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Q61578 (ADRO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:adrenodoxin oxidoreductase, mitochondrial

Short name=AR
Short name=Adrenodoxin reductase
EC=1.18.1.6
Alternative name(s):
Ferredoxin--NADP(+) reductase
Short name=Ferredoxin reductase
Gene names
Name:Fdxr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 adrenodoxin + NADP+ = 2 oxidized adrenodoxin + 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion Potential
Chain35 – 494460NADPH:adrenodoxin oxidoreductase, mitochondrial
PRO_0000019421

Regions

Nucleotide binding187 – 1904NADP By similarity
Nucleotide binding231 – 2322NADP By similarity
Nucleotide binding408 – 4103FAD By similarity

Sites

Binding site511FAD; via amide nitrogen By similarity
Binding site721FAD By similarity
Binding site801FAD; via amide nitrogen By similarity
Binding site1161FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2431NADP By similarity
Binding site4011FAD; via amide nitrogen By similarity
Binding site4081NADP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q61578 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4BD279DFC606A5C5

FASTA49454,202
        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 

« Hide

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] [Europe PMC] [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.
PIRS60028.
RefSeqNP_032023.1. NM_007997.1.
UniGeneMm.4719.

3D structure databases

ProteinModelPortalQ61578.
SMRQ61578. Positions 40-494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ61578. 1 interaction.
MINTMINT-151907.

PTM databases

PhosphoSiteQ61578.

2D gel databases

REPRODUCTION-2DPAGEQ61578.

Proteomic databases

PaxDbQ61578.
PRIDEQ61578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021078; ENSMUSP00000021078; ENSMUSG00000018861.
GeneID14149.
KEGGmmu:14149.
UCSCuc007mgy.1. mouse.

Organism-specific databases

CTD2232.
MGIMGI:104724. Fdxr.

Phylogenomic databases

eggNOGCOG0493.
GeneTreeENSGT00390000013574.
HOVERGENHBG002132.
InParanoidQ61578.
KOK00528.
OMAVGYKSRP.
OrthoDBEOG7H1JJX.
TreeFamTF314193.

Enzyme and pathway databases

UniPathwayUPA00296.

Gene expression databases

BgeeQ61578.
CleanExMM_FDXR.
GenevestigatorQ61578.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR021163. Adrenodoxin_Rdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFPIRSF000362. FNR. 1 hit.
ProtoNetSearch...

Other

NextBio285258.
PROQ61578.
SOURCESearch...

Entry information

Entry nameADRO_MOUSE
AccessionPrimary (citable) accession number: Q61578
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot