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P22570 (ADRO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length491 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.

Cofactor

FAD.

Pathway

Steroid metabolism; cholesterol metabolism.

Subunit structure

Monomer. Interacts directly with FDX1 By similarity.

Subcellular location

Mitochondrion matrix.

Sequence similarities

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

Ontologies

Keywords
   Biological processCholesterol metabolism
Electron transport
Lipid metabolism
Steroid metabolism
Sterol metabolism
Transport
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNADPH oxidation

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

generation of precursor metabolites and energy

Traceable author statement Ref.1. Source: ProtInc

oxidation-reduction process

Traceable author statement Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid biosynthetic process

Traceable author statement PubMed 1863359. Source: ProtInc

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay. Source: HPA

   Molecular_functionNADPH binding

Inferred from electronic annotation. Source: Ensembl

NADPH-adrenodoxin reductase activity

Inferred from electronic annotation. Source: Ensembl

ferredoxin-NADP+ reductase activity

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 18319262. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FHITP497894EBI-1751533,EBI-741760

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform Short (identifier: P22570-1)

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: P22570-2)

The sequence of this isoform differs from the canonical sequence as follows:
     203-203: E → EALLLCQ
Note: Represents 10-20% of all adrenodoxin reductase mRNAs and seems to be inactive.
Isoform 3 (identifier: P22570-3)

The sequence of this isoform differs from the canonical sequence as follows:
     59-59: K → KRVEALCSQPRVLNSPALSGEGEDLGASQPLSLDPTSCHPVPQQ
Isoform 4 (identifier: P22570-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAGFYTAQHLLK → MEDKDRE
Isoform 5 (identifier: P22570-5)

The sequence of this isoform differs from the canonical sequence as follows:
     91-98: Missing.
Isoform 6 (identifier: P22570-6)

The sequence of this isoform differs from the canonical sequence as follows:
     59-59: K → KQ
     91-131: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: P22570-7)

The sequence of this isoform differs from the canonical sequence as follows:
     27-34: SFCHHFST → TFGGSDEVRDPANAKALRNKRRRMQVRVKLGKFQLLLDI
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion
Chain33 – 491459NADPH:adrenodoxin oxidoreductase, mitochondrial
PRO_0000019420

Regions

Nucleotide binding184 – 1874NADP By similarity
Nucleotide binding228 – 2292NADP By similarity
Nucleotide binding405 – 4073FAD By similarity

Sites

Binding site491FAD; via amide nitrogen By similarity
Binding site691FAD By similarity
Binding site771FAD; via amide nitrogen By similarity
Binding site1131FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2401NADP By similarity
Binding site3981FAD; via amide nitrogen By similarity
Binding site4051NADP; via amide nitrogen By similarity

Natural variations

Alternative sequence1 – 5959MASRC…QHLLK → MEDKDRE in isoform 4.
VSP_046669
Alternative sequence27 – 348SFCHHFST → TFGGSDEVRDPANAKALRNK RRRMQVRVKLGKFQLLLDI in isoform 7.
VSP_046670
Alternative sequence591K → KRVEALCSQPRVLNSPALSG EGEDLGASQPLSLDPTSCHP VPQQ in isoform 3.
VSP_045135
Alternative sequence591K → KQ in isoform 6.
VSP_046671
Alternative sequence91 – 13141Missing in isoform 6.
VSP_046672
Alternative sequence91 – 988Missing in isoform 5.
VSP_046673
Alternative sequence2031E → EALLLCQ in isoform Long.
VSP_003416
Natural variant71R → L. Ref.3
Corresponds to variant rs28365947 [ dbSNP | Ensembl ].
VAR_025192
Natural variant1231R → Q. Ref.1 Ref.3 Ref.4
Corresponds to variant rs690514 [ dbSNP | Ensembl ].
VAR_004624
Natural variant2131G → V. Ref.3
Corresponds to variant rs35692345 [ dbSNP | Ensembl ].
VAR_025193
Natural variant2481P → L. Ref.3
Corresponds to variant rs35072974 [ dbSNP | Ensembl ].
VAR_025194
Natural variant2511R → W. Ref.3
Corresponds to variant rs34038065 [ dbSNP | Ensembl ].
VAR_025195
Natural variant3011R → C. Ref.3
Corresponds to variant rs34118765 [ dbSNP | Ensembl ].
VAR_025196
Natural variant3451T → M. Ref.3
Corresponds to variant rs35660143 [ dbSNP | Ensembl ].
VAR_025197
Natural variant3521P → S. Ref.3
Corresponds to variant rs35696549 [ dbSNP | Ensembl ].
VAR_025198
Natural variant4721T → A. Ref.3
Corresponds to variant rs35769464 [ dbSNP | Ensembl ].
VAR_025199

