain (residues 296-665) PMID:25621824.

5 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (5 proteins: gene, accession, name)

• PADI1
• PADI2
• PADI3
• PADI4
• PADI6