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Protein

Ferric reductase transmembrane component 4

Gene

FRE4

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

Functioni

Siderophore-iron reductase responsible for reducing extracellular iron prior to import. Catalyzes the reductive uptake of Fe3+ bound to dihydroxamate rhodotorulic acid. 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.1 Publication

Catalytic activityi

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

Cofactori

FADCurated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi309 – 3091Iron (heme 1 axial ligand)By similarity
Metal bindingi323 – 3231Iron (heme 2 axial ligand)By similarity
Metal bindingi379 – 3791Iron (heme 1 axial ligand)By similarity
Metal bindingi393 – 3931Iron (heme 2 axial ligand)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi472 – 4787FADSequence analysis
Nucleotide bindingi519 – 5224NADPSequence analysis
Nucleotide bindingi685 – 6862NADPSequence analysis

GO - Molecular functioni

  • ferric-chelate reductase (NADPH) activity Source: UniProtKB-EC
  • ferric-chelate reductase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • ion transport Source: UniProtKB-KW
  • iron ion homeostasis Source: UniProtKB-KW
  • siderophore transport Source: SGD
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-33364-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferric reductase transmembrane component 4 (EC:1.16.1.9)
Alternative name(s):
Ferric-chelate reductase 4
Gene namesi
Name:FRE4
Ordered Locus Names:YNR060W
ORF Names:N3518
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNR060W.
SGDiS000005343. FRE4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 156138ExtracellularBy similarityAdd
BLAST
Transmembranei157 – 17721Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini178 – 22851CytoplasmicBy similarityAdd
BLAST
Transmembranei229 – 24921Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini250 – 26718ExtracellularBy similarityAdd
BLAST
Transmembranei268 – 28821Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini289 – 30416CytoplasmicBy similarityAdd
BLAST
Transmembranei305 – 32521Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini326 – 34621ExtracellularBy similarityAdd
BLAST
Transmembranei347 – 36721Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini368 – 3736CytoplasmicBy similarity
Transmembranei374 – 39421Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini395 – 3951ExtracellularBy similarity
Transmembranei396 – 41621Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini417 – 719303CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 719701Ferric reductase transmembrane component 4PRO_0000010140Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...)Sequence analysis
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence analysis
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence analysis
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence analysis
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence analysis
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

PTM databases

iPTMnetiP53746.

Expressioni

Inductioni

By iron deprivation.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi35886. 13 interactions.
DIPiDIP-7626N.
IntActiP53746. 1 interaction.
MINTiMINT-1354495.

Structurei

3D structure databases

ProteinModelPortaliP53746.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini273 – 407135Ferric oxidoreductaseAdd
BLAST
Domaini408 – 527120FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiP53746.
KOiK00521.
OMAiTDVKETY.
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.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P53746-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLVHIISFL LFFQLSAAKA PPSKTSLINT HERRSIYSCY VGLRKETWGF
60 70 80 90 100
NGSAICRYEP AIQSMLYCLY EDTHEKGYSN KTLEKGFEEM RQFCYTPKFL
110 120 130 140 150
NMTDAEFYTS LDNGTYYIQD QPKAGINITY PIRLNTTLRK AYYDAYYGYY
160 170 180 190 200
YNHDIPYYFG GIICAYFVGV MLLAGLIRFL NYTPIKKIMF QQKLVNYVRG
210 220 230 240 250
YTTLPTLYEK HAEPFSYLKV ITGYLPTRFE TLVILGYLIL HTIFMAYKYQ
260 270 280 290 300
YDPYHIIFAA HRAEVAHFVA YRSGILSFAH LPLIVLFAGR NNFLQLISGL
310 320 330 340 350
KHTSFIVFHK WLGRMMFLDA IIHAAGFTNY YLYYKKWNTV RLRVYWKFGI
360 370 380 390 400
ATTCLAGMLI FFSIAAFRRH YYETFMALHI VFAALFLYTC WEHVTNFSGI
410 420 430 440 450
EWIYAAIAIW GVDRIVRITR IALLGFPKAD LQLVGSDLVR VTVKKPKKFW
460 470 480 490 500
KAKPGQYVFV SFLRPLCFWQ SHPFTVMDSC VNDRELVIVL KAKKGVTKLV
510 520 530 540 550
RNFVERKGGK ASMRLAIEGP YGSKSTAHRF DNVLLLAGGS GLPGPISHAL
560 570 580 590 600
ELGKTTAASG KNFVQLVIAV RGLDMLNACK KELMALKGLN VQVHIYNSKQ
610 620 630 640 650
ELASAEKISS NEVKNGETTA EKAPSSLSNS EKAPSESENT ELPLSLNDTS
660 670 680 690 700
ISDLEFATFH VGRPNVEEIL NESVNHSGSL AVVCCGPPIF VDTARNQTAK
710
AVIRNPSRMI EYLEEYQAW
Length:719
Mass (Da):82,015
Last modified:October 1, 1996 - v1
Checksum:i9CA91F1F890AF1F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71675 Genomic DNA. Translation: CAA96342.1.
BK006947 Genomic DNA. Translation: DAA10601.1.
PIRiS63392.
RefSeqiNP_014458.1. NM_001183237.1.

Genome annotation databases

EnsemblFungiiYNR060W; YNR060W; YNR060W.
GeneIDi855797.
KEGGisce:YNR060W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71675 Genomic DNA. Translation: CAA96342.1.
BK006947 Genomic DNA. Translation: DAA10601.1.
PIRiS63392.
RefSeqiNP_014458.1. NM_001183237.1.

3D structure databases

ProteinModelPortaliP53746.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35886. 13 interactions.
DIPiDIP-7626N.
IntActiP53746. 1 interaction.
MINTiMINT-1354495.

PTM databases

iPTMnetiP53746.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNR060W; YNR060W; YNR060W.
GeneIDi855797.
KEGGisce:YNR060W.

Organism-specific databases

EuPathDBiFungiDB:YNR060W.
SGDiS000005343. FRE4.

Phylogenomic databases

GeneTreeiENSGT00390000007891.
HOGENOMiHOG000000805.
InParanoidiP53746.
KOiK00521.
OMAiTDVKETY.
OrthoDBiEOG7PGF10.

Enzyme and pathway databases

BioCyciYEAST:G3O-33364-MONOMER.

Miscellaneous databases

NextBioi980297.
PROiP53746.

Family and domain databases

InterProiIPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(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. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiFRE4_YEAST
AccessioniPrimary (citable) accession number: P53746
Secondary accession number(s): D6W1N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 121 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.