Experimental info

Sequence conflict2231V → G in BAG56748. Ref.4

Sequences

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

Last modified January 24, 2006. Version 3.
Checksum: 15D07E714F592C9D

FASTA49153,837
        10         20         30         40         50         60 
MASRCWRWWG WSAWPRTRLP PAGSTPSFCH HFSTQEKTPQ ICVVGSGPAG FYTAQHLLKH 

        70         80         90        100        110        120 
PQAHVDIYEK QPVPFGLVRF GVAPDHPEVK NVINTFTQTA HSGRCAFWGN VEVGRDVTVP 

       130        140        150        160        170        180 
ELREAYHAVV LSYGAEDHRA LEIPGEELPG VCSARAFVGW YNGLPENQEL EPDLSCDTAV 

       190        200        210        220        230        240 
ILGQGNVALD VARILLTPPE HLERTDITKA ALGVLRQSRV KTVWLVGRRG PLQVAFTIKE 

       250        260        270        280        290        300 
LREMIQLPGA RPILDPVDFL GLQDKIKEVP RPRKRLTELL LRTATEKPGP AEAARQASAS 

       310        320        330        340        350        360 
RAWGLRFFRS PQQVLPSPDG RRAAGVRLAV TRLEGVDEAT RAVPTGDMED LPCGLVLSSI 

       370        380        390        400        410        420 
GYKSRPVDPS VPFDSKLGVI PNVEGRVMDV PGLYCSGWVK RGPTGVIATT MTDSFLTGQM 

       430        440        450        460        470        480 
LLQDLKAGLL PSGPRPGYAA IQALLSSRGV RPVSFSDWEK LDAEEVARGQ GTGKPREKLV 

       490 
DPQEMLRLLG H 

« Hide

Isoform Long [UniParc].

Checksum: 08C3D3F2C86564DA
Show »

FASTA49754,479
Isoform 3 [UniParc].

Checksum: 755B0612AAD29612
Show »

FASTA53458,304
Isoform 4 [UniParc].

Checksum: 20D88F1A91909900
Show »

FASTA43948,056
Isoform 5 [UniParc].

Checksum: 8AD11CAC35C3E4C1
Show »

FASTA48352,919
Isoform 6 [UniParc].

Checksum: 367CE00CA673D9E2
Show »

FASTA45149,425
Isoform 7 [UniParc].

Checksum: 1D82107E5C08C814
Show »

FASTA52257,370

References

« Hide 'large scale' references
[1]"Human adrenodoxin reductase: two mRNAs encoded by a single gene on chromosome 17cen-->q25 are expressed in steroidogenic tissues."
Solish S.B., Picado-Leonard J., Morel Y., Kuhn R.W., Mohandas T.K., Hanukoglu I., Miller W.L.
Proc. Natl. Acad. Sci. U.S.A. 85:7104-7108(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT AND LONG), VARIANT GLN-123.
[2]"Cloning and sequence of the human adrenodoxin reductase gene."
Lin D., Shi Y., Miller W.L.
Proc. Natl. Acad. Sci. U.S.A. 87:8516-8520(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]NIEHS SNPs program
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-7; GLN-123; VAL-213; LEU-248; TRP-251; CYS-301; MET-345; SER-352 AND ALA-472.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), VARIANT GLN-123.
Tissue: Adrenal gland, Caudate nucleus and Testis.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
Tissue: Lung.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03826 mRNA. Translation: AAB59498.1.
J03826 mRNA. Translation: AAB59497.1.
M58509, M58508 Genomic DNA. Translation: AAA51668.1.
M58509, M58508 Genomic DNA. Translation: AAA51669.1.
DQ085780 Genomic DNA. Translation: AAY68215.1.
AK293208 mRNA. Translation: BAG56748.1.
AK295307 mRNA. Translation: BAG58287.1.
AK298908 mRNA. Translation: BAG61016.1.
AK301779 mRNA. Translation: BAG63236.1.
AK301977 mRNA. Translation: BAH13598.1.
AC068874 Genomic DNA. No translation available.
BC002960 mRNA. Translation: AAH02960.1.
CCDSCCDS11707.1. [P22570-2]
CCDS58591.1. [P22570-4]
CCDS58592.1. [P22570-5]
CCDS58593.1. [P22570-1]
CCDS58594.1. [P22570-6]
CCDS58595.1. [P22570-3]
CCDS58596.1. [P22570-7]
PIRA40487.
RefSeqNP_001244941.1. NM_001258012.2. [P22570-3]
NP_001244942.1. NM_001258013.2. [P22570-7]
NP_001244943.1. NM_001258014.2. [P22570-5]
NP_001244944.1. NM_001258015.2. [P22570-6]
NP_001244945.1. NM_001258016.2. [P22570-4]
NP_004101.2. NM_004110.4. [P22570-2]
NP_077728.2. NM_024417.3. [P22570-1]
UniGeneHs.69745.

3D structure databases

ProteinModelPortalP22570.
SMRP22570. Positions 38-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108523. 1 interaction.
IntActP22570. 2 interactions.
STRING9606.ENSP00000293195.

PTM databases

PhosphoSiteP22570.

Polymorphism databases

DMDM85681283.

2D gel databases

REPRODUCTION-2DPAGEIPI00026958.

Proteomic databases

MaxQBP22570.
PaxDbP22570.
PeptideAtlasP22570.
PRIDEP22570.

Protocols and materials databases

DNASU2232.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000293195; ENSP00000293195; ENSG00000161513. [P22570-1]
ENST00000413947; ENSP00000408595; ENSG00000161513. [P22570-7]
ENST00000420580; ENSP00000414172; ENSG00000161513. [P22570-6]
ENST00000442102; ENSP00000416515; ENSG00000161513. [P22570-3]
ENST00000544854; ENSP00000445432; ENSG00000161513. [P22570-4]
ENST00000581530; ENSP00000462972; ENSG00000161513. [P22570-2]
ENST00000582944; ENSP00000462183; ENSG00000161513. [P22570-5]
GeneID2232.
KEGGhsa:2232.
UCSCuc002jlx.3. human. [P22570-2]
uc002jly.3. human. [P22570-1]
uc010wrl.2. human.

Organism-specific databases

CTD2232.
GeneCardsGC17M072858.
HGNCHGNC:3642. FDXR.
HPACAB008597.
HPA044393.
MIM103270. gene.
neXtProtNX_P22570.
PharmGKBPA28086.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0493.
HOGENOMHOG000249250.
HOVERGENHBG002132.
InParanoidP22570.
KOK00528.
OMAFTTKEFR.
PhylomeDBP22570.
TreeFamTF314193.

Enzyme and pathway databases

BioCycMetaCyc:HS08587-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00296.

Gene expression databases

ArrayExpressP22570.
BgeeP22570.
CleanExHS_FDXR.
GenevestigatorP22570.

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

GeneWikiAdrenodoxin_reductase.
GenomeRNAi2232.
NextBio9037.
PROP22570.
SOURCESearch...

Entry information

Entry nameADRO_HUMAN
AccessionPrimary (citable) accession number: P22570
Secondary accession number(s): B4DDI7 expand/collapse secondary AC list , B4DHX5, B4DQQ4, B4DX24, B7Z7G2, E7EQC1, Q13716, Q4PJI0, Q9BU12
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 24, 2006
Last modified: July 9, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM