Seroatlas · Protein domains

Protein kinase C-like, phorbol ester/diacylglycerol-binding domain

IPR002219

Definition

This entry represents the N-terminal region of PKC, known as C1. It has been shown to bind PE and DAG in a phospholipid and zinc-dependent fashion PMID:2500657. The C1 region contains one or two copies (depending on the isozyme of PKC) of a cysteine-rich domain, which is about 50 amino-acid residues long, and which is essential for DAG/PE-binding. The DAG/PE-binding domain binds two zinc ions; the ligands of these metal ions are probably the six cysteines and two histidines that are conserved in this domain. Protein kinase C (PKC) is a family of serine/threonine protein kinases found in eukaryotic organisms, including humans, animals, and fungi. These enzymes play crucial roles in various signal transduction cascades, regulating cellular processes such as gene expression, protein secretion, cell proliferation, and inflammatory responses PMID:7499357. PKCs are activated by second messengers, primarily diacylglycerol (DAG) PMID:1396661. The PKC family comprises multiple isozymes, categorised into three subfamilies: conventional, novel, and atypical, based on their second messenger requirements PMID:18923184. Structurally, PKCs consist of a regulatory domain and a catalytic domain connected by a hinge region PMID:21215369. The regulatory domain typically contains C1 [interpro:IPR002219] and C2 domain, which are responsible for DAG and calcium binding. The catalytic domain [interpro:IPR000719], highly conserved among PKC isozymes, contains the ATP- and substrate-binding sites.

65 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.

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