You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Yeast Metabolome Database.
Identification
NameFerric/cupric reductase transmembrane component 2
Synonyms
  • Ferric-chelate reductase 2
Gene NameFRE2
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionMetalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake
Cellular LocationCell membrane; Multi-pass membrane protein
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00194Iron(3+)Show
YMDB00379Iron(2+)Show
YMDB00426NADPHShow
YMDB00427NADPShow
GO Classification
Component
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
metal ion binding
transition metal ion binding
iron ion binding
catalytic activity
oxidoreductase activity
electron carrier activity
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
FAD or FADH2 binding
ion binding
cation binding
Process
metabolic process
oxidation reduction
Gene Properties
Chromosome Locationchromosome 11
LocusYKL220C
Gene Sequence>2136 bp ATGCATTGGACGTCCATCTTGAGCGCTATTTTGCTTTTCTGCCTGTCAGGAGCAAGAGCA TCACCTGCAAAGACAGTTATTCGTAACAAGGTGCCCTTGCTTGTCACTAATGCCTGCACG AGGATTTTTCAAAAAGTTACTTGGGAGTATACCAGCAAGTCTAAGCGTTCATCACCAGTA TGTTCTTACGAACCAGCGTTTCAATCAATGCTGTATTGTATCTATGAAACGTTGGATGAA AAAGGTTATTCGAATAAAACCTTAGAAAAAACATTTAGTACCATCAAAAAAAACTGTGCA AGTTATAGTGATGCTCTTCAGAACATGACTAATTCTGAGTTTTATGACGTTCTAAACAAC GGAACGAGGCATATGACGCCCTATGTCAAAGGCAGTGCAAACCTAACATATCCAGTTGAA ATGGATACACAGTTAAGAAAAGCCTACTATCATGCATTGCATGGTTTCTATGCTAACTTA GATGTCGGAAACATATATGGTGGCATTATATGTGCTTATTTTGTCGCTATCATGGCTTTT GCAGGCGTTCTTCATTGCATGAATTACACTCCCTTTAAAACTGTTCTATTGAAGCAAAAG CTTGTGGGATATGTAAGGGGATACCTCACTCTACCTACCATTGGAAGCAAACATGCGTCA GATTTCTCTTATTTTAGAATATTCACAGGATATTTACCTACAAGATTAGAGGGTATCATT ATTCTTGGATATCTCGTGCTTCATACCGTTTTTTTGGCATACGGTTATGAATACGATCCT GAAAATATAATATTCAAGTCTCGTAGAGTTCAAGTTGCTCGATATGTGGCAGACAGAAGT GGTGTACTCGCATTCGCACACTTTCCATTAATAGTTCTTTTCGCGGGAAGAAACAACTTT CTCGAGTATATTTCTGGGGTTAAATATACTTCCTTCATTATGTTTCACAAATGGTTGGGA AGAATGATGTTTTTGGATGCTATGATTCATGGCTCTGCATATACTAGTTATACGGTAGCG AATAAAACTTGGGCAACAAGTAAAAACCGATTATATTGGCAATTCGGGGTGGCAGCACTT TGTTTAGCTGGCACAATGGTTTTCTTTTCCTTTGCAGTATTCAGGAAGTATTTTTATGAA GCCTTTCTTTTTCTTCATATCGTCCTTGGTGCAATGTTCTTTTATGCATGTTGGGAGCAT