CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014870
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Quinone oxidoreductase 
Protein Synonyms/Alias
 NADPH:quinone reductase; Zeta-crystallin 
Gene Name
 Cryz 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
6**MATGQKLMRAIRVacetylation[1]
23FGGPEVLKLQSDVVVacetylation[1]
88GDGVSAFKKGDRVFCacetylation[1]
175IARAHGLKVLGTAGSacetylation[1]
186TAGSEEGKKLVLQNGacetylation[1]
187AGSEEGKKLVLQNGAacetylation[1]
201AHEVFNHKEANYIDKacetylation[1]
208KEANYIDKIKTSAGDacetylation[1]
210ANYIDKIKTSAGDKGacetylation[1]
216IKTSAGDKGVDVIIEacetylation[1]
228IIEMLANKNLSNDLKacetylation[1]
235KNLSNDLKLLSCGGRacetylation[1]
296GIEKGWVKPVIGSEYacetylation[1]
307GSEYPLEKAAQAHEDacetylation[1]
321DIIHSSGKMGKMILLacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 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). 
Sequence Annotation
 NP_BIND 158 161 NADP (By similarity).
 NP_BIND 246 249 NADP (By similarity).
 NP_BIND 269 271 NADP (By similarity).
 BINDING 53 53 NADP (By similarity).
 BINDING 181 181 NADP; via amide nitrogen (By similarity).
 BINDING 200 200 NADP (By similarity).
 BINDING 229 229 NADP (By similarity).
 MOD_RES 23 23 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; NADP; Oxidoreductase; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 329 AA 
Protein Sequence
MATGQKLMRA IRVFEFGGPE VLKLQSDVVV PAPQSHQVLI KVHACGVNPV ETYIRSGTYS 60
RKPALPYTPG SDVAGIIESV GDGVSAFKKG DRVFCFSTVS GGYAEFALSA DNTTYPLPET 120
LDFRQGAALG IPYFTACRAL FHSARARAGE SVLVHGASGG VGLATCQIAR AHGLKVLGTA 180
GSEEGKKLVL QNGAHEVFNH KEANYIDKIK TSAGDKGVDV IIEMLANKNL SNDLKLLSCG 240
GRVIVVGCRG SIEINPRDTM AKETSIIGVS LFSSTKEEFQ QFAGILQAGI EKGWVKPVIG 300
SEYPLEKAAQ AHEDIIHSSG KMGKMILLL 329 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
 GO:0070402; F:NADPH binding; ISS:UniProtKB.
 GO:0003960; F:NADPH:quinone reductase activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0042178; P:xenobiotic catabolic process; ISS:UniProtKB. 
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. 
Pfam
 PF08240; ADH_N
 PF00107; ADH_zinc_N 
SMART
  
PROSITE
 PS01162; QOR_ZETA_CRYSTAL 
PRINTS