Reviewed,
UniProtKB/Swiss-Prot P00389 (NCPR_RABIT)
Last modified
October 13, 2009.
Version 82.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: NADPH--cytochrome P450 reductase Short name=CPR Short name=P450R EC=1.6.2.4 | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 679 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. |
| Catalytic activity | NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein. |
| Cofactor | FAD. FMN. |
| Subcellular location | Endoplasmic reticulum membrane; Peripheral membrane protein. Note: Anchored to the ER membrane by its N-terminal hydrophobic region. |
| Sequence similarities | In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Membrane |
| Ligand | FAD FMN Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activityInferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro iron 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 – 679 | 679 | NADPH--cytochrome P450 reductase | PRO_0000167599 | |||||
Regions | |||||||||
| Domain | 81 – 225 | 145 | Flavodoxin-like | ||||||
| Domain | 280 – 522 | 243 | FAD-binding FR-type | ||||||
| Nucleotide binding | 171 – 202 | 32 | FMN By similarity | ||||||
| Nucleotide binding | 315 – 326 | 12 | FAD By similarity | ||||||
| Nucleotide binding | 452 – 462 | 11 | FAD By similarity | ||||||
| Nucleotide binding | 530 – 548 | 19 | NADP By similarity | ||||||
| Nucleotide binding | 625 – 641 | 17 | NADP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine | ||||||
| Modified residue | 576 | 1 | Phosphotyrosine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 40 – 41 | 2 | YW → NY AA sequence Ref.2 | ||||||
| Sequence conflict | 53 | 1 | E → N AA sequence Ref.2 | ||||||
Sequences
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References
| [1] | "Molecular cloning and sequence analysis of full-length cDNA for rabbit liver NADPH-cytochrome P-450 reductase mRNA." Katagiri M., Murakami H., Yabusaki Y., Sugiyama T., Okamoto M., Yamano T., Ohkawa H. J. Biochem. 100:945-954(1986) [PubMed: 3029050] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region." Black S.D., Coon M.J. J. Biol. Chem. 257:5929-5938(1982) [PubMed: 6802823] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF 1-81. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| D00101 mRNA. Translation: BAA00063.1. X04610 mRNA. Translation: CAA28279.1. | |
| PIR | A25505. |
| RefSeq | NP_001153762.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1B1C based on UniProtKB P16435. |
| SMR | P00389. Positions 65-679. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100301554. |
Phylogenomic databases | |
| HOVERGEN | P00389. |
Enzyme and pathway databases | |
| BRENDA | 1.6.2.4. 255. |
Family and domain databases | |
| InterPro | IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin-like. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR015702. NADPH_Cyt_P450_Rdtase. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view] |
| PANTHER | PTHR19384:SF17. NADPH_Cyt_Red. 1 hit. |
| Pfam | PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00369. FLAVODOXIN. PR00371. FPNCR. |
| PROSITE | PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NCPR_RABIT | ||||||||
| Accession | Primary (citable) accession number: P00389 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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