Q28452 (QOR_LAMGU) Reviewed, UniProtKB/Swiss-Prot
Last modified
July 27, 2011.
Version 55.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Quinone oxidoreductase EC=1.6.5.5 Alternative name(s): NADPH:quinone reductase Zeta-crystallin | ||
| Gene names |
| ||
| Organism | Lama guanicoe (Guanaco) | ||
| Taxonomic identifier | 9840 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Tylopoda › Camelidae › Lama |
Protein attributes
| Sequence length | 330 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript 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 By similarity. |
| Catalytic activity | NADPH + 2 quinone = NADP+ + 2 semiquinone. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | NADP RNA-binding |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| 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 activityInferred from sequence or structural similarity. Source: UniProtKB mRNA 3'-UTR bindingInferred from sequence or structural similarity. Source: UniProtKB zinc ion bindingInferred 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 – 330 | 330 | Quinone oxidoreductase | PRO_0000160907 | |||||
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 | ||||||
| Modified residue | 208 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Evidence for independent recruitment of zeta-crystallin/quinone reductase (CRYZ) as a crystallin in camelids and hystricomorph rodents." Gonzalez P., Rao P.V., Nunez S.B., Zigler J.S. Jr. Mol. Biol. Evol. 12:773-781(1995) [PubMed: 7476124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L34159 mRNA. Translation: AAA99986.1. |
3D structure databases | |
| ProteinModelPortal | Q28452. |
| SMR | Q28452. Positions 6-329. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG002466. |
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_LAMGU | ||||||||
| Accession | Primary (citable) accession number: Q28452 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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