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P19618 (NCPR_SALTR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH--cytochrome P450 reductase

Short name=CPR
Short name=P450R
EC=1.6.2.4
OrganismSalmo trutta (Brown trout)
Taxonomic identifier8032 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeSalmo

Protein attributes

Sequence length601 AA.
Sequence statusFragments.
Protein existenceEvidence 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 componentEndoplasmic reticulum
Membrane
   LigandFAD
Flavoprotein
FMN
NADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionFMN binding

Inferred from electronic annotation. Source: InterPro

NADPH-hemoprotein reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 601›601NADPH--cytochrome P450 reductase
PRO_0000167601

Regions

Domain25 – 169145Flavodoxin-like
Domain224 – 425202FAD-binding FR-type

Experimental info

Non-adjacent residues426 – 4272
Non-adjacent residues434 – 4352
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P19618 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: BC801767DE1D44C9

FASTA60168,305
        10         20         30         40         50         60 
KLDQPAPSTQ ETSFIEKMKK TGRNIVVFYG SQTGTGEEFA NRLSKDAHRY GMGSMAADPE 

        70         80         90        100        110        120 
EYDMSELSRL AEIGNSLAIF CMATYGEGDP TDNAQDFYDW LQETDGQLSG VNYPVFALGD 

       130        140        150        160        170        180 
KTYEHYNAMG AYVDKRLEEL GAKRVFDLGM GDDDGNLEED FVTWREQFWP AMCEHFGVEA 

       190        200        210        220        230        240 
SGEDSSVRQY ELKEHNDINM NKVYTGELGR LKSFETQKPP FDAKNPFLAP VTVNRKLNKA 

       250        260        270        280        290        300 
GELHKMHLEV DITGSKIRYE SGDHVAVYPT NNTVIVNRLG QILGVDLDSV ISLNNLDEES 

       310        320        330        340        350        360 
NKKHPFPCPT TYRTALTHYL DIIHPPRTNV LYELAQYATD LKDQENTDSM ASSAPEGKAL 

       370        380        390        400        410        420 
YQSFVLEDNR NILAILEDLP SLRPPIDHLC ELMPRLQARY YSIASSSKVH PNSIHICAVL 

       430        440        450        460        470        480 
VEYXTKGVAT TWLKYIRKSQ FRLPFKASNP VIMVGPGTGI APFMGFIQER GWLKESGKEV 

       490        500        510        520        530        540 
GETVLYCGCR HKEEDYLYQE ELEQAHKKGA LTKLNVAFSR EQDQKVYVQH LLRKNKVDLW 

       550        560        570        580        590        600 
RQIHEDYAHI YICGDARNMA RDVQTAFYEI AEELGGMTRT QATDYIKKLM TKGRYSQDVW 


S 

« Hide

References

[1]"Structural comparison between the trout and mammalian hydrophilic domain of NADPH-cytochrome P-450 reductase."
Urenjak J., Linder D., Lumper L.
J. Chromatogr. A 397:123-136(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRA28577.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000432.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNCPR_SALTR
AccessionPrimary (citable) accession number: P19618
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 16, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families