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Protein

Adrenodoxin, mitochondrial

Gene

Fdx1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Cofactori

[2Fe-2S] clusterNote: Binds 1 [2Fe-2S] cluster.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi110 – 1101Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi116 – 1161Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi119 – 1191Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi156 – 1561Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB
  • electron carrier activity Source: RGD
  • enzyme binding Source: RGD
  • iron ion binding Source: RGD

GO - Biological processi

  • adrenal gland development Source: RGD
  • cellular response to epinephrine stimulus Source: RGD
  • cellular response to leptin stimulus Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • cholesterol metabolic process Source: UniProtKB
  • hormone biosynthetic process Source: UniProtKB
  • NADPH oxidation Source: RGD
  • positive regulation of oxidoreductase activity Source: RGD
  • regulation of catalytic activity Source: RGD
  • response to gonadotropin Source: RGD
  • response to leptin Source: RGD
  • steroid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Electron transport, Lipid metabolism, Steroid metabolism, Steroidogenesis, Sterol metabolism, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Adrenodoxin, mitochondrial
Alternative name(s):
Adrenal ferredoxin
Ferredoxin-1
Gene namesi
Name:Fdx1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi62036. Fdx1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial crista Source: RGD
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6464MitochondrionAdd
BLAST
Chaini65 – 188124Adrenodoxin, mitochondrialPRO_0000000991Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei70 – 701N6-acetyllysine; alternateBy similarity
Modified residuei70 – 701N6-succinyllysine; alternateBy similarity
Modified residuei162 – 1621N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP24483.
PRIDEiP24483.

PTM databases

iPTMnetiP24483.

Expressioni

Tissue specificityi

Found in all tissues, most abundant in adrenals, ovaries and testes.

Interactioni

Subunit structurei

Interacts with CYP11A1.By similarity

GO - Molecular functioni

  • enzyme binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016263.

Structurei

3D structure databases

ProteinModelPortaliP24483.
SMRiP24483. Positions 69-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 1751072Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adrenodoxin/putidaredoxin family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3309. Eukaryota.
COG0633. LUCA.
HOGENOMiHOG000244518.
HOVERGENiHBG000092.
InParanoidiP24483.
PhylomeDBiP24483.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAPGARLL RAACASVAFR GLDCRRLLVC GTRAGPAVPQ WTPSPHTLAE
60 70 80 90 100
AGPGRPLSVS ARARSSSEDK VTVHFKNRDG ETLTTKGKVG DSLLDVVIEN
110 120 130 140 150
NLDIDGFGAC EGTLACSTCH LIFEDHIYEK LDAITDEEND MLDLAFGLTN
160 170 180
RSRLGCQVCL TKAMDNMTVR VPEAVADVRQ SVDMSKNS
Length:188
Mass (Da):20,135
Last modified:March 1, 1992 - v1
Checksum:iB0686D5159A30240
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50436 mRNA. Translation: BAA08927.1.
PIRiA39553.
RefSeqiNP_058822.1. NM_017126.1.
UniGeneiRn.6946.

Genome annotation databases

GeneIDi29189.
KEGGirno:29189.
UCSCiRGD:62036. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50436 mRNA. Translation: BAA08927.1.
PIRiA39553.
RefSeqiNP_058822.1. NM_017126.1.
UniGeneiRn.6946.

3D structure databases

ProteinModelPortaliP24483.
SMRiP24483. Positions 69-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016263.

PTM databases

iPTMnetiP24483.

Proteomic databases

PaxDbiP24483.
PRIDEiP24483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29189.
KEGGirno:29189.
UCSCiRGD:62036. rat.

Organism-specific databases

CTDi2230.
RGDi62036. Fdx1.

Phylogenomic databases

eggNOGiKOG3309. Eukaryota.
COG0633. LUCA.
HOGENOMiHOG000244518.
HOVERGENiHBG000092.
InParanoidiP24483.
PhylomeDBiP24483.

Miscellaneous databases

NextBioi608311.
PROiP24483.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Expression and regulation of adrenodoxin and P450scc mRNA in rodent tissues."
    Mellon S.H., Kushner J.A., Vaisse C.
    DNA Cell Biol. 10:339-347(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.
  2. "Cloning and sequence analysis of a full-length cDNA of rat adrenodoxin."
    Sagara Y., Watanabe Y., Kawamura K., Yubisui T.
    Biol. Pharm. Bull. 19:39-41(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Adrenal gland.

Entry informationi

Entry nameiADX_RAT
AccessioniPrimary (citable) accession number: P24483
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: January 20, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.