Reviewed,
UniProtKB/Swiss-Prot P56522 (ADRO_RAT)
Last modified
October 13, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: NADPH:adrenodoxin oxidoreductase, mitochondrial Short name=Adrenodoxin reductase Short name=AR EC=1.18.1.2 Alternative name(s): Ferredoxin--NADP(+) reductase Short name=Ferredoxin reductase | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 494 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver. |
| Catalytic activity | 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH. |
| Cofactor | FAD. |
| Pathway | |
| Subunit structure | Monomer. Interacts directly with FDX1 By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the ferredoxin--NADP reductase type 1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cholesterol metabolism Electron transport Lipid metabolism Steroid metabolism Transport |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cholesterol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW electron transport chainInferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NADPH-adrenodoxin reductase activity Ref.1 Inferred from direct assay. Source: RGD electron carrier activityInferred from electronic annotation. Source: InterPro ferredoxin-NADP+ reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 34 | 34 | Mitochondrion | ||||||
| Chain | 35 – 494 | 460 | NADPH:adrenodoxin oxidoreductase, mitochondrial | PRO_0000019422 | |||||
Regions | |||||||||
| Nucleotide binding | 187 – 190 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 231 – 232 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 408 – 410 | 3 | FAD By similarity | ||||||
Sites | |||||||||
| Binding site | 51 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 72 | 1 | FAD By similarity | ||||||
| Binding site | 80 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 116 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 243 | 1 | NADP By similarity | ||||||
| Binding site | 401 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 408 | 1 | NADP; via amide nitrogen By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "cDNA cloning, overproduction and characterization of rat adrenodoxin reductase." Sagara Y., Watanabe Y., Kodama H., Aramaki H. Biochim. Biophys. Acta 1434:284-295(1999) [PubMed: 10525147] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-54. Strain: Wistar. Tissue: Adrenal gland. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| D63761 mRNA. Translation: BAA23759.1. BC088844 mRNA. Translation: AAH88844.1. | |
| IPI | IPI00193379. |
| RefSeq | NP_077067.1. |
| UniGene | Rn.10860 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CJC based on UniProtKB P08165. |
| SMR | P56522. Positions 40-494. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P56522. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000004592; ENSRNOP00000004592; ENSRNOG00000003387; Rattus norvegicus. [Genome view] |
| GeneID | 79122. |
| KEGG | rno:79122. |
Organism-specific databases | |
| CTD | 79122. |
| RGD | 621648. Fdxr. |
Phylogenomic databases | |
| HOVERGEN | P56522. |
Enzyme and pathway databases | |
| BRENDA | 1.18.1.2. 248. |
Gene expression databases | |
| ArrayExpress | P56522. |
| Genevestigator | P56522. |
| GermOnline | ENSRNOG00000003387. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000759. Adrndx_reductase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. [Graphical view] |
| Pfam | PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00419. ADXRDTASE. |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 614546. |
Entry information
| Entry name | ADRO_RAT | ||||||||
| Accession | Primary (citable) accession number: P56522 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


