CRYM

CRYM
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2I99
Identifiers
Aliases	CRYM, DFNA40, THBP, crystallin mu
External IDs	MGI: 102675 HomoloGene: 1424 GeneCards: CRYM
Gene ontology Molecular function • oxidoreductase activity • hormone binding • protein binding • protein homodimerization activity • transcription corepressor activity • NADP binding • thyroid hormone binding • thiomorpholine-carboxylate dehydrogenase activity • oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Cellular component • cytoplasm • extracellular exosome • mitochondrion • nucleus • peroxisomal matrix • cytosol Biological process • thyroid hormone transport • negative regulation of transcription from RNA polymerase II promoter • oxidation-reduction process • sensory perception of sound • lysine catabolic process • thyroid hormone metabolic process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1428	12971
Ensembl	ENSG00000103316	ENSMUSG00000030905
UniProt	Q14894	O54983
RefSeq (mRNA)	NM_001014444 NM_001888	NM_016669
RefSeq (protein)	NP_001879	NP_057878
Location (UCSC)	Chr 16: 21.24 – 21.3 Mb	Chr 7: 120.19 – 120.2 Mb
PubMed search

2I99

1428

12971

ENSG00000103316

ENSMUSG00000030905

Q14894

O54983

NM_001014444
NM_001888

NM_016669

NP_001879

NP_057878

Mu-crystallin homolog also known as NADP-regulated thyroid-hormone-binding protein (THBP) is a protein that in humans is encoded by the CRYM gene. Multiple alternatively spliced transcript variants have been found for this gene.

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.

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