CRYM Peptide - N-Terminal Region Blocking Peptide

Crystallins are separated into two classes: taxon-specific and ubiquitous. The former class is also called phylogenetically-restricted crystallins. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. This gene encodes a taxon-specific crystallin protein that binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. The encoded protein does not perform a structural role in lens tissue, and instead it binds thyroid hormone for possible regulatory or developmental roles. Mutations in this gene have been associated with autosomal dominant non-syndromic deafness. [provided by RefSeq, Sep 2014]

CRYM: Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors. Belongs to the ornithine cyclodeaminase family.

Protein type: Lyase; EC 1.5.1.25

Chromosomal Location of Human Ortholog: 16p12.2

Cellular Component: mitochondrion; cytoplasm; nucleus

Molecular Function: thiomorpholine-carboxylate dehydrogenase activity; protein homodimerization activity; NADP binding; transcription corepressor activity

Biological Process: sensory perception of sound; negative regulation of transcription from RNA polymerase II promoter; thyroid hormone metabolic process

Disease: Deafness, Autosomal Dominant 40