Reviewed,
UniProtKB/Swiss-Prot P04175 (NCPR_PIG)
Last modified
June 16, 2009.
Version 83.
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 |
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| Organism | Sus scrofa (Pig) | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
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 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 membrane Inferred 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 Ref.2 | ||||||
| Chain | 2 – 678 | 677 | NADPH--cytochrome P450 reductase | PRO_0000167598 | |||||
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 | 529 – 547 | 19 | NADP By similarity | ||||||
| Nucleotide binding | 624 – 640 | 17 | NADP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylglycine Ref.2 | ||||||
| Modified residue | 575 | 1 | Phosphotyrosine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 55 | 1 | S → T in AAA85368. Ref.2 | ||||||
| Sequence conflict | 164 | 1 | T → S in AAA85368. Ref.2 | ||||||
| Sequence conflict | 175 | 1 | N → D AA sequence Ref.3 | ||||||
| Sequence conflict | 340 | 1 | T → A AA sequence Ref.3 | ||||||
| Sequence conflict | 379 | 1 | N → D AA sequence Ref.3 | ||||||
| Sequence conflict | 401 | 1 | Q → E AA sequence Ref.3 | ||||||
| Sequence conflict | 447 | 1 | R → L in AAA85368. Ref.2 | ||||||
| Sequence conflict | 503 | 1 | N → D AA sequence Ref.3 | ||||||
| Sequence conflict | 509 | 1 | V → L AA sequence Ref.2 | ||||||
| Sequence conflict | 509 | 1 | V → L AA sequence Ref.3 | ||||||
| Sequence conflict | 675 | 1 | D → N AA sequence Ref.3 | ||||||
Sequences
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References
| [1] | Amborn J., Preiss B., Stender B., Viale M., Repp R.Z., Lampert F., Kroger M., Lumper L. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Complete amino acid sequence of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes." Haniu M., Iyanagi T., Miller P., Lee T.D., Shively J.E. Biochemistry 25:7906-7911(1986) [PubMed: 3099837] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-678, ACETYLATION AT GLY-2. |
| [3] | "Complete structure of the hydrophilic domain in the porcine NADPH-cytochrome P-450 reductase." Vogel F., Lumper L. Biochem. J. 236:871-878(1986) [PubMed: 3098240] [Abstract] Cited for: PROTEIN SEQUENCE OF 57-678. |
Cross-references
Sequence databases | |
|---|---|
| L33893 mRNA. Translation: AAA85368.1. | |
| PIR | RDPGO4. A25584. |
| RefSeq | NP_001123431.1. |
| UniGene | Ssc.50299 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1B1C based on UniProtKB P16435. |
| SMR | P04175. Positions 64-678. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100170114. |
| KEGG | ssc:100170114. |
Phylogenomic databases | |
| HOVERGEN | P04175. |
Enzyme and pathway databases | |
| BRENDA | 1.6.2.4. 249. |
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_PIG | ||||||||
| Accession | Primary (citable) accession number: P04175 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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