Reviewed, UniProtKB/Swiss-Prot P00389 (NCPR_RABIT)

Names and origin

Protein names

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

Gene names

Name:

POR

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 membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred 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

	Sequence		Length	Mass (Da)
	P00389-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: B1A163FA53A5988B	FASTA	679	76,588
	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

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
EMBLGenBankDDBJ	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

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	October 13, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)