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Q28452 (QOR_LAMGU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismLama guanicoe (Guanaco)
Taxonomic identifier9840 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaTylopodaCamelidaeLama

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 and enhances their stability. NADPH binding interferes with mRNA binding By similarity.

Catalytic activity

NADPH + 2 quinone = NADP+ + 2 semiquinone.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Quinone oxidoreductase
PRO_0000160907

Regions

Nucleotide binding158 – 1614NADP By similarity
Nucleotide binding246 – 2494NADP By similarity
Nucleotide binding269 – 2713NADP By similarity

Sites

Binding site531NADP By similarity
Binding site1811NADP; via amide nitrogen By similarity
Binding site2001NADP By similarity
Binding site2291NADP By similarity

Amino acid modifications

Modified residue231N6-acetyllysine By similarity
Modified residue2081N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28452 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E784E414D2BA23D6

FASTA33035,187
        10         20         30         40         50         60 
MATGQRLMRA IRVSEFGGPE VLKLQSDVAV PIPEEHQVLI KVQACGVNPV DTYIRSGTYS 

        70         80         90        100        110        120 
RKPRLPYTPG LDVAGLIEAV GERVSAFKKG DRVFTTSTVS GGYAEYALAA DHTVYKLPGE 

       130        140        150        160        170        180 
LDFQKGAAIG VPYFTAYRAL LHSACAKAGE SVLVHGASGG VGLAACQIAR ACCFKVLGTA 

       190        200        210        220        230        240 
GTEEGQRVVL QNGAHEVFNH REDINIDKIK KSVGEKGIDV IIEMLANVNL SNDLNLLSQG 

       250        260        270        280        290        300 
GRVIIVGSKG PVEINPRDTM TKESSIKGVT LFSSTKEEFQ QFAAALQAGM EIGWLRPVIG 

       310        320        330 
SQYPLEKVAQ AHEDLTHSSG AAGKVVLLLK 

« Hide

References

[1]"Evidence for independent recruitment of zeta-crystallin/quinone reductase (CRYZ) as a crystallin in camelids and hystricomorph rodents."
Gonzalez P., Rao P.V., Nunez S.B., Zigler J.S. Jr.
Mol. Biol. Evol. 12:773-781(1995) [PubMed: 7476124] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lens.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L34159 mRNA. Translation: AAA99986.1.

3D structure databases

ProteinModelPortalQ28452.
SMRQ28452. Positions 6-329.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG002466.

Family and domain databases

InterProIPR013149. 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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
PROSITEPS01162. QOR_ZETA_CRYSTAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQOR_LAMGU
AccessionPrimary (citable) accession number: Q28452
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: July 27, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families