Fdx1 ferredoxin 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Fdx1provided by MGI
Official Full Name: ferredoxin 1provided by MGI
Primary source: MGI:MGI:103224
See related: Ensembl:ENSMUSG00000032051 AllianceGenome:MGI:103224
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Summary: Ferrodoxins are iron-sulfur proteins that facilitate monooxygenase reactions catalyzed by P450 enzymes. The protein encoded by this gene is present in the mitochondrial matrix and transfers electrons from ferredoxin reductase to steroidogenic mitochondrial cytochrome P450 proteins. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Sep 2014]
Expression: Biased expression in adrenal adult (RPKM 1441.7) and ovary adult (RPKM 344.8) See more
Orthologs: human all
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Genomic context

Location:: 9 A5.3; 9 28.62 cM

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	9	NC_000075.7 (51854323..51874902, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	9	NC_000075.6 (51943023..51963602, complement)

Chromosome 9 - NC_000075.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Ferredoxin 1 is essential for embryonic development and lipid homeostasis.
Title: Ferredoxin 1 is essential for embryonic development and lipid homeostasis.
FDX1 regulates leydig cell ferroptosis mediates PM2.5-induced testicular dysfunction of mice.
Title: FDX1 regulates leydig cell ferroptosis mediates PM(2.5)-induced testicular dysfunction of mice.
FDX1 enhances endometriosis cell cuproptosis via G6PD-mediated redox homeostasis.
Title: FDX1 enhances endometriosis cell cuproptosis via G6PD-mediated redox homeostasis.
Ferredoxin 1 regulates granulosa cell apoptosis and autophagy in polycystic ovary syndrome.
Title: Ferredoxin 1 regulates granulosa cell apoptosis and autophagy in polycystic ovary syndrome.
Data suggest that Sf1 and c-jun interact and cooperate to activate the Fdx1 promoter in MA-10 (tumorigenic cell line) and TM3 (non-tumorigenic cell line) Leydig cells; such activation requires different regulatory elements located between -124 and -306 bp of Fdx1 promoter and involves recruitment of Sf1 to this region.
Title: Transcription factors SF1 and cJUN cooperate to activate the Fdx1 promoter in MA-10 Leydig cells.
mouse MT-CYP1A1 is an extrinsic membrane protein, which exhibited high FDX1 plus FDXR-mediated N-demethylation of a number of tricyclic antidepressants, pain killers, anti-psychotics, and narcotics that are poor substrates for microsomal CYP1A1
Title: Role of protein kinase C-mediated protein phosphorylation in mitochondrial translocation of mouse CYP1A1, which contains a non-canonical targeting signal.

Submit: New GeneRIF Correction

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (2)
Endonuclease-mediated (4)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Fdx1 (e-PCR), detects polymorphism
- UniSTS:256610

35.MMHAP56FLD5.seq (e-PCR)
- UniSTS:124147

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables 2 iron, 2 sulfur cluster binding	ISO Inferred from Sequence Orthology more info
contributes_to NADPH-adrenodoxin reductase activity	ISO Inferred from Sequence Orthology more info
contributes_to cholesterol monooxygenase (side-chain-cleaving) activity	ISO Inferred from Sequence Orthology more info
enables electron transfer activity	IBA Inferred from Biological aspect of Ancestor more info
enables electron transfer activity	ISO Inferred from Sequence Orthology more info
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables iron ion binding	ISO Inferred from Sequence Orthology more info
enables iron-sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in NADPH oxidation	ISO Inferred from Sequence Orthology more info
involved_in P450-containing electron transport chain	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within cellular response to cAMP	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within cellular response to forskolin	IDA Inferred from Direct Assay more info	PubMed
involved_in cholesterol metabolic process	ISO Inferred from Sequence Orthology more info
involved_in electron transport chain	IBA Inferred from Biological aspect of Ancestor more info
involved_in hormone biosynthetic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within lipid metabolic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within steroid biosynthetic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within steroid metabolic process	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in mitochondrial crista	ISO Inferred from Sequence Orthology more info
located_in mitochondrial matrix	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	HDA more info	PubMed
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: adrenodoxin, mitochondrial

Names: adrenal ferredoxin

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001301728.1 → NP_001288657.1 adrenodoxin, mitochondrial isoform 2 precursor

Status: REVIEWED

Description

Transcript Variant: This variant (2) contains an alternate exon, which results in a frameshift, compared to variant 1. The resulting protein (isoform 2) has a shorter, distinct C-terminus compared to isoform 1.

Source sequence(s)

AC140363, AK148115, BB578768, BX516353, D43689

Consensus CDS

CCDS90568.1

UniProtKB/TrEMBL

A0A1L1STP5, Q3UG56

Related

ENSMUSP00000150434.2, ENSMUST00000214013.2

Conserved Domains (1) summary

cl00159
Location:71 → 150

fer2; 2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis ...
NM_007996.2 → NP_032022.1 adrenodoxin, mitochondrial isoform 1 precursor

See identical proteins and their annotated locations for NP_032022.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the shorter transcript and encodes the longer isoform (1).

Source sequence(s)

AI050584, BB578768, D43689

Consensus CDS

CCDS23178.1

UniProtKB/Swiss-Prot

P46656

UniProtKB/TrEMBL

Q4FZG2, Q545P3

Related

ENSMUSP00000034552.7, ENSMUST00000034552.8

Conserved Domains (1) summary

cl00159
Location:71 → 174

fer2; 2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis ...