Q08257 (QOR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Quinone oxidoreductase
EC=1.6.5.5

Alternative name(s):
NADPH:quinone reductase
Zeta-crystallin

Gene names

Name:

CRYZ

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding. Ref.6 Ref.8
Catalytic activity	NADPH + 2 quinone = NADP+ + 2 semiquinone. Ref.6
Subunit structure	Homotetramer. Ref.6
Subcellular location	Cytoplasm Ref.8.
Tissue specificity	Only very low amounts in the lens.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NADP RNA-binding
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein homotetramerization Inferred from physical interaction Ref.6. Source: UniProtKB visual perception Traceable author statement. Source: ProtInc xenobiotic catabolic process Inferred from direct assay Ref.6. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA cytosol Inferred from direct assay Ref.6. Source: UniProtKB
Molecular function	NADPH binding Inferred from direct assay Ref.6. Source: UniProtKB NADPH:quinone reductase activity Inferred from direct assay Ref.6. Source: UniProtKB mRNA 3'-UTR binding Inferred from direct assay Ref.6. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 329

329

Quinone oxidoreductase

PRO_0000160906

Regions

Nucleotide binding

158 – 161

4

NADP

Nucleotide binding

246 – 249

4

NADP

Nucleotide binding

269 – 271

3

NADP

Sites

Binding site

53

1

NADP

Binding site

181

1

NADP; via amide nitrogen

Binding site

200

1

NADP

Binding site

229

1

NADP

Amino acid modifications

Modified residue

23

1

N6-acetyllysine Ref.7

Modified residue

208

1

N6-acetyllysine Ref.7

Natural variations

Natural variant

66

1

P → S. Ref.5
Corresponds to variant rs11551729 [ dbSNP | Ensembl ].

VAR_022913

Natural variant

176

1

I → V. Ref.3
Corresponds to variant rs3819946 [ dbSNP | Ensembl ].

VAR_022914

Natural variant

183

1

E → K.
Corresponds to variant rs17095822 [ dbSNP | Ensembl ].

VAR_048200

Secondary structure

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329

Helix Strand Turn

Details...

Beta strand

7 – 15

9

Helix

19 – 21

3

Beta strand

22 – 29

8

Beta strand

37 – 46

10

Helix

49 – 55

7

Beta strand

65 – 67

3

Beta strand

73 – 80

8

Beta strand

92 – 96

5

Beta strand

102 – 110

9

Helix

111 – 113

3

Beta strand

114 – 116

3

Helix

123 – 126

4

Turn

127 – 129

3

Helix

130 – 141

12

Beta strand

151 – 156

6

Helix

160 – 171

12

Beta strand

175 – 182

8

Helix

183 – 191

9

Beta strand

195 – 199

5

Helix

205 – 213

9

Beta strand

218 – 224

7

Helix

226 – 236

11

Beta strand

237 – 245

9

Beta strand

252 – 254

3

Helix

257 – 260

4

Turn

261 – 263

3

Beta strand

265 – 268

4

Helix

271 – 273

3

Helix

276 – 292

17

Beta strand

299 – 304

6

Helix

305 – 307

3

Helix

308 – 317

10

Beta strand

322 – 328

7

Sequences

	Sequence		Length	Mass (Da)
	Q08257 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 68C1828911486D4E	FASTA	329	35,207
	10 20 30 40 50 60 MATGQKLMRA VRVFEFGGPE VLKLRSDIAV PIPKDHQVLI KVHACGVNPV ETYIRSGTYS 70 80 90 100 110 120 RKPLLPYTPG SDVAGVIEAV GDNASAFKKG DRVFTSSTIS GGYAEYALAA DHTVYKLPEK 130 140 150 160 170 180 LDFKQGAAIG IPYFTAYRAL IHSACVKAGE SVLVHGASGG VGLAACQIAR AYGLKILGTA 190 200 210 220 230 240 GTEEGQKIVL QNGAHEVFNH REVNYIDKIK KYVGEKGIDI IIEMLANVNL SKDLSLLSHG 250 260 270 280 290 300 GRVIVVGSRG TIEINPRDTM AKESSIIGVT LFSSTKEEFQ QYAAALQAGM EIGWLKPVIG 310 320 SQYPLEKVAE AHENIIHGSG ATGKMILLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver." Gonzalez P., Rao P.V., Zigler J.S. Jr. Biochem. Biophys. Res. Commun. 191:902-907(1993) [PubMed: 8466529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Organization of the human zeta-crystallin/quinone reductase gene (CRYZ)." Gonzalez P., Rao P.V., Zigler J.S. Jr. Genomics 21:317-324(1994) [PubMed: 8088825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[3]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-176. Tissue: Brain, Kidney proximal tubule and Lung.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-66. Tissue: Testis.
[6]	"Human and yeast zeta-crystallins bind AU-rich elements in RNA." Fernandez M.R., Porte S., Crosas E., Barbera N., Farres J., Biosca J.A., Pares X. Cell. Mol. Life Sci. 64:1419-1427(2007) [PubMed: 17497241] [Abstract] Cited for: FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23 AND LYS-208, MASS SPECTROMETRY.
[8]	"{zeta}-Crystallin is a bcl-2 mRNA binding protein involved in bcl-2 overexpression in T-cell acute lymphocytic leukemia." Lapucci A., Lulli M., Amedei A., Papucci L., Witort E., Di Gesualdo F., Bertolini F., Brewer G., Nicolin A., Bevilacqua A., Schiavone N., Morello D., Donnini M., Capaccioli S. FASEB J. 24:1852-1865(2010) [PubMed: 20103721] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Crystal structure of human zeta-crystallin at 1.85 A." Structural genomics consortium (SGC) Submitted (MAR-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH NADP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L13278 mRNA. Translation: AAA36536.1.
L31526 , L31521, L31522, L31523, L31524, L31525 Genomic DNA. Translation: AAK40311.1.
AB209714 mRNA. Translation: BAD92951.1.
AK223150 mRNA. Translation: BAD96870.1.
AK223201 mRNA. Translation: BAD96921.1.
CH471059 Genomic DNA. Translation: EAX06410.1.
CH471059 Genomic DNA. Translation: EAX06411.1.
CH471059 Genomic DNA. Translation: EAX06412.1.
BC039578 mRNA. Translation: AAH39578.1.
BC070058 mRNA. Translation: AAH70058.1.

IPI

IPI00000792.

PIR

PN0448.

RefSeq

NP_001123514.1. NM_001130042.1.
NP_001123515.1. NM_001130043.1.
NP_001128231.1. NM_001134759.1.
NP_001880.2. NM_001889.3.

UniGene

Hs.83114.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YB5	X-ray	1.85	A/B	1-329	[»]

ProteinModelPortal

Q08257.

SMR

Q08257. Positions 6-329.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q08257. 1 interaction.

STRING

Q08257.

PTM databases

PhosphoSite

Q08257.

Polymorphism databases

DMDM

585013.

2D gel databases

REPRODUCTION-2DPAGE

IPI00000792.

Proteomic databases

PRIDE

Q08257.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000340866; ENSP00000339399; ENSG00000116791.
ENST00000417775; ENSP00000399805; ENSG00000116791.

GeneID

1429.

KEGG

hsa:1429.

UCSC

uc001dgj.1. human.

Organism-specific databases

CTD

1429.

GeneCards

GC01M075171.

H-InvDB

HIX0023567.

HGNC

HGNC:2419. CRYZ.

HPA

HPA021921.
HPA023290.

MIM

123691. gene.

neXtProt

NX_Q08257.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17325.

GeneTree

ENSGT00550000074483.

HOGENOM

HBG753318.

HOVERGEN

HBG002466.

InParanoid

Q08257.

OMA

DTMAKES.

OrthoDB

EOG4Q2DFW.

PhylomeDB

Q08257.

Gene expression databases

Bgee

Q08257.

CleanEx

HS_CRYZ.

Genevestigator

Q08257.

GermOnline

ENSG00000116791. Homo sapiens.

Family and domain databases

InterPro

IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR002364. Quin_OxRdtase/zeta-crystal_CS.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

KO

K00344.

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]

SUPFAM

SSF50129. GroES_like. 1 hit.

PROSITE

PS01162. QOR_ZETA_CRYSTAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00266. Dicumarol.

NextBio

5829.

SOURCE

Search...

Entry information

Entry name

QOR_HUMAN

Accession

Primary (citable) accession number: Q08257
Secondary accession number(s): D3DQ76 , Q53FT0, Q59EU7, Q6NSK9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.