Cingulin-like 1
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Cingulin-like 1
Cingulin-like protein 1, also known as paracingulin or junction-associated-coiled-coil protein (JACOP), is a protein which is encoded by the ''CGNL1'' gene. The paracingulin polypeptide comprises a globular N-terminal "head" domain and an α-helical C-terminal domain which is presumed to form a coiled-coil dimer. Paracingulin is a paralog of cingulin that arose probably from gene duplication. The CGNL1 gene is conserved among different vertebrate species and has not been so far identified in invertebrates. The homology search highlights that paracingulin and cingulin have 39% identity in the rod tail sequences. They possess also two highly homologous regions in their N-terminus “head” domain including the ZIM region (ZO-1 interaction motif). The etymology of the name cingulin comes from the Latin "cingere" which means « to form a belt around ». Both, cingulin and paracingulin are localized in the cytoplasmic face of tight junctions (TJ). The prefix « para » refers to “p ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ...
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