Quinone oxidoreductase - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q08257 (QOR_HUMAN)

Last modified July 7, 2009. Version 86. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones are the best substrates. May act in the detoxification of xenobiotics.
Catalytic activity	NADPH + 2 quinone = NADP⁺ + 2 semiquinone.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Tissue specificity	Only very low amounts in the lens.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW visual perception Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADPH:quinone reductase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 329

329

Quinone oxidoreductase

PRO_0000160906

Natural variations

Natural variant

P → S: dbSNP rs11551729. Ref.4

VAR_022913

Natural variant

176

I → V: dbSNP rs3819946. Ref.3

VAR_022914

Natural variant

183

E → K: dbSNP rs17095822.

VAR_048200

Secondary structure

329

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q08257-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 68C1828911486D4E
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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

« Hide

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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]	"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.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"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).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

L13278 mRNA. Translation: AAA36536.1.
L31526

L31525 Genomic DNA. Translation: AAK40311.1.
AB209714 mRNA. Translation: BAD92951.1.
AK223150 mRNA. Translation: BAD96870.1.
AK223201 mRNA. Translation: BAD96921.1.
BC039578 mRNA. Translation: AAH39578.1.
BC070058 mRNA. Translation: AAH70058.1.

IPI

IPI00000792.

PIR

PN0448.

RefSeq

NP_001123514.1.
NP_001123515.1.
NP_001880.2.

UniGene

Hs.83114

3D structure databases

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

ModBase

Search...

Protein-protein interaction databases

IntAct

Q08257. 2 interactions.

PTM databases

PhosphoSite

Q08257.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00000792.

Proteomic databases

PRIDE

Q08257.

Genome annotation databases

Ensembl

ENSG00000116791. Homo sapiens. [Contig view]

GeneID

1429.

KEGG

hsa:1429.

UCSC

uc001dgj.1. human.

Organism-specific databases

GeneCards

GC01M074883.

H-InvDB

HIX0023567.

HGNC

HGNC:2419. CRYZ.

MIM

123691. gene.

PharmGKB

PA26925.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q08257.

HOVERGEN

Q08257.

OMA

Q08257. DTMAKES.

Enzyme and pathway databases

BRENDA

1.6.5.5. 247.

Gene expression databases

ArrayExpress

Q08257.

Bgee

Q08257.

CleanEx

HS_CRYZ.

GermOnline

ENSG00000116791. Homo sapiens.

Family and domain databases

InterPro

IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002364. Quin_OxRdtase/zeta-crystal_CS.
[Graphical view]

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

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

PROSITE

PS01162. QOR_ZETA_CRYSTAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00266. Dicumarol.

NextBio

5829.

SOURCE

Search...

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Entry information

Entry name

QOR_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	July 7, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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