Adrenodoxin, mitochondrial precursor

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P10109 (ADX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 135. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Adrenodoxin, mitochondrial

Alternative name(s):
Adrenal ferredoxin
Ferredoxin-1
Hepatoredoxin

Gene names

Name:	FDX1
Synonyms:	ADX

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Cofactor	Binds 1 2Fe-2S cluster.
Subunit structure	Interacts with CYP11A1.
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.

Ontologies

Keywords
Biological process	Cholesterol metabolism Electron transport Lipid metabolism Steroid metabolism Steroidogenesis Sterol metabolism Transport
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW generation of precursor metabolites and energy Traceable author statement Ref.3. Source: ProtInc
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: HPA
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Traceable author statement PubMed 1863359. Source: ProtInc iron ion binding Traceable author statement Ref.3. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 60

Mitochondrion

Chain

61 – 184

124

Adrenodoxin, mitochondrial

PRO_0000000988

Regions

Domain

67 – 171

105

2Fe-2S ferredoxin-type

Sites

Metal binding

106

Iron-sulfur (2Fe-2S)

Metal binding

112

Iron-sulfur (2Fe-2S)

Metal binding

115

Iron-sulfur (2Fe-2S)

Metal binding

152

Iron-sulfur (2Fe-2S)

Secondary structure

184

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P10109 [UniParc].

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

FASTA

184

19,393

        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' referencesShow '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.

IPI

IPI00019326.

PIR

AXHU. A31853.

RefSeq

NP_004100.1. NM_004109.4.

UniGene

Hs.744.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3N9Y	X-ray	2.10	C/D	62-175	[»]
3N9Z	X-ray	2.17	C/D	62-184	[»]
3NA0	X-ray	2.50	C/D	88-155	[»]
3NA1	X-ray	2.25	C/D	62-184	[»]
3P1M	X-ray	2.54	A/B/C/D/E/F/G/H	61-184	[»]

ProteinModelPortal

P10109.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10109. 1 interaction.

STRING

9606.ENSP00000260270.

PTM databases

PhosphoSite

P10109.

Polymorphism databases

DMDM

113471.

Proteomic databases

PaxDb

P10109.

PRIDE

P10109.

Protocols and materials databases

DNASU

2230.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260270; ENSP00000260270; ENSG00000137714.

GeneID

2230.

KEGG

hsa:2230.

UCSC

uc001pkx.3. human.

Organism-specific databases

CTD

2230.

GeneCards

GC11P110334.

HGNC

HGNC:3638. FDX1.

HPA

HPA041630.

MIM

103260. gene.

neXtProt

NX_P10109.

PharmGKB

PA28082.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0633.

HOGENOM

HOG000244518.

HOVERGEN

HBG000092.

InParanoid

P10109.

OMA

GCQVCLT.

OrthoDB

EOG4DNF5T.

PhylomeDB

P10109.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

P10109.

CleanEx

HS_FDX1.

Genevestigator

P10109.

GermOnline

ENSG00000137714. Homo sapiens.

Family and domain databases

Gene3D

3.10.20.30. 1 hit.

InterPro

IPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]

Pfam

PF00111. Fer2. 1 hit.
[Graphical view]

PRINTS

PR00355. ADRENODOXIN.

SUPFAM

SSF54292. Ferredoxin. 1 hit.

PROSITE

PS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00648. Mitotane.

EvolutionaryTrace

P10109.

GenomeRNAi

2230.

NextBio

9031.

SOURCE

Search...

Entry information

Entry name

ADX_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 11

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents