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Reviewed, UniProtKB/Swiss-Prot P36033 (FRE2_YEAST)

Last modified November 24, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ferric/cupric reductase transmembrane component 2
    EC=1.16.1.-
Alternative name(s):
    Ferric-chelate reductase 2
Gene names
Name: FRE2
Ordered Locus Names: YKL220C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length711 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe3+-salts and Fe3+ bound to catecholate or hydroxamate siderophores. Fe3+ is reduced to Fe2+, which then dissociates from the siderophore and can be imported by the high-affinity Fe2+ transport complex in the plasma membrane. Also participates in Cu2+ reduction and Cu+ uptake. Ref.5 Ref.10

Catalytic activity

2 Fe2+ + NADP+ = 2 Fe3+ + NADPH.

Cofactor

FAD Probable.

Heme By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Induction

By transcription factors AFT1 and AFT2 upon iron deprivation. Ref.5 Ref.4 Ref.6 Ref.7 Ref.9 Ref.11

Sequence similarities

Belongs to the ferric reductase (FRE) family.

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 711688Ferric/cupric reductase transmembrane component 2
PRO_0000010138

Regions

Topological domain24 – 164141Extracellular Potential
Transmembrane165 – 185211 Potential
Topological domain186 – 23550Cytoplasmic Potential
Transmembrane236 – 256212 Potential
Topological domain257 – 28024Extracellular Potential
Transmembrane281 – 301213 Potential
Topological domain302 – 31716Cytoplasmic Potential
Transmembrane318 – 340234 Potential
Topological domain341 – 35313Extracellular Potential
Transmembrane354 – 374215 Potential
Topological domain375 – 3773Cytoplasmic Potential
Transmembrane378 – 398216 Potential
Topological domain399 – 4002Extracellular Potential
Transmembrane401 – 423237 Potential
Topological domain424 – 711288Cytoplasmic Potential
Domain280 – 414135Ferric oxidoreductase
Domain415 – 534120FAD-binding FR-type
Nucleotide binding479 – 4857FAD Potential
Nucleotide binding526 – 5294NADP Potential
Nucleotide binding677 – 6782NADP Potential

Sites

Metal binding3161Iron (heme 1 axial ligand) By similarity
Metal binding3301Iron (heme 2 axial ligand) By similarity
Metal binding3861Iron (heme 1 axial ligand) By similarity
Metal binding4001Iron (heme 2 axial ligand) By similarity

Amino acid modifications

Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation1081N-linked (GlcNAc...) Potential
Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
P36033-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 3C60346577C80E53

FASTA71180,072
        10         20         30         40         50         60 
MHWTSILSAI LLFCLSGARA SPAKTVIRNK VPLLVTNACT RIFQKVTWEY TSKSKRSSPV 

        70         80         90        100        110        120 
CSYEPAFQSM LYCIYETLDE KGYSNKTLEK TFSTIKKNCA SYSDALQNMT NSEFYDVLNN 

       130        140        150        160        170        180 
GTRHMTPYVK GSANLTYPVE MDTQLRKAYY HALHGFYANL DVGNIYGGII CAYFVAIMAF 

       190        200        210        220        230        240 
AGVLHCMNYT PFKTVLLKQK LVGYVRGYLT LPTIGSKHAS DFSYFRIFTG YLPTRLEGII 

       250        260        270        280        290        300 
ILGYLVLHTV FLAYGYEYDP ENIIFKSRRV QVARYVADRS GVLAFAHFPL IVLFAGRNNF 

       310        320        330        340        350        360 
LEYISGVKYT SFIMFHKWLG RMMFLDAMIH GSAYTSYTVA NKTWATSKNR LYWQFGVAAL 

       370        380        390        400        410        420 
CLAGTMVFFS FAVFRKYFYE AFLFLHIVLG AMFFYACWEH VVSLSGIEWI YTAIAIWIVD 

       430        440        450        460        470        480 
RIIRIIKASY FGFPKASLQL IGDDLIRLTV KKPARPWRAK PGQYVFVSFL HPLYFWQSHP 

       490        500        510        520        530        540 
FTVLDSVSKN GELVIILKEK KGVTRLVKKY VCRNGGKTSM RLAIEGPYGS SSPVNNYNNV 

