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Reviewed, UniProtKB/Swiss-Prot P11415 (QOR_CAVPO)

Last modified November 25, 2008. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismCavia porcellus (Guinea pig)
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

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

In guinea pigs it constitutes about 10% of the water soluble proteins of the lens.

Involvement in disease

A genomic mutation causing the deletion of 34 amino acids was clearly associated with a hereditary nuclear cataract in a line of strain 13 guinea pigs.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Ontologies

Keywords

   Cellular componentCytoplasm
Eye lens protein
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNADPH:quinone reductase activity

Inferred from electronic annotation. Source: EC

structural constituent of eye lens

Inferred from electronic annotation. Source: UniProtKB-KW

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_0000160905

Sequences

Sequence LengthMass (Da)Tools
P11415-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 1463632C672C234F

FASTA32935,202
        10         20         30         40         50         60 
MATGQKLMRA IRVFEFGGPE VLKVQSDVAV PIPKDHQVLI KVHACGINPV ETYIRSGTYT 

        70         80         90        100        110        120 
RIPLLPYTPG TDVAGVVESI GNDVSAFKKG DRVFTTSTIS GGYAEYALAS DHTVYRLPEK 

       130        140        150        160        170        180 
LDFRQGAAIG IPYFTACRAL FHSARAKAGE SVLVHGASGG VGLAACQIAR AYGLKVLGTA 

       190        200        210        220        230        240 
GTEEGQKVVL QNGAHEVFNH RDAHYIDEIK KSIGEKGVDV IIEMLANVNL SNDLKLLSCG 

       250        260        270        280        290        300 
GRVIIVGCRG SIEINPRDTM AKESTISGVS LFSSTKEEFQ QFASTIQAGM ELGWVKPVIG 

       310        320 
SQYPLEKASQ AHENIIHSSG TVGKTVLLM 

« Hide

References

[1]"Zeta-crystallin, a novel protein from the guinea pig lens is related to alcohol dehydrogenases."
Rodokanaki A., Holmes R.K., Borras T.
Gene 78:215-224(1989) [PubMed: 2777081] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Purification and characterization of zeta-crystallin/quinone reductase from guinea pig liver."
Rao P.V., Zigler J.S. Jr.
Biochim. Biophys. Acta 1117:315-320(1992) [PubMed: 1420281] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Liver.
[3]"Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase."
Rao P.V., Krishna C.M., Zigler J.S. Jr.
J. Biol. Chem. 267:96-102(1992) [PubMed: 1370456] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Liver.

Cross-references

Sequence databases

M26936 mRNA. Translation: AAA37035.1.
PIRCYGPZ. JS0230.

3D structure databases

HSSPHSSP built from PDB template 1JVB based on UniProtKB P39462.
SMRP11415. Positions 6-329.
ModBaseSearch...

Genome annotation databases

EnsemblENSCPOG00000006521. Cavia porcellus. [Contig view]

Phylogenomic databases

HOVERGENP11415.

Family and domain databases

InterProIPR013154. AlcDHase_GroES-like.
IPR002085. AlcDHase_SF_Zn.
IPR013149. AlcDHase_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...

Entry information

Entry nameQOR_CAVPO
AccessionPrimary (citable) accession number: P11415
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 25, 2008
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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