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Mu-crystallin homolog

Cat. No.: CBCRY14
Background: 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. Multiple alternatively spliced transcript variants have been found for this gene.
Protein Classification: Oxidoreductase
Structure Weight: 68589.65 Da
Polymer: 1
Molecule: Mu-crystallin homolog
Chain Length: 312 amino acids
PDB ID: 2I99
MMDB ID: 44495
Source: E.coli
Method: X-Ray Diffraction
Resolution: 2.6Å
Ligand Chemical Component: NAD
Reference: Cheng, Z., Sun, L., He, J., Gong, W.(2007) Crystal structure of human {micro}-crystallin complexed with NADPHProtein Sci.16: 329-335
Gene Name: CRYM
Synonyms: DFNA40; THBP; NADP-regulated thyroid-hormone binding protein; OTTHUMP00000115878; dfna40; crystallin mu
UniProt ID: Q14894
Gene ID: 1428
Chromosome Location: 16p13.11-p12.3
Function: NADP or NADPH binding; catalytic activity; thyroid hormone binding; transcription corepressor activity

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