CRYZ

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Crystallin, zeta (quinone reductase)
PDB rendering based on 1yb5.
Available structures: 1yb5
Identifiers
Symbol(s) CRYZ; DKFZp779E0834; FLJ41475
External IDs OMIM: 123691 MGI: 88527 HomoloGene: 68210
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 1429 12972
Ensembl ENSG00000116791 ENSMUSG00000028199
Uniprot Q08257 Q3UYY0
Refseq NM_001889 (mRNA)
NP_001880 (protein)		 NM_009968 (mRNA)
NP_034098 (protein)
Location Chr 1: 74.94 - 74.97 Mb Chr 3: 154.53 - 154.56 Mb
Pubmed search [1] [2]

Crystallin, zeta (quinone reductase), also known as CRYZ, is a human gene.[1]

Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. The former class is also called phylogenetically-restricted crystallins. This gene encodes a taxon-specific crystallin protein which has NADPH-dependent quinone reductase activity distinct from other known quinone reductases. It lacks alcohol dehydrogenase activity although by similarity it is considered a member of the zinc-containing alcohol dehydrogenase family. Unlike other mammalian species, in humans, lens expression is low. One pseudogene is known to exist.[1]

[edit] References

  1. ^ a b Entrez Gene: CRYZ crystallin, zeta (quinone reductase).

[edit] Further reading

  • Heinzmann C, Kojis TL, Gonzalez P, et al. (1995). "Assignment of the zeta-crystallin gene (CRYZ) to human chromosome 1p22-p31 and identification of restriction fragment length polymorphisms.". Genomics 23 (2): 403-7. doi:10.1006/geno.1994.1516. PMID 7835889. 
  • Gonzalez P, Rao PV, Zigler JS (1994). "Organization of the human zeta-crystallin/quinone reductase gene (CRYZ).". Genomics 21 (2): 317-24. doi:10.1006/geno.1994.1272. PMID 8088825. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298. 
  • Gonzalez P, Rao PV, Zigler JS (1993). "Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver.". Biochem. Biophys. Res. Commun. 191 (3): 902-7. doi:10.1006/bbrc.1993.1302. PMID 8466529. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149. 
  • Wang W, Liu LQ, Higuchi CM, Chen H (1998). "Induction of NADPH:quinone reductase by dietary phytoestrogens in colonic Colo205 cells.". Biochem. Pharmacol. 56 (2): 189-95. PMID 9698072. 
  • Goenka S, Raman B, Ramakrishna T, Rao CM (2001). "Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation.". Biochem. J. 359 (Pt 3): 547-56. PMID 11672428. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Bianco NR, Perry G, Smith MA, et al. (2004). "Functional implications of antiestrogen induction of quinone reductase: inhibition of estrogen-induced deoxyribonucleic acid damage.". Mol. Endocrinol. 17 (7): 1344-55. doi:10.1210/me.2002-0382. PMID 12714703. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334. 
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