       550        560        570        580        590        600 
LLLTGGTGLP GPIAHAIKLG KTSAAAGKQS VKLVIAVRGF DVLEAYKPEL MCLENLNVQL 

       610        620        630        640        650        660 
HIYNTMEVPS LTPSDSLDIS QQDEKADEKG TVVATTLEKS ANPLGFDGVV FHCGRPNVKE 

       670        680        690        700        710 
LLHEAAELSG SLSVVCCGPP IFVDKVRNET AKIVLDKSAK AIEYFEEYQC W

« Hide

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References

« Hide 'large scale' references
[1]"Sequencing of a 13.2 kb segment next to the left telomere of yeast chromosome XI revealed five open reading frames and recent recombination events with the right arms of chromosomes III and V."
Alexandraki D., Tzermia M.
Yeast 10:S81-S91(1994) [PubMed: 8091865] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed: 8196765] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Two distinctly regulated genes are required for ferric reduction, the first step of iron uptake in Saccharomyces cerevisiae."
Georgatsou E., Alexandraki D.
Mol. Cell. Biol. 14:3065-3073(1994) [PubMed: 8164662] [Abstract]
Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.
Strain: ATCC 204508 / S288c.
[4]"AFT1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae."
Yamaguchi-Iwai Y., Dancis A., Klausner R.D.
EMBO J. 14:1231-1239(1995) [PubMed: 7720713] [Abstract]
Cited for: INDUCTION.
[5]"The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Mac1p activator."
Georgatsou E., Mavrogiannis L.A., Fragiadakis G.S., Alexandraki D.
J. Biol. Chem. 272:13786-13792(1997) [PubMed: 9153234] [Abstract]
Cited for: FUNCTION, INDUCTION.
[6]"The AFT1 transcriptional factor is differentially required for expression of high-affinity iron uptake genes in Saccharomyces cerevisiae."
Casas C., Aldea M., Espinet C., Gallego C., Gil R., Herrero E.
Yeast 13:621-637(1997) [PubMed: 9200812] [Abstract]
Cited for: INDUCTION.
[7]"Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae."
Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.
J. Biol. Chem. 273:23716-23721(1998) [PubMed: 9726978] [Abstract]
Cited for: INDUCTION.
[8]Erratum
Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.
J. Biol. Chem. 273:30056-30056(1998)
[9]"Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu reductase related genes."
Georgatsou E., Alexandraki D.
Yeast 15:573-584(1999) [PubMed: 10341420] [Abstract]
Cited for: INDUCTION.
[10]"The role of the FRE family of plasma membrane reductases in the uptake of siderophore-iron in Saccharomyces cerevisiae."
Yun C.-W., Bauler M., Moore R.E., Klebba P.E., Philpott C.C.
J. Biol. Chem. 276:10218-10223(2001) [PubMed: 11120744] [Abstract]
Cited for: FUNCTION.
[11]"Direct activation of genes involved in intracellular iron use by the yeast iron-responsive transcription factor Aft2 without its paralog Aft1."
Courel M., Lallet S., Camadro J.-M., Blaiseau P.-L.
Mol. Cell. Biol. 25:6760-6771(2005) [PubMed: 16024809] [Abstract]
Cited for: INDUCTION BY AFT1 AND AFT2.
[12]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

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Cross-references

Sequence databases

X75950 Genomic DNA. Translation: CAA53553.1.
Z28220 Genomic DNA. Translation: CAA82065.1.
PIRS38063.
RefSeqNP_012702.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:7473N.
STRINGP36033.

Genome annotation databases

EnsemblYKL220C; YKL220C; YKL220C; Saccharomyces cerevisiae. [Genome view]
GeneID853660.
KEGGsce:YKL220C.
NMPDRfig|4932.3.peg.3680.

Organism-specific databases

CYGDYKL220c.
SGDS000001703. FRE2.

Phylogenomic databases

HOGENOMP36033.
OMAEEINEAN
OrthoDBEOG9QZ930

Enzyme and pathway databases

BRENDA1.16.1.7. 250.

Gene expression databases

ArrayExpressP36033.
GenevestigatorP36033.
GermOnlineYKL220C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR013112. FAD_bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_reduct_TM_N.
IPR013121. Fe_red_NAD_bd_6.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio974584.

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Entry information

Entry nameFRE2_YEAST
AccessionPrimary (citable) accession number: P36033
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 24, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents