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Reviewed, UniProtKB/Swiss-Prot Q08257 (QOR_HUMAN)

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

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Quinone oxidoreductase
    EC=1.6.5.5
Alternative name(s):
    NADPH:quinone reductase
    Zeta-crystallin
Gene names
Name: CRYZ
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

visual perception

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADPH:quinone reductase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Quinone oxidoreductase
PRO_0000160906

Natural variations

Natural variant661P → S: dbSNP rs11551729. Ref.4
VAR_022913
Natural variant1761I → V: dbSNP rs3819946. Ref.3
VAR_022914
Natural variant1831E → K: dbSNP rs17095822.
VAR_048200

Secondary structure

......................................................... 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08257-1 [UniParc].

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

FASTA32935,207
        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

References

« Hide '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.

Cross-references

Sequence databases

L13278 mRNA. Translation: AAA36536.1.
L31526 expand/collapse EMBL AC list , 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.
BC039578 mRNA. Translation: AAH39578.1.
BC070058 mRNA. Translation: AAH70058.1.
IPIIPI00000792.
PIRPN0448.
RefSeqNP_001123514.1.
NP_001123515.1.
NP_001880.2.
UniGeneHs.83114

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1YB5X-ray1.85A/B1-329[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ08257. 2 interactions.

PTM databases

PhosphoSiteQ08257.

2-D gel databases

REPRODUCTION-2DPAGEIPI00000792.

Proteomic databases

PRIDEQ08257.

Genome annotation databases

EnsemblENSG00000116791. Homo sapiens. [Contig view]
GeneID1429.
KEGGhsa:1429.
UCSCuc001dgj.1. human.

Organism-specific databases

GeneCardsGC01M074883.
H-InvDBHIX0023567.
HGNCHGNC:2419. CRYZ.
MIM123691. gene.
PharmGKBPA26925.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ08257.
HOVERGENQ08257.
OMAQ08257. DTMAKES.

Enzyme and pathway databases

BRENDA1.6.5.5. 247.

Gene expression databases

ArrayExpressQ08257.
BgeeQ08257.
CleanExHS_CRYZ.
GermOnlineENSG00000116791. Homo sapiens.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002364. Quin_OxRdtase/zeta-crystal_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS01162. QOR_ZETA_CRYSTAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00266. Dicumarol.
NextBio5829.
SOURCESearch...

Entry information

Entry nameQOR_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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