NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lens;
PubMed=7476124 [NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez P., Rao P.V., Nunez S.B., Zigler J.S. Jr.;
"Evidence for independent recruitment of zeta-crystallin/quinone reductase (CRYZ) as a crystallin in camelids and hystricomorph rodents.";
Mol. Biol. Evol. 12:773-781(1995).

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

Copyright

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Cross-references

Sequence databases

EMBL

L34159; AAA99986.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P28304; 1QOR. [HSSP ENTRY / PDB]

SMR

Q28452; 6-329.

ModBase

Q28452.

Family and domain databases

InterPro

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

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

Q28452.

Phylogenomic databases

HOVERGEN

Q28452; -.

Other

ProtoNet

Q28452.

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`	`1 330`	`330`		`Quinone oxidoreductase.`	`PRO_0000160907`

Sequence information

Length: 330 AA [This is the length of the unprocessed precursor]

Molecular weight: 35187 Da [This is the MW of the unprocessed precursor]

CRC64: E784E414D2BA23D6 [This is a checksum on the sequence]

        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

Q28452 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