P11415 (QOR_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Quinone oxidoreductase
EC=1.6.5.5

Alternative name(s):
NADPH:quinone reductase
Zeta-crystallin

Gene names

Name:

CRYZ

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. Ref.2 Ref.3
Catalytic activity	NADPH + 2 quinone = NADP+ + 2 semiquinone. Ref.2 Ref.3
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	Note=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 component	Cytoplasm
Ligand	NADP RNA-binding
Molecular function	Eye lens protein Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	xenobiotic catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	NADPH binding Inferred from sequence or structural similarity. Source: UniProtKB NADPH:quinone reductase activity Inferred from sequence or structural similarity. Source: UniProtKB mRNA 3'-UTR binding Inferred from sequence or structural similarity. Source: UniProtKB 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 329	329	Quinone oxidoreductase		PRO_0000160905
Regions
	Nucleotide binding	158 – 161	4	NADP By similarity
	Nucleotide binding	246 – 249	4	NADP By similarity
	Nucleotide binding	269 – 271	3	NADP By similarity
Sites
	Binding site	53	1	NADP By similarity
	Binding site	181	1	NADP; via amide nitrogen By similarity
	Binding site	200	1	NADP By similarity
	Binding site	229	1	NADP By similarity
Amino acid modifications
	Modified residue	23	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P11415 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 1463632C672C234F	FASTA	329	35,202
	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

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: FUNCTION, CATALYTIC ACTIVITY. 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: FUNCTION, CATALYTIC ACTIVITY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M26936 mRNA. Translation: AAA37035.1.
PIR	CYGPZ. JS0230.
RefSeq	NP_001166407.1. NM_001172936.1.
3D structure databases
ProteinModelPortal	P11415.
SMR	P11415. Positions 6-329.
ModBase	Search...
Protein-protein interaction databases
STRING	P11415.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSCPOT00000006587; ENSCPOP00000005873; ENSCPOG00000006521.
GeneID	100135507.
Organism-specific databases
CTD	1429.
Phylogenomic databases
eggNOG	roNOG06296.
GeneTree	ENSGT00550000074483.
HOVERGEN	HBG002466.
InParanoid	P11415.
OMA	DTMAKES.
OrthoDB	EOG4Q2DFW.
Family and domain databases
InterPro	IPR013149. 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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
SUPFAM	SSF50129. GroES_like. 1 hit.
PROSITE	PS01162. QOR_ZETA_CRYSTAL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

QOR_CAVPO

Accession

Primary (citable) accession number: P11415

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	July 27, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program