Reviewed, UniProtKB/Swiss-Prot P10109 (ADX_HUMAN)

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) [Complete 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. Transfers electrons from adrenodoxin reductase to the cholesterol side chain cleavage cytochrome P450.
Cofactor	Binds 1 2Fe-2S cluster.
Subcellular location	Mitochondrion matrix.
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	Electron transport Transport
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Traceable author statement. Source: ProtInc iron ion binding Ref.3 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 60	60	Mitochondrion
	Chain	61 – 184	124	Adrenodoxin, mitochondrial		PRO_0000000988
Regions
	Domain	67 – 171	105	2Fe-2S ferredoxin-type
Sites
	Metal binding	106	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	112	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	115	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	152	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P10109-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: A234EC601136C85F	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

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: 3229285] [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: 3343244] [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: 2969697] [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: 2340092] [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: 15489334] [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: 12699818] [Abstract] Cited for: CYCLIC VOLTAMMETRY.
[9]	"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: 1909889] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Hs.744
3D structure databases
SMR	P10109. Positions 65-168.
ModBase	Search...
Protein-protein interaction databases
STRING	P10109.
PTM databases
PhosphoSite	P10109.
Proteomic databases
PRIDE	P10109.
Genome annotation databases
Ensembl	ENST00000260270; ENSP00000260270; ENSG00000137714; Homo sapiens. [Genome view]
GeneID	2230.
KEGG	hsa:2230.
NMPDR	fig|9606.3.peg.6579.
UCSC	uc001pkx.1. human.
Organism-specific databases
CTD	2230.
GeneCards	GC11P109805.
H-InvDB	HIX0010099. HIX0059989.
HGNC	HGNC:3638. FDX1.
MIM	103260. gene.
PharmGKB	PA28082.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P10109.
HOVERGEN	P10109.
OMA	ARQSVDM
OrthoDB	EOG9SFCRM
Gene expression databases
ArrayExpress	P10109.
Bgee	P10109.
CleanEx	HS_FDX1.
Genevestigator	P10109.
GermOnline	ENSG00000137714. Homo sapiens.
Family and domain databases
InterPro	IPR001055. Adrenodoxin. IPR018298. Adrenodoxin_Fe-S_BS. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF00111. Fer2. 1 hit. [Graphical view]
PRINTS	PR00355. ADRENODOXIN.
PROSITE	PS51085. 2FE2S_FER_2. 1 hit. PS00814. ADX. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00648. Mitotane.
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:	November 24, 2009
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.