Reviewed, UniProtKB/Swiss-Prot Q61578 (ADRO_MOUSE)

Names and origin

Protein names

Recommended name:
    NADPH:adrenodoxin oxidoreductase, mitochondrial
      Short name=Adrenodoxin reductase
      Short name=AR
    EC=1.18.1.2
Alternative name(s):
    Ferredoxin--NADP(+) reductase
      Short name=Ferredoxin reductase

Gene names

Name:

Fdxr

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	494 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	Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.
Catalytic activity	2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.
Cofactor	FAD.
Pathway	Steroid metabolism; cholesterol metabolism.
Subunit structure	Monomer. Interacts directly with FDX1 By similarity.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Expressed in the adrenal, testis and ovary and to a lesser extent in the liver and kidney.
Sequence similarities	Belongs to the ferredoxin--NADP reductase type 1 family.

Ontologies

Keywords
Biological process	Cholesterol metabolism Electron transport Lipid metabolism Steroid metabolism Transport
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	cholesterol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ferredoxin-NADP+ reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 34	34	Mitochondrion Potential
	Chain	35 – 494	460	NADPH:adrenodoxin oxidoreductase, mitochondrial		PRO_0000019421
Regions
	Nucleotide binding	187 – 190	4	NADP By similarity
	Nucleotide binding	231 – 232	2	NADP By similarity
	Nucleotide binding	408 – 410	3	FAD By similarity
Sites
	Binding site	51	1	FAD; via amide nitrogen By similarity
	Binding site	72	1	FAD By similarity
	Binding site	80	1	FAD; via amide nitrogen By similarity
	Binding site	116	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	243	1	NADP By similarity
	Binding site	401	1	FAD; via amide nitrogen By similarity
	Binding site	408	1	NADP; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q61578-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4BD279DFC606A5C5	FASTA	494	54,202
	10 20 30 40 50 60 MAPRCWHWWR WSAWSGLRPS PSRSTPTPGF CQKFSTQEKT PQICVVGSGP AGFYTAQHLL 70 80 90 100 110 120 KHHTHAHVDI YEKQLVPFGL VRFGVAPDHP EVKNVINTFT QTARSDRCAF QGNVVVGRDV 130 140 150 160 170 180 SVPELREAYH AVVLSYGAED HQPLGIPGEE LPGVVSARAF VGWYNGLPEN QELAPDLSCD 190 200 210 220 230 240 TAVILGQGNV ALDVARILLT PPEHLEKTDI TEAALGALRQ SRVKTVWIVG RRGPLQVAFT 250 260 270 280 290 300 IKELREMIQL PGTRPILDPS DFLGLQDRIK DVPRPRRRLT ELLLRTATEK PGVEEAARQA 310 320 330 340 350 360 LASRAWGLRF FRSPQQVLPT PDGQRVAGIR LAVTSLEGVG ESTRAVPTGD VEDLPCGLLL 370 380 390 400 410 420 SSVGYKSRPI DPSVPFDPKL GVIPNTEGRV VNVPGLYCSG WVKRGPTGVI TTTMTDSFLT 430 440 450 460 470 480 SQALLEDLKA GLLPSGPRPG YVAIQALLSN RGVRPVSFSD WEKLDAEEVS RGQGTGKPRE 490 KLVDRREMLR LLGH

References

[1]	"cDNA cloning of mouse ferredoxin reductase from kidney." Itoh S., Iemura O., Yamada E., Yoshimura T., Tsujikawa K., Kohama Y., Mimura T. Biochim. Biophys. Acta 1264:159-162(1995) [PubMed: 7495857] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D49920 mRNA. Translation: BAA08659.1.
IPI	IPI00453981.
PIR	S60028.
RefSeq	NP_032023.1.
UniGene	Mm.4719
3D structure databases
SMR	Q61578. Positions 40-494.
ModBase	Search...
Protein-protein interaction databases
STRING	Q61578.
2-D gel databases
REPRODUCTION-2DPAGE	Q61578.
Proteomic databases
PRIDE	Q61578.
Genome annotation databases
Ensembl	ENSMUST00000021078; ENSMUSP00000021078; ENSMUSG00000018861; Mus musculus. [Genome view]
GeneID	14149.
KEGG	mmu:14149.
NMPDR	fig|10090.3.peg.25604.
UCSC	uc007mgy.1. mouse.
Organism-specific databases
CTD	14149.
MGI	MGI:104724. Fdxr.
Phylogenomic databases
HOVERGEN	Q61578.
InParanoid	Q61578.
OMA	DRIKEVP.
OrthoDB	EOG9C5G48.
PhylomeDB	Q61578.
Enzyme and pathway databases
BRENDA	1.18.1.2. 244.
Gene expression databases
ArrayExpress	Q61578.
Bgee	Q61578.
CleanEx	MM_FDXR.
Genevestigator	Q61578.
GermOnline	ENSMUSG00000018861. Mus musculus.
Family and domain databases
InterPro	IPR000759. Adrndx_reductase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. [Graphical view]
Pfam	PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00419. ADXRDTASE.
ProtoNet	Search...
Other Resources
NextBio	285258.
SOURCE	Search...

Entry information

Entry name

ADRO_MOUSE

Accession

Primary (citable) accession number: Q61578

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)