AlphaFold predicted structure
CRYM · Q14894
Mean pLDDT
96.1/ 100
Very high
314 residues
Confidence breakdown
- Very high(≥ 90)94%
- Confident(70–90)3%
- Low(50–70)3%
- Very low(< 50)0%
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AlphaFold (Jumper et al., 2021) · CC BY 4.0
CRYM
Chr 16p12.2crystallin mu
- Aliases:
- DFNA40
- MANE:
- ENST00000572914.2
Annotations refreshed 9 hours ago.
Predicted protein structure
Clinical relevance (Genomics England PanelApp)
Diagnostic Grade (Green)
Monogenic hearing loss
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown
Disease associations (Open Targets)
autosomal dominant nonsyndromic hearing loss 40
0.63autosomal dominant nonsyndromic hearing loss
0.37liver disorder
0.24diabetes mellitus
0.12posterior cortical atrophy
0.08familial thyroid dyshormonogenesis
0.08hyperthyroxinemia
0.08gastric cancer
0.06thyroid hormone metabolism, abnormal 1
0.06glioblastoma
0.06
Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.
Protein function (UniProt)
Ketimine reductase mu-crystallin
Catalyzes the NAD(P)H-dependent reduction of imine double bonds of a number of cyclic ketimine substrates, including sulfur-containing cyclic ketimines (PubMed:21332720, PubMed:25931162). Under physiological conditions, it efficiently catalyzes delta(1)-piperideine-2-carboxylate (P2C) and delta(1)-pyrroline-2-carboxylate (Pyr2C) reduction, suggesting a central role in lysine and glutamate metabolism (PubMed:25931162). Additional substrates are delta(2)-thiazoline-2-carboxylate (T2C), 3,4-dehydrothiomorpholine-3-carboxylate (AECK), and (R)-lanthionine ketimine (LK) that is reduced at very low rate compared to other substrates (PubMed:25931162). Also catalyzes the NAD(P)H-dependent reduction of (S)-cystathionine ketimine (CysK) (By similarity)