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Protein

Quinone oxidoreductase

Gene

CRYZ

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

NADPH + 2 quinone = NADP+ + 2 semiquinone.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531NADPBy similarity
Binding sitei181 – 1811NADP; via amide nitrogenBy similarity
Binding sitei200 – 2001NADPBy similarity
Binding sitei229 – 2291NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 1614NADPBy similarity
Nucleotide bindingi246 – 2494NADPBy similarity
Nucleotide bindingi269 – 2713NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein, Oxidoreductase

Keywords - Ligandi

NADP, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Quinone oxidoreductase (EC:1.6.5.5)
Alternative name(s):
NADPH:quinone reductase
Zeta-crystallin
Gene namesi
Name:CRYZ
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 329328Quinone oxidoreductasePRO_0000160905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei23 – 231N6-acetyllysineBy similarity
Modified residuei296 – 2961N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP11415.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000005873.

Structurei

3D structure databases

ProteinModelPortaliP11415.
SMRiP11415. Positions 6-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1197. Eukaryota.
COG0604. LUCA.
GeneTreeiENSGT00550000074483.
HOGENOMiHOG000294672.
HOVERGENiHBG002466.
InParanoidiP11415.
KOiK00344.
OMAiPIPKGHQ.
OrthoDBiEOG7BGHM8.
TreeFamiTF314255.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
IPR002364. Quin_OxRdtase/zeta-crystal_CS.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS01162. QOR_ZETA_CRYSTAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11415-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATGQKLMRA IRVFEFGGPE VLKVQSDVAV PIPKDHQVLI KVHACGINPV
60 70 80 90 100
ETYIRSGTYT RIPLLPYTPG TDVAGVVESI GNDVSAFKKG DRVFTTSTIS
110 120 130 140 150
GGYAEYALAS DHTVYRLPEK LDFRQGAAIG IPYFTACRAL FHSARAKAGE
160 170 180 190 200
SVLVHGASGG VGLAACQIAR AYGLKVLGTA GTEEGQKVVL QNGAHEVFNH
210 220 230 240 250
RDAHYIDEIK KSIGEKGVDV IIEMLANVNL SNDLKLLSCG GRVIIVGCRG
260 270 280 290 300
SIEINPRDTM AKESTISGVS LFSSTKEEFQ QFASTIQAGM ELGWVKPVIG
310 320
SQYPLEKASQ AHENIIHSSG TVGKTVLLM
Length:329
Mass (Da):35,202
Last modified:October 1, 1989 - v1
Checksum:i1463632C672C234F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26936 mRNA. Translation: AAA37035.1.
PIRiJS0230. CYGPZ.
RefSeqiNP_001166407.1. NM_001172936.1.
XP_005007806.1. XM_005007749.2.
XP_012998113.1. XM_013142659.1.

Genome annotation databases

EnsembliENSCPOT00000006587; ENSCPOP00000005873; ENSCPOG00000006521.
GeneIDi100135507.
KEGGiag:AAA37035.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26936 mRNA. Translation: AAA37035.1.
PIRiJS0230. CYGPZ.
RefSeqiNP_001166407.1. NM_001172936.1.
XP_005007806.1. XM_005007749.2.
XP_012998113.1. XM_013142659.1.

3D structure databases

ProteinModelPortaliP11415.
SMRiP11415. Positions 6-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000005873.

Proteomic databases

PRIDEiP11415.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCPOT00000006587; ENSCPOP00000005873; ENSCPOG00000006521.
GeneIDi100135507.
KEGGiag:AAA37035.

Organism-specific databases

CTDi1429.

Phylogenomic databases

eggNOGiKOG1197. Eukaryota.
COG0604. LUCA.
GeneTreeiENSGT00550000074483.
HOGENOMiHOG000294672.
HOVERGENiHBG002466.
InParanoidiP11415.
KOiK00344.
OMAiPIPKGHQ.
OrthoDBiEOG7BGHM8.
TreeFamiTF314255.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
IPR002364. Quin_OxRdtase/zeta-crystal_CS.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS01162. QOR_ZETA_CRYSTAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
    Tissue: Liver.
  4. "A guinea-pig hereditary cataract contains a splice-site deletion in a crystallin gene."
    Rodriguez I.R., Gonzalez P., Zigler J.S. Jr., Borras T.
    Biochim. Biophys. Acta 1180:44-52(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CATARACT.

Entry informationi

Entry nameiQOR_CAVPO
AccessioniPrimary (citable) accession number: P11415
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 11, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.