[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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 (By similarity).
CATALYTIC ACTIVITY: NADPH + quinone = NADP⁺ + semiquinone.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BC078927; AAH78927.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001012183.1; -.

UniGene

Rn.6746

3D structure databases

SMR

Q6AYT0; 6-329.

ModBase

Q6AYT0.

Organism-specific databases

RGD

1311639; Cryz.

Gene expression databases

ArrayExpress

Q6AYT0; -.

GermOnline

ENSRNOG00000028319; Rattus norvegicus.

Ontologies

GO:0003960;	Molecular function: NADPH:quinone reductase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR016040; NAD(P)-bd.
IPR002364; Quin_OxRdtase/zeta-crystal_CS.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS01162; QOR_ZETA_CRYSTAL; 1.

BLOCKS

Q6AYT0.

Genome annotation databases

Ensembl

ENSRNOG00000028319; Rattus norvegicus. [Contig view]

GeneID

362061; -.

KEGG

rno:362061; -.

NMPDR

fig|10116.3.peg.17202; -.

Phylogenomic databases

HOVERGEN

Q6AYT0; -.

Other

ProtoNet

Q6AYT0.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 329`	`329`		`Quinone oxidoreductase.`	`PRO_0000160910`

Sequence information

Length: 329 AA [This is the length of the unprocessed precursor]

Molecular weight: 34975 Da [This is the MW of the unprocessed precursor]

CRC64: 02BD613047BF4B04 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATGQKLMRA IRVFEFGGPE VLKLQSDVVV PAPQSHQVLI KVHACGVNPV ETYIRSGTYS 

        70         80         90        100        110        120 
RKPALPYTPG SDVAGIIESV GDGVSAFKKG DRVFCFSTVS GGYAEFALSA DNTTYPLPET 

       130        140        150        160        170        180 
LDFRQGAALG IPYFTACRAL FHSARARAGE SVLVHGASGG VGLATCQIAR AHGLKVLGTA 

       190        200        210        220        230        240 
GSEEGKKLVL QNGAHEVFNH KEANYIDKIK TSAGDKGVDV IIEMLANKNL SNDLKLLSCG 

       250        260        270        280        290        300 
GRVIVVGCRG SIEINPRDTM AKETSIIGVS LFSSTKEEFQ QFAGILQAGI EKGWVKPVIG 

       310        320 
SEYPLEKAAQ AHEDIIHSSG KMGKMILLL

Q6AYT0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools