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Protein

Ferric reductase transmembrane component 6

Gene

FRE6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Metalloreductase responsible for reducing vacuolar iron and copper prior to transport into the cytosol. Catalyzes the reduction of Fe3+ to Fe2+ and Cu2+ to Cu+, respectively, which can then be transported by the respective vacuolar efflux systems to the cytosol.2 Publications

Catalytic activityi

2 Fe(II)-siderophore + NADP+ + H+ = 2 Fe(III)-siderophore + NADPH.

Cofactori

FADCurated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi323 – 3231Iron (heme 1 axial ligand)By similarity
Metal bindingi337 – 3371Iron (heme 2 axial ligand)By similarity
Metal bindingi393 – 3931Iron (heme 1 axial ligand)By similarity
Metal bindingi407 – 4071Iron (heme 2 axial ligand)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi493 – 4997FADSequence analysis
Nucleotide bindingi538 – 5414NADPSequence analysis
Nucleotide bindingi678 – 6792NADPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • copper ion import Source: SGD
  • intracellular sequestering of iron ion Source: SGD
  • iron ion transport Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Ion transport, Iron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciYEAST:G3O-32150-MONOMER.

Protein family/group databases

TCDBi5.B.1.7.1. the phagocyte (gp91(phox)) nadph oxidase family.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferric reductase transmembrane component 6 (EC:1.16.1.9)
Alternative name(s):
Ferric-chelate reductase 6
Gene namesi
Name:FRE6
Ordered Locus Names:YLL051C
ORF Names:L0593
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLL051C.
SGDiS000003974. FRE6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 167150VacuolarSequence analysisAdd
BLAST
Transmembranei168 – 18821Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini189 – 24456CytoplasmicSequence analysisAdd
BLAST
Transmembranei245 – 26521Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini266 – 28722VacuolarSequence analysisAdd
BLAST
Transmembranei288 – 30821Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini309 – 32820CytoplasmicSequence analysisAdd
BLAST
Transmembranei329 – 34921Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini350 – 36011VacuolarSequence analysisAdd
BLAST
Transmembranei361 – 38121Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini382 – 3876CytoplasmicSequence analysis
Transmembranei388 – 40821Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini409 – 4168VacuolarSequence analysis
Transmembranei417 – 43721Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini438 – 712275CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi493 – 4964HPFT → AAAA: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 712695Ferric reductase transmembrane component 6PRO_0000010142Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi89 – 891N-linked (GlcNAc...)Sequence analysis
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence analysis
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ12473.

PTM databases

iPTMnetiQ12473.

Expressioni

Inductioni

By transcription factor AFT2 upon iron deprivation.3 Publications

Interactioni

Protein-protein interaction databases

BioGridi31264. 10 interactions.
DIPiDIP-5019N.
MINTiMINT-565619.

Structurei

3D structure databases

ProteinModelPortaliQ12473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini287 – 411125Ferric oxidoreductaseAdd
BLAST
Domaini412 – 546135FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi553 – 5564Poly-Leu

Sequence similaritiesi

Belongs to the ferric reductase (FRE) family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 ferric oxidoreductase domain.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000007891.
HOGENOMiHOG000000805.
InParanoidiQ12473.
KOiK00521.
OMAiFLLFHRW.
OrthoDBiEOG7PGF10.

Family and domain databases

InterProiIPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q12473-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHRTLLFLTW LISLTKAFNI KLPHTEKKDH LESNAVLACA SYINTLKWSF
60 70 80 90 100
DSSVVPGFYS TICSYSPAFD TWSLCIFNSL TDQIIPMDNT SFEESLGNVR
110 120 130 140 150
KTCSFVDKKF SNISLEQYYS SLNNASSHAL EDYGSIESLS TSIRVDRETR
160 170 180 190 200
SRWIRAFHAH AYNLDISSVY GAYLTYYFVI VGIIAVFFHM SHYNGLNRAL
210 220 230 240 250
FASRFVNYIR GHFVLPTFLV DKHANHFKFL NVEVFTGLMP NSLEAWIIFG
260 270 280 290 300
YTLANIIFLS ISYIIDPYNL IFNSHLSQFT RLLADRSGIL AFTQFPLIII
310 320 330 340 350
FTARNSFLEF LTGVKFNSFI SFHKWIGRIM VLNATIHSLS YSLFAIINHA
360 370 380 390 400
FKISNKQLYW KFGIASITVL CVLLVLSLGI VRKRHYEFFL YTHIILALLF
410 420 430 440 450
FYCCWQHVKI FNGWKEWIVV SLLIWGLEKL FRIWNILQFR FPKATLINLN
460 470 480 490 500
TSNNPHDEMF KVIIPKYNRR WHSKPGQYCF IYFLHPLVFW QCHPFTIIDE
510 520 530 540 550
GEKCVLVIKP KSGLTRFIYN HILQSLNGKL QLRVAIEGPY GPSNLHLDKF
560 570 580 590 600
DHLLLLSGGT GLPGPLDHAI KLSRNPDKPK SIDLIMAIKN PSFLNGYKSE
610 620 630 640 650
ILELKNSRSH VNVQVYLTQK TAVTKAANAR DQLIHFDDIM TELTSFAHIG
660 670 680 690 700
NARPNFSNVI ENAIKSTPPG DSLAVVCCGP PVLVDDVRNT VSQKLLGYPE
710
RIIEYFEEYQ CW
Length:712
Mass (Da):81,989
Last modified:November 1, 1996 - v1
Checksum:i5224F12B51544BAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47973 Genomic DNA. Translation: CAA88006.1.
Z73156 Genomic DNA. Translation: CAA97503.1.
BK006945 Genomic DNA. Translation: DAA09273.1.
PIRiS50969.
RefSeqiNP_013049.1. NM_001181871.1.

Genome annotation databases

EnsemblFungiiYLL051C; YLL051C; YLL051C.
GeneIDi850675.
KEGGisce:YLL051C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47973 Genomic DNA. Translation: CAA88006.1.
Z73156 Genomic DNA. Translation: CAA97503.1.
BK006945 Genomic DNA. Translation: DAA09273.1.
PIRiS50969.
RefSeqiNP_013049.1. NM_001181871.1.

3D structure databases

ProteinModelPortaliQ12473.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31264. 10 interactions.
DIPiDIP-5019N.
MINTiMINT-565619.

Protein family/group databases

TCDBi5.B.1.7.1. the phagocyte (gp91(phox)) nadph oxidase family.

PTM databases

iPTMnetiQ12473.

Proteomic databases

MaxQBiQ12473.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLL051C; YLL051C; YLL051C.
GeneIDi850675.
KEGGisce:YLL051C.

Organism-specific databases

EuPathDBiFungiDB:YLL051C.
SGDiS000003974. FRE6.

Phylogenomic databases

GeneTreeiENSGT00390000007891.
HOGENOMiHOG000000805.
InParanoidiQ12473.
KOiK00521.
OMAiFLLFHRW.
OrthoDBiEOG7PGF10.

Enzyme and pathway databases

BioCyciYEAST:G3O-32150-MONOMER.

Miscellaneous databases

PROiQ12473.

Family and domain databases

InterProiIPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  4. Erratum
    Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.
    J. Biol. Chem. 273:30056-30056(1998)
  5. "Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu reductase related genes."
    Georgatsou E., Alexandraki D.
    Yeast 15:573-584(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. "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] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY AFT2.
  8. "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] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  9. "Identification of a vacuole-associated metalloreductase and its role in Ctr2-mediated intracellular copper mobilization."
    Rees E.M., Thiele D.J.
    J. Biol. Chem. 282:21629-21638(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A REDUCTASE, SUBCELLULAR LOCATION, MUTAGENESIS OF 493-HIS--THR-496.
  10. "The metalloreductase Fre6p in Fe-efflux from the yeast vacuole."
    Singh A., Kaur N., Kosman D.J.
    J. Biol. Chem. 282:28619-28626(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A REDUCTASE ACTIVITY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFRE6_YEAST
AccessioniPrimary (citable) accession number: Q12473
Secondary accession number(s): D6VXV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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.