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P00389 (NCPR_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
NADPH--cytochrome P450 reductase
Short name=CPR
Short name=P450R
EC=1.6.2.4

Cleaved into the following chain:

  1. NADPH--cytochrome P450 reductase, N-terminally processed
Gene names
Name:POR
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length679 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 679679NADPH--cytochrome P450 reductase
PRO_0000167599
Initiator methionine11Removed; alternate By similarity
Chain2 – 679678NADPH--cytochrome P450 reductase, N-terminally processed
PRO_0000421789

Regions

Domain81 – 225145Flavodoxin-like
Domain280 – 522243FAD-binding FR-type
Nucleotide binding171 – 20232FMN By similarity
Nucleotide binding315 – 32612FAD By similarity
Nucleotide binding452 – 46211FAD By similarity
Nucleotide binding530 – 54819NADP By similarity
Nucleotide binding625 – 64117NADP By similarity

Amino acid modifications

Modified residue21N-acetylalanine
Modified residue5761Phosphotyrosine By similarity

Experimental info

Sequence conflict40 – 412YW → NY AA sequence Ref.2
Sequence conflict531E → N AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00389 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: B1A163FA53A5988B

FASTA67976,588
        10         20         30         40         50         60 
MADSHGDTGA TMPEAAAQEA SVFSMTDVVL FSLIVGLITY WFLFRKKKEE VPEFTKIQAP 

        70         80         90        100        110        120 
TSSSVKESSF VEKMKKTGRN IVVFYGSQTG TAEEFANRLS KDAHRYGMRG MAADPEEYDL 

       130        140        150        160        170        180 
ADLSSLPEIN NALAVFCMAT YGEGDPTDNA QDFYDWLQET DVDLSGVKYA VFGLGNKTYE 

       190        200        210        220        230        240 
HFNAMGKYVD QRLEQLGAQR IFELGMGDDD ANLEEDFITW REQFWPAVCE HFGVEATGEE 

       250        260        270        280        290        300 
SSIRQYELVL HTDIDVAKVY QGEMGRLKSY ENQKPPFDAK NPFLATVTTN RKLNQGTERH 

       310        320        330        340        350        360 
LMHLELDISD SKIRYESGDH VAVYPANDSA LVNQLGEILG ADLDVVMSLN NLDEESNKKH 

       370        380        390        400        410        420 
PFPCPTSYRT ALTYYLDITN PPRTNVLYEL AQYAADPAEQ EQLRKMASSS GEGKELYLSW 

       430        440        450        460        470        480 
VVEARRHILA ILQDYPSLRP PIDHLCELLP RLQARYYSIA SSSKVHPNSV HICAVAVEYE 

       490        500        510        520        530        540 
TKAGRLNKGV ATSWLRAKEP AGENGGRALV PMFVRKSQFR LPFKATTPVI MVGPGTGVAP 

       550        560        570        580        590        600 
FIGFIQERAW LRQQGKEVGE TLLYYGCRRA AEDYLYREEL AGFQKDGTLS QLNVAFSREQ 

       610        620        630        640        650        660 
AQKVYVQHLL RRDKEHLWRL IHEGGAHIYV CGDARNMARD VQNTFYDIVA ELGAMEHAQA 

       670 
VDYVKKLMTK GRYSLDVWS

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-81.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D00101 mRNA. Translation: BAA00063.1.
X04610 mRNA. Translation: CAA28279.1.
PIRA25505.
RefSeqNP_001153762.1. NM_001160290.1.
UniGeneOcu.2197.

3D structure databases

ProteinModelPortalP00389.
SMRP00389. Positions 65-679.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000020921.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100301554.

Organism-specific databases

CTD5447.

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHOG000282027.
HOVERGENHBG000432.
OrthoDBEOG46HG96.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14302.

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.
IPR023208. P450R.
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]
PIRSFPIRSF000208. P450R. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNCPR_RABIT
AccessionPrimary (citable) accession number: P00389
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 3, 2013
This is version 108 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

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