Functional and structural characteristics of Caspase Recruitment Domain Protein 18 (CARD18)

Target Name: CARD18

NCBI ID: G59082

CARD18

Functional and structural characteristics of Caspase Recruitment Domain Protein 18 (CARD18)

Caspase recruitment domain protein 18 (CARD18) is a protein that is expressed in various cell types, including neurons, muscle cells, and immune cells. It is a key regulator of the caspase-dependent cell death pathway , which is a critical mechanism for cell suicide in response to DNA damage, viruses, and other stressors.

CARD18 is a member of the Bcl-2 family of proteins, which are known for their ability to regulate cell death. The Bcl-2 family of proteins are composed of at least 12 different isoforms, including Bcl-2, Bcl-3, Bcl -4, Bcl-5, Bcl-6, Bcl-7, Bcl-8, Bcl-9, Bcl-10, Bcl-11, and Bcl-12. These proteins share a conserved domain that includes a leucine-rich repeat ( LRR) and a variable region (V) that is unique to each isoform.

CARD18 is a 21-kDa protein that is expressed in a variety of tissues, including brain, spinal cord, muscle, and blood cells. It is primarily localized to the endoplasmic reticulum (ER) and is also found in the cytoplasm. CARD18 is a monomer that consists of a unique N-terminal region, a catalytic domain, and a C-terminal region that is involved in its cell surface localization and interactions.

The catalytic domain of CARD18 consists of a parallel beta-sheet structure that is characterized by a central transmembrane region and two distinct alpha-helices that are involved in the regulation of cellular processes, including cell death. The transmembrane region of CARD18 is composed of a unique arrangement of amino acids that is specific to this protein and is involved in the formation of a complex with other molecules, including Bcl-2 and Bcl-3.

The C-terminal region of CARD18 is involved in its interactions with other molecules, including neighboring

Protein Name: Caspase Recruitment Domain Family Member 18

Functions: Inhibits generation of IL-1-beta by interacting with caspase-1 and preventing its association with RIP2. Down-regulates the release of IL1B

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