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P00257 (ADX_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
Hepato-ferredoxin
Gene names
Name:FDX1
Synonyms:ADX
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length186 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Cofactor

Binds 1 2Fe-2S cluster.

Subunit structure

Interacts with CYP11A1 By similarity.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the adrenodoxin/putidaredoxin family.

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FDXRP081652EBI-593992,EBI-593948

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P00257-1)

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 2 (identifier: P00257-2)

The sequence of this isoform differs from the canonical sequence as follows:
     24-60: ARPRAGAGGLRGSRGPGLGGGAVATRTLSVSGRAQSS → LKSSQFIKVSCSGSWISAAQRAFICYSKSGNITCFLR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5858Mitochondrion Ref.8
Chain59 – 186128Adrenodoxin, mitochondrial
PRO_0000000986

Regions

Domain65 – 1691052Fe-2S ferredoxin-type

Sites

Metal binding1041Iron-sulfur (2Fe-2S)
Metal binding1101Iron-sulfur (2Fe-2S)
Metal binding1131Iron-sulfur (2Fe-2S)
Metal binding1501Iron-sulfur (2Fe-2S)

Amino acid modifications

Modified residue641N6-acetyllysine; alternate By similarity
Modified residue641N6-succinyllysine; alternate By similarity
Modified residue1561N6-succinyllysine By similarity

Natural variations

Alternative sequence24 – 6037ARPRA…RAQSS → LKSSQFIKVSCSGSWISAAQ RAFICYSKSGNITCFLR in isoform 2.
VSP_016558

Experimental info

Sequence conflict61L → M in AAI09850. Ref.6
Sequence conflict241A → V in AAA30357. Ref.1
Sequence conflict621E → Q AA sequence Ref.8
Sequence conflict1301D → N AA sequence Ref.8
Sequence conflict1341D → N AA sequence Ref.8

Secondary structure

............................ 186
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: F0F2EE027BFAC371

FASTA18619,756
        10         20         30         40         50         60 
MAARLLRVAS AALGDTAGRW RLLARPRAGA GGLRGSRGPG LGGGAVATRT LSVSGRAQSS 

        70         80         90        100        110        120 
SEDKITVHFI NRDGETLTTK GKIGDSLLDV VVQNNLDIDG FGACEGTLAC STCHLIFEQH 

       130        140        150        160        170        180 
IFEKLEAITD EENDMLDLAY GLTDRSRLGC QICLTKAMDN MTVRVPDAVS DARESIDMGM 


NSSKIE 

« Hide

Isoform 2 [UniParc].

Checksum: 7D3E98D62C9D12D3
Show »

FASTA18620,395

References

« Hide 'large scale' references
[1]"Molecular cloning and amino acid sequence of the precursor form of bovine adrenodoxin: evidence for a previously unidentified COOH-terminal peptide."
Okamura T., John M.E., Zuber M.X., Simpson E.R., Waterman M.R.
Proc. Natl. Acad. Sci. U.S.A. 82:5705-5709(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Multiple species of bovine adrenodoxin mRNA. Occurrence of two different mitochondrial precursor sequences associated with the same mature sequence."
Okamura T., Kagimoto M., Simpson E.R., Waterman M.R.
J. Biol. Chem. 262:10335-10338(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Structural organization of the bovine adrenodoxin gene."
Sagara Y., Sawae H., Kimura A., Sagara-Nakano Y., Morohashi K., Miyoshi K., Horiuchi T.
J. Biochem. 107:77-83(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]"Molecular cloning and nucleotide sequences of bovine hepato-ferredoxin cDNA; identical primary structures of hepato- and adreno-ferredoxins."
Matsuo Y., Tomita S., Tsuneoka Y., Furukawa A., Ichikawa Y.
Int. J. Biochem. 24:289-295(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[5]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]NIH - Mammalian Gene Collection (MGC) project
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: Crossbred X Angus.
Tissue: Liver.
[7]"Transcription of the bovine adrenodoxin gene produces two species of mRNA of which only one is translated into adrenodoxin."
Kagimoto M., Kagimoto K., Simpson E.R., Waterman M.R.
J. Biol. Chem. 263:8925-8928(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
[8]"The amino acid sequence of bovine adrenodoxin."
Tanaka M., Haniu M., Yasunobu K.T., Kimura T.
J. Biol. Chem. 248:1141-1157(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 59-172 (ISOFORM 1).
[9]"Isolation and purification of mature bovine adrenocortical ferredoxin with an elongated carboxyl end."
Sakihama N., Hiwatashi A., Miyatake A., Shin M., Ichikawa Y.
Arch. Biochem. Biophys. 264:23-29(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 171-185.
[10]"Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis."
Mueller J.J., Lapko A., Bourenkov G., Ruckpaul K., Heinemann U.
J. Biol. Chem. 276:2786-2789(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 59-186 IN COMPLEX WITH ADRENODOXIN REDUCTASE.
[11]"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 OF 59-186.
[12]"A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin."
Beilke D., Weiss R., Loehr F., Pristovsek P., Hannemann F., Bernhardt R., Rueterjans H.
Biochemistry 41:7969-7978(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 59-186.
[13]"New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)."
Mueller A., Mueller J.J., Muller Y.A., Uhlmann H., Bernhardt R., Heinemann U.
Structure 6:269-280(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 63-166.
[14]"The tertiary structure of full-length bovine adrenodoxin suggests functional dimers."
Pikuleva I.A., Tesh K., Waterman M.R., Kim Y.
Arch. Biochem. Biophys. 373:44-55(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11746 mRNA. Translation: AAA30357.1.
M16934 mRNA. Translation: AAA30358.1.
D00467 mRNA. Translation: BAA00362.1.
D00471 Genomic DNA. Translation: BAA00363.1.
M19656, M19474 Genomic DNA. Translation: AAA78950.1.
BT030601 mRNA. Translation: ABQ13041.1.
BC109849 mRNA. Translation: AAI09850.1.
S78831 mRNA. Translation: AAB21264.1.
PIRAXBO. JX0094.
RefSeqNP_851354.1. NM_181011.2.
UniGeneBt.1573.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYFX-ray1.85A/B62-166[»]
1CJEX-ray2.50A/B/C/D60-186[»]
1E6EX-ray2.30B/D60-186[»]
1L6UNMR-A59-186[»]
1L6VNMR-A59-186[»]
2BT6X-ray1.50A/B60-166[»]
2JQRNMR-B62-166[»]
ProteinModelPortalP00257.
SMRP00257. Positions 63-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00257. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000015660; ENSBTAP00000015660; ENSBTAG00000011793. [P00257-1]
GeneID281157.
KEGGbta:281157.

Organism-specific databases

CTD2230.

Phylogenomic databases

eggNOGCOG0633.
GeneTreeENSGT00530000063577.
HOGENOMHOG000244518.
HOVERGENHBG000092.
InParanoidP00257.
TreeFamTF319845.

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

EvolutionaryTraceP00257.
NextBio20805220.

Entry information

Entry nameADX_BOVIN
AccessionPrimary (citable) accession number: P00257
Secondary accession number(s): A5D9I2 expand/collapse secondary AC list , P08498, P12713, Q32KZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references