Adrenodoxin, mitochondrial precursor

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P10109 (ADX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 122. 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)

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	3D-structure Complete proteome Reference 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 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

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) By similarity

Metal binding

112

Iron-sulfur (2Fe-2S) By similarity

Metal binding

115

Iron-sulfur (2Fe-2S) By similarity

Metal binding

152

Iron-sulfur (2Fe-2S) By similarity

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: 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

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.

SMR

P10109. Positions 64-184.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10109. 1 interaction.

STRING

P10109.

PTM databases

PhosphoSite

P10109.

Polymorphism databases

DMDM

113471.

Proteomic databases

PRIDE

P10109.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260270; ENSP00000260270; ENSG00000137714.

GeneID

2230.

KEGG

hsa:2230.

NMPDR

fig|9606.3.peg.6579.

UCSC

uc001pkx.1. human.

Organism-specific databases

CTD

2230.

GeneCards

GC11P110334.

H-InvDB

HIX0010099.

HGNC

HGNC:3638. FDX1.

HPA

HPA041630.

MIM

103260. gene.

neXtProt

NX_P10109.

PharmGKB

PA28082.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08895.

GeneTree

ENSGT00530000063577.

HOGENOM

HBG524254.

HOVERGEN

HBG000092.

InParanoid

P10109.

OMA

CQVCLTK.

OrthoDB

EOG4DNF5T.

PhylomeDB

P10109.

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. Beta-grasp_ferredoxin-type.
IPR001041. Ferredoxin.
[Graphical view]

Gene3D

G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.

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.

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:	January 25, 2012
This is version 122 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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents