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P08165 (ADRO_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. 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·Interactions·Alt products·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
Synonyms:ADXR
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.7

Cofactor

FAD.

Pathway

Steroid metabolism; cholesterol metabolism.

Subunit structure

Monomer. Interacts directly with FDX1.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FDX1P002572EBI-593948,EBI-593992
isiBP0A3E03EBI-593948,EBI-593907From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Short (identifier: P08165-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Long (identifier: P08165-2)

The sequence of this isoform differs from the canonical sequence as follows:
     204-204: E → EVLLLCQ
Note: Represents 10-20% of all adrenodoxin reductase mRNAs and seems to be inactive.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion Ref.6 Ref.7 Ref.8
Chain33 – 492460NADPH:adrenodoxin oxidoreductase, mitochondrial
PRO_0000019419

Regions

Nucleotide binding185 – 1884NADP
Nucleotide binding229 – 2302NADP
Nucleotide binding406 – 4083FAD

Sites

Binding site491FAD; via amide nitrogen
Binding site701FAD
Binding site781FAD; via amide nitrogen
Binding site1141FAD; via amide nitrogen and carbonyl oxygen
Binding site2411NADP
Binding site3991FAD; via amide nitrogen
Binding site4061NADP; via amide nitrogen

Natural variations

Alternative sequence2041E → EVLLLCQ in isoform Long.
VSP_003415

Experimental info

Sequence conflict421C → S AA sequence Ref.6
Sequence conflict771G → R in AAA30362. Ref.2
Sequence conflict81 – 9414FGVAP…VKNVI → VWLALTTPRSRMLL Ref.2
Sequence conflict124 – 1285QDAYH → RVYRLT in AAA30362. Ref.2
Sequence conflict2681K → R in AAA30362. Ref.2
Sequence conflict317 – 3182PS → RL in AAA30362. Ref.2
Sequence conflict323 – 33311RAAGIRLAVTR → ARRSAWQSPE in AAA30362. Ref.2
Sequence conflict341 – 35212TRAVP…DVEDL → HPGSAHWGCGGP in AAA30362. Ref.2
Sequence conflict488 – 4892RL → TM AA sequence Ref.6
Sequence conflict4911G → R in AAX46664. Ref.5

Secondary structure

.............................................................................. 492
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Short [UniParc].

Last modified July 15, 1998. Version 3.
Checksum: E68F6F5D18F53131

FASTA49254,338
        10         20         30         40         50         60 
MAPRCWRWWP WSSWTRTRLP PSRSIQNFGQ HFSTQEQTPQ ICVVGSGPAG FYTAQHLLKH 

        70         80         90        100        110        120 
HSRAHVDIYE KQLVPFGLVR FGVAPDHPEV KNVINTFTQT ARSDRCAFYG NVEVGRDVTV 

       130        140        150        160        170        180 
QELQDAYHAV VLSYGAEDHQ ALDIPGEELP GVFSARAFVG WYNGLPENRE LAPDLSCDTA 

       190        200        210        220        230        240 
VILGQGNVAL DVARILLTPP DHLEKTDITE AALGALRQSR VKTVWIVGRR GPLQVAFTIK 

       250        260        270        280        290        300 
ELREMIQLPG TRPMLDPADF LGLQDRIKEA ARPRKRLMEL LLRTATEKPG VEEAARRASA 

       310        320        330        340        350        360 
SRAWGLRFFR SPQQVLPSPD GRRAAGIRLA VTRLEGIGEA TRAVPTGDVE DLPCGLVLSS 

       370        380        390        400        410        420 
IGYKSRPIDP SVPFDPKLGV VPNMEGRVVD VPGLYCSGWV KRGPTGVITT TMTDSFLTGQ 

       430        440        450        460        470        480 
ILLQDLKAGH LPSGPRPGSA FIKALLDSRG VWPVSFSDWE KLDAEEVSRG QASGKPREKL 

       490 
LDPQEMLRLL GH 

« Hide

Isoform Long [UniParc].

Checksum: BB3238129E92F3D1
Show »

FASTA49855,008

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of adrenodoxin reductase cDNA from bovine adrenal cortex."
Sagara Y., Takata Y., Miyata T., Hara T., Horiuchi T.
J. Biochem. 102:1333-1336(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Molecular cloning and sequence analysis of full-length cDNA for mRNA of adrenodoxin oxidoreductase from bovine adrenal cortex."
Nonaka Y., Murakami H., Yabusaki Y., Kuramitsu S., Kagamiyama H., Yamano T., Okamoto M.
Biochem. Biophys. Res. Commun. 145:1239-1247(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases."
Hanukoglu I., Gutfinger T.
Eur. J. Biochem. 180:479-484(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal cortex.
[4]"Gene structure of bovine adrenodoxin reductase."
Takata Y., Sagara Y., Kono A., Sekimizu K., Horiuchi T.
Biol. Pharm. Bull. 16:1200-1206(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[5]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Adrenoferredoxin-binding peptide of NADPH-adrenoferredoxin reductase."
Hamamoto I., Kurokohchi K., Tanaka S., Ichikawa Y.
Biochim. Biophys. Acta 953:207-213(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-62; 254-276 AND 487-492.
[7]"Structural and functional characterization of bovine adrenodoxin reductase by limited proteolysis."
Warburton R.J., Seybert D.W.
Biochim. Biophys. Acta 1246:39-46(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-51 AND 298-320, CATALYTIC ACTIVITY.
[8]"Isolation of a cDNA for adrenodoxin reductase (ferredoxin-NADP+ reductase). Implications for mitochondrial cytochrome P-450 systems."
Hanukoglu I., Gutfinger T., Haniu M., Shively J.E.
Eur. J. Biochem. 169:449-455(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE.
Tissue: Adrenal cortex.
[9]"The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis."
Ziegler G.A., Vonrhein C., Hanukoglu I., Schulz G.E.
J. Mol. Biol. 289:981-990(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 33-492 IN COMPLEX WITH FAD.
[10]"Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family."
Ziegler G.A., Schulz G.E.
Biochemistry 39:10986-10995(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 33-492 IN COMPLEX WITH NADP.
[11]"Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis."
Mueller J.J., Lapko A., Bourenkov G., Ruckpaul K., Heinemann U.
J. Biol. Chem. 276:2786-2789(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-492 IN COMPLEX WITH FDX1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17029 mRNA. Translation: AAA30362.1.
D00211 mRNA. Translation: BAA00150.1.
X13736 mRNA. Translation: CAA32002.1.
D83475 Genomic DNA. Translation: BAA11921.1.
BT021817 mRNA. Translation: AAX46664.1.
PIRJT0751.
RefSeqNP_777116.1. NM_174691.1.
UniGeneBt.64647.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CJCX-ray1.70A33-492[»]
1E1KX-ray1.95A33-492[»]
1E1LX-ray2.30A33-492[»]
1E1MX-ray1.85A33-492[»]
1E1NX-ray2.40A33-492[»]
1E6EX-ray2.30A/C33-492[»]
ProteinModelPortalP08165.
SMRP08165. Positions 36-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08165. 2 interactions.

Proteomic databases

PRIDEP08165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID282604.
KEGGbta:282604.

Organism-specific databases

CTD2232.

Phylogenomic databases

eggNOGCOG0493.
HOGENOMHOG000249250.
HOVERGENHBG002132.
InParanoidP08165.
KOK00528.

Enzyme and pathway databases

SABIO-RKP08165.
UniPathwayUPA00296.

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

EvolutionaryTraceP08165.
NextBio20806310.

Entry information

Entry nameADRO_BOVIN
AccessionPrimary (citable) accession number: P08165
Secondary accession number(s): Q58CY0, Q95KN8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 142 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways