Reviewed,
UniProtKB/Swiss-Prot P37039 (NCPR_CAVPO)
Last modified
October 13, 2009.
Version 75.
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 | Cavia porcellus (Guinea pig) | ||
| Taxonomic identifier | 10141 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia |
Protein attributes
| Sequence length | 678 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript 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. |
| Caution | Was originally (Ref.1) thought to originate from mouse. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Membrane |
| Ligand | FAD FMN Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 678 | 677 | NADPH--cytochrome P450 reductase | PRO_0000167595 | |||||
Regions | |||||||||
| Domain | 80 – 224 | 145 | Flavodoxin-like | ||||||
| Domain | 279 – 521 | 243 | FAD-binding FR-type | ||||||
| Nucleotide binding | 170 – 201 | 32 | FMN By similarity | ||||||
| Nucleotide binding | 314 – 325 | 12 | FAD By similarity | ||||||
| Nucleotide binding | 451 – 461 | 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-acetylglycine By similarity | ||||||
| Modified residue | 575 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
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References
| [1] | "Molecular cloning and sequence analysis of guinea-pig NADPH-cytochrome P-450 oxidoreductase." Ohgiya S., Goda T., Ishizaki K., Kamataki T., Shinriki N. Biochim. Biophys. Acta 1171:103-105(1992) [PubMed: 1420354] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Hartley. |
| [2] | Erratum Ohgiya S., Goda T., Ishizaki K., Kamataki T., Shinriki N. Biochim. Biophys. Acta 1174:313-313(1993) [PubMed: 8373812] [Abstract] |
Cross-references
Sequence databases | |
|---|---|
| D10498 mRNA. Translation: BAA01385.1. | |
| PIR | S27158. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AMO based on UniProtKB P00388. |
| SMR | P37039. Positions 64-678. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P37039. |
Genome annotation databases | |
| Ensembl | ENSCPOT00000006266; ENSCPOP00000005592; ENSCPOG00000006202; Cavia porcellus. [Genome view] |
Phylogenomic databases | |
| HOVERGEN | P37039. |
Enzyme and pathway databases | |
| BRENDA | 1.6.2.4. 44. |
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_CAVPO | ||||||||
| Accession | Primary (citable) accession number: P37039 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


