FET3 [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

Official Symbol: FET3
Primary source: FungiDB:YMR058W
Locus tag: YMR058W
See related: SGD:S000004662; AllianceGenome:SGD:S000004662; VEuPathDB:YMR058W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables ferroxidase activity. Contributes to iron ion transmembrane transporter activity. Involved in arsenate ion transmembrane transport; iron ion transport; and response to copper ion. Located in plasma membrane. Part of high-affinity iron permease complex. Human ortholog(s) of this gene implicated in aceruloplasminemia; epilepsy; and hemosiderosis. Orthologous to human CP (ceruloplasmin); HEPH (hephaestin); and HEPHL1 (hephaestin like 1). [provided by Alliance of Genome Resources, Apr 2022]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (388822..390732)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

this work unveils a novel protection mechanism against copper toxicity mediated by Ace1, which relies in the activation of FET3 and results in the restriction of Aft1 activity as a means to prevent excessive copper accumulation
Title: Ace1 prevents intracellular copper accumulation by regulating Fet3 expression and thereby restricting Aft1 activity.
study reveals a novel functional role of K(+) in the binding of copper to apoFet3p and identifies a K(+)/H(+) exchanger at the secretory pathway as a new molecular factor associated with iron uptake in yeast.
Title: Potassium and the K+/H+ Exchanger Kha1p Promote Binding of Copper to ApoFet3p Multi-copper Ferroxidase.
Presence of crowding agents does not affect Fet3p structural content but increases thermal resistance. The observations are compatible with ordering of a non-optimal substrate-binding site and restricted internal dynamics.
Title: Non-linear effects of macromolecular crowding on enzymatic activity of multi-copper oxidase.
We find that unfolding reactions of apo and different holo forms of Fet3p are irreversible reactions that depend on the scan rate and there is a metal-induced tradeoff between overall protein stability and metal coordination
Title: In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site.
Data show that overproduction of Izh2p prevents the iron-dependent induction of the Fet3p component of the high-affinity iron-uptake system and is deleterious for growth in iron-limited medium.
Title: Probing the mechanism of FET3 repression by Izh2p overexpression.
Substitution of Asp320 with asparagine essentially abolished the Fet3-dependent iron transport activity. All other mutants (D278Q, D279N, D312N and D315I) behaved essentially as the wild-type protein.
Title: Specific aspartate residues in FET3 control high-affinity iron transport in Saccharomyces cerevisiae.
D283, E185, and D409 in Fet3p provide a Fe(II) binding site that actually favors ferric iron.
Title: Structural basis of the ferrous iron specificity of the yeast ferroxidase, Fet3p.
Structure-function analysis of the cuprous oxidase activity in Fet3p from Saccharomyces cerevisiae
Title: Structure-function analysis of the cuprous oxidase activity in Fet3p from Saccharomyces cerevisiae.
The D94 residue appears to activate a proton of the type 2 Cu(+)-bound water for participation in the transition state.
Title: Role of aspartate 94 in the decay of the peroxide intermediate in the multicopper oxidase Fet3p.
results are consistent with a (minimal) heterodimer model of the Fet3p.Ftr1p complex that supports the trafficking of iron from Fet3p to Ftr1p for iron permeation across the yeast plasma membrane
Title: Assembly, activation, and trafficking of the Fet3p.Ftr1p high affinity iron permease complex in Saccharomyces cerevisiae.

Submit: New GeneRIF Correction

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables copper ion binding	IEA Inferred from Electronic Annotation more info
enables ferroxidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ferroxidase activity	IDA Inferred from Direct Assay more info	PubMed
enables ferroxidase activity	IEA Inferred from Electronic Annotation more info
contributes_to iron ion transmembrane transporter activity	IDA Inferred from Direct Assay more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in arsenate ion transmembrane transport	IGI Inferred from Genetic Interaction more info	PubMed
involved_in cellular response to iron ion starvation	IBA Inferred from Biological aspect of Ancestor more info
involved_in iron ion transmembrane transport	IGI Inferred from Genetic Interaction more info	PubMed
involved_in iron ion transmembrane transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in iron ion transport	IEA Inferred from Electronic Annotation more info
involved_in monoatomic ion transport	IEA Inferred from Electronic Annotation more info
involved_in reductive iron assimilation	IBA Inferred from Biological aspect of Ancestor more info
involved_in reductive iron assimilation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to copper ion	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in endoplasmic reticulum	HDA more info	PubMed
located_in fungal-type vacuole	HDA more info	PubMed
part_of high-affinity iron permease complex	IBA Inferred from Biological aspect of Ancestor more info
part_of high-affinity iron permease complex	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: ferroxidase FET3

NP_013774.1

EC 1.16.3.1

EC 1.16.3.4

Ferro-O2-oxidoreductase; multicopper oxidase that oxidizes ferrous (Fe2+) to ferric iron (Fe3+) for subsequent cellular uptake by transmembrane permease Ftr1p; required for high-affinity iron uptake and involved in mediating resistance to copper ion toxicity, belongs to class of integral membrane multicopper oxidases; protein abundance increases in response to DNA replication stress

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001145.3 Reference assembly

Range

388822..390732

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182556.1 → NP_013774.1 TPA: ferroxidase FET3 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013774.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VZN2, P38993

UniProtKB/TrEMBL

A6ZMB7, B3LLV1, C7GL66, C8ZER0, N1NYP0

Conserved Domains (1) summary

COG2132
Location:7 → 489

SufI; Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenes