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P10109 (ADX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Adrenodoxin, mitochondrial
Alternative name(s):
Adrenal ferredoxin
Ferredoxin-1
Hepatoredoxin
Gene names
Name:FDX1
Synonyms:ADX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in the synthesis of thyroid hormones. Essential for the synthesis of various steroid hormones, participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage. Ref.10 Ref.14

Cofactor

Binds 1 2Fe-2S cluster. Ref.13 Ref.14

Subunit structure

Interacts with CYP11A1. Ref.14

Subcellular location

Mitochondrion matrix Ref.10.

Tissue specificity

Highest levels in the adrenal gland (at protein level). Also detected in kidney and testis (at protein level). Ref.10

Sequence similarities

Belongs to the adrenodoxin/putidaredoxin family.

Contains 1 2Fe-2S ferredoxin-type domain.

Biophysicochemical properties

Redox potential:

E0 is -448 mV.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6060Mitochondrion
Chain61 – 184124Adrenodoxin, mitochondrial
PRO_0000000988

Regions

Domain67 – 1711052Fe-2S ferredoxin-type

Sites

Metal binding1061Iron-sulfur (2Fe-2S)
Metal binding1121Iron-sulfur (2Fe-2S)
Metal binding1151Iron-sulfur (2Fe-2S)
Metal binding1521Iron-sulfur (2Fe-2S)

Amino acid modifications

Modified residue661N6-acetyllysine; alternate By similarity
Modified residue661N6-succinyllysine; alternate By similarity
Modified residue1581N6-succinyllysine By similarity

Secondary structure

............................ 184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10109 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: A234EC601136C85F

FASTA18419,393
        10         20         30         40         50         60 
MAAAGGARLL RAASAVLGGP AGRWLHHAGS RAGSSGLLRN RGPGGSAEAS RSLSVSARAR 

        70         80         90        100        110        120 
SSSEDKITVH FINRDGETLT TKGKVGDSLL DVVVENNLDI DGFGACEGTL ACSTCHLIFE 

       130        140        150        160        170        180 
DHIYEKLDAI TDEENDMLDL AYGLTDRSRL GCQICLTKSM DNMTVRVPET VADARQSIDV 


GKTS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and structure of the human adrenodoxin gene."
Chang C.-Y., Wu D.-A., Lai C.-C., Miller W.L., Chung B.-C.
DNA 7:609-615(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells."
Picado-Leonard J., Voutilainen R., Kao L.-C., Chung B.-C., Strauss J.F. III, Miller W.L.
J. Biol. Chem. 263:3240-3244(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Molecular cloning and sequence analysis of human placental ferredoxin."
Mittal S., Zhu Y.-Z., Vickery L.E.
Arch. Biochem. Biophys. 264:383-391(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[4]"Structure, sequence, chromosomal location, and evolution of the human ferredoxin gene family."
Chang C.-Y., Wu D.-A., Mohandas T.K., Chung B.-C.
DNA Cell Biol. 9:205-212(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"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].
Tissue: Lung and Placenta.
[8]"Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode."
Johnson D., Norman S., Tuckey R.C., Martin L.L.
Bioelectrochemistry 59:41-47(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CYCLIC VOLTAMMETRY.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis."
Sheftel A.D., Stehling O., Pierik A.J., Elsasser H.P., Muhlenhoff U., Webert H., Hobler A., Hannemann F., Bernhardt R., Lill R.
Proc. Natl. Acad. Sci. U.S.A. 107:11775-11780(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]"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].
[12]"1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins."
Skjeldal L., Markley J.L., Coghlan V.M., Vickery L.E.
Biochemistry 30:9078-9083(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[13]"Crystal structure of human ferredoxin-1 (FDX1) in complex with iron-sulfur cluster."
Structural genomics consortium (SGC)
Submitted (NOV-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 61-184 IN COMPLEX WITH IRON-SULFUR CLUSTER, COFACTOR.
[14]"Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system."
Strushkevich N., MacKenzie F., Cherkesova T., Grabovec I., Usanov S., Park H.W.
Proc. Natl. Acad. Sci. U.S.A. 108:10139-10143(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 62-175 IN COMPLEX WITH IRON-SULFUR CLUSTER AND CYP11A1, FUNCTION, COFACTOR, INTERACTION WITH CYP11A1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23668 Genomic DNA. Translation: AAA50462.1.
J03548 mRNA. Translation: AAA96806.1.
M18003 mRNA. Translation: AAA76853.1.
M34788 mRNA. Translation: AAA35829.1.
M34786, M34784 Genomic DNA. Translation: AAA35856.1.
M34785, M34783 Genomic DNA. Translation: AAA35855.1.
BT006681 mRNA. Translation: AAP35327.1.
EF444978 Genomic DNA. Translation: ACA05992.1.
BC010284 mRNA. Translation: AAH10284.1.
BC017063 mRNA. Translation: AAH17063.1.
CCDSCCDS8344.1.
PIRAXHU. A31853.
RefSeqNP_004100.1. NM_004109.4.
UniGeneHs.744.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3N9YX-ray2.10C/D62-175[»]
3N9ZX-ray2.17C/D62-184[»]
3NA0X-ray2.50C/D88-155[»]
3NA1X-ray2.25C/D62-184[»]
3P1MX-ray2.54A/B/C/D/E/F/G/H61-184[»]
ProteinModelPortalP10109.
SMRP10109. Positions 64-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108521. 4 interactions.
IntActP10109. 1 interaction.
STRING9606.ENSP00000260270.

Chemistry

DrugBankDB00648. Mitotane.

PTM databases

PhosphoSiteP10109.

Polymorphism databases

DMDM113471.

Proteomic databases

MaxQBP10109.
PaxDbP10109.
PRIDEP10109.

Protocols and materials databases

DNASU2230.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260270; ENSP00000260270; ENSG00000137714.
GeneID2230.
KEGGhsa:2230.
UCSCuc001pkx.3. human.

Organism-specific databases

CTD2230.
GeneCardsGC11P110334.
HGNCHGNC:3638. FDX1.
HPAHPA041630.
MIM103260. gene.
neXtProtNX_P10109.
PharmGKBPA28082.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0633.
HOGENOMHOG000244518.
HOVERGENHBG000092.
InParanoidP10109.
OMAARQSVDM.
OrthoDBEOG708W1D.
PhylomeDBP10109.
TreeFamTF319845.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP10109.
CleanExHS_FDX1.
GenevestigatorP10109.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSPR00355. ADRENODOXIN.
SUPFAMSSF54292. SSF54292. 1 hit.
PROSITEPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10109.
GeneWikiAdrenal_ferredoxin.
GenomeRNAi2230.
NextBio9031.
PROP10109.
SOURCESearch...

Entry information

Entry nameADX_HUMAN
AccessionPrimary (citable) accession number: P10109
Secondary accession number(s): B0YJ14, Q53YD6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 147 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM