Search Results
Overview
| Uniprot ID | Q08257 |
|---|---|
| Protein Name | Zeta-crystallin |
| Gene Name | CRYZ |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 120 | TVYKLPEKLDFKQGA |
| 175 | IARAYGLKILGTAGT |
| 187 | AGTEEGQKIVLQNGA |
| 208 | REVNYIDKIKKYVGE |
| 23 | FGGPEVLKLRSDIAV |
| 307 | GSQYPLEKVAEAHEN |
| 34 | DIAVPIPKDHQVLIK |
| 6 | **MATGQKLMRAVRV |
| 62 | RSGTYSRKPLLPYTP |
Function
Multifunctional crystallin endowed with unrelated mRNA stabilization and enzymatic oxidoreductase activities (PubMed:17497241, PubMed:20103721). Binds (AU)-rich elements (ARE) in the 3'-UTR of target mRNA to enhance their stability (PubMed:17497241, PubMed:20103721). Upon metabolic acidosis, stabilizes the mRNA encoding SLC12A1 a cotransporter involved in transepithelial NH4(+) reabsorption in the medullary thick ascending limb in kidney (By similarity). In response to acidosis, also participates to the adaptive increase in renal ammoniagenesis by stabilizing the mRNAs of enzymes involved in glutamine catabolism (By similarity). By the same mechanism, it also regulates the expression of the antiapoptotic protein BCL2 (PubMed:20103721). Beside its mRNA stabilization activity, also catalyzes the reduction of orthoquinones such as 1,2-naphthoquinone or 9,10-phenanthrenequinone in the presence of NADPH in vitro and could be involved in the detoxification of xenobiotics and protection against oxidative stress (PubMed:17497241)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0003730 | mRNA 3'-UTR binding |
| Molecular Function | GO:0070402 | NADPH binding |
| Molecular Function | GO:0003960 | quinone reductase (NADPH) activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0048255 | mRNA stabilization |
| Biological Process | GO:0051289 | protein homotetramerization |
| Biological Process | GO:0007601 | visual perception |
| Biological Process | GO:0042178 | xenobiotic catabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.