GTTGTTAGTTTAAGTGGCATTGAGTGGATATACACTGCTATTGCGATTTGGATCGTTGAC CGGATTATTAGAATTATCAAAGCTTCTTATTTTGGTTTCCCCAAAGCTTCCCTACAACTA ATCGGGGATGATCTCATTCGTTTAACAGTTAAAAAACCGGCAAGGCCATGGAGGGCCAAA CCTGGGCAATATGTTTTCGTTTCGTTTTTACATCCACTGTACTTCTGGCAGTCACATCCA TTTACTGTTTTGGATTCAGTAAGCAAGAATGGTGAACTGGTTATTATCCTGAAAGAAAAA AAGGGAGTAACAAGACTTGTCAAAAAGTATGTGTGTCGCAATGGAGGTAAGACATCTATG AGACTAGCTATAGAAGGTCCATATGGTTCTTCATCTCCGGTCAATAATTACAATAATGTA TTGTTACTCACTGGAGGTACCGGTTTGCCTGGACCTATTGCACATGCAATTAAACTTGGA AAGACGTCAGCGGCTGCTGGAAAACAATCTGTAAAATTAGTGATTGCAGTTAGAGGATTC GACGTACTCGAGGCTTATAAGCCGGAGTTGATGTGTTTAGAAAATCTGAATGTACAGCTT CACATCTACAACACAATGGAAGTCCCATCATTAACCCCTAGTGATAGTTTAGATATTTCT CAACAGGATGAGAAGGCTGATGAAAAAGGCACTGTTGTGGCAACTACTTTAGAAAAGTCT GCCAATCCACTTGGTTTTGATGGTGTTGTTTTCCATTGCGGGCGACCAAATGTTAAGGAA CTTCTACATGAAGCGGCTGAATTGAGTGGCTCATTATCTGTGGTTTGCTGTGGACCTCCT ATTTTTGTTGACAAAGTGAGGAATGAAACCGCAAAAATAGTTTTAGATAAGTCTGCAAAA GCCATTGAGTACTTTGAAGAGTATCAATGCTGGTGA
Protein Properties
Pfam Domain Function
Protein Residues711
Protein Molecular Weight80071.5
Protein Theoretical pI9.39
Signalling Regions
  • 1-23
Transmembrane Regions
  • 165-185
  • 236-256
  • 281-301
  • 318-340
  • 354-374
  • 378-398
  • 401-423
Protein Sequence>Ferric/cupric reductase transmembrane component 2 MHWTSILSAILLFCLSGARASPAKTVIRNKVPLLVTNACTRIFQKVTWEYTSKSKRSSPV CSYEPAFQSMLYCIYETLDEKGYSNKTLEKTFSTIKKNCASYSDALQNMTNSEFYDVLNN GTRHMTPYVKGSANLTYPVEMDTQLRKAYYHALHGFYANLDVGNIYGGIICAYFVAIMAF AGVLHCMNYTPFKTVLLKQKLVGYVRGYLTLPTIGSKHASDFSYFRIFTGYLPTRLEGII ILGYLVLHTVFLAYGYEYDPENIIFKSRRVQVARYVADRSGVLAFAHFPLIVLFAGRNNF LEYISGVKYTSFIMFHKWLGRMMFLDAMIHGSAYTSYTVANKTWATSKNRLYWQFGVAAL CLAGTMVFFSFAVFRKYFYEAFLFLHIVLGAMFFYACWEHVVSLSGIEWIYTAIAIWIVD RIIRIIKASYFGFPKASLQLIGDDLIRLTVKKPARPWRAKPGQYVFVSFLHPLYFWQSHP FTVLDSVSKNGELVIILKEKKGVTRLVKKYVCRNGGKTSMRLAIEGPYGSSSPVNNYNNV LLLTGGTGLPGPIAHAIKLGKTSAAAGKQSVKLVIAVRGFDVLEAYKPELMCLENLNVQL HIYNTMEVPSLTPSDSLDISQQDEKADEKGTVVATTLEKSANPLGFDGVVFHCGRPNVKE LLHEAAELSGSLSVVCCGPPIFVDKVRNETAKIVLDKSAKAIEYFEEYQCW
References
External Links
ResourceLink
Saccharomyces Genome Database FRE2
Uniprot IDP36033
Uniprot NameFRE2_YEAST
GenBank Gene IDX75950
Genebank Protein ID473129
General Reference
  • Alexandraki, D., Tzermia, M. (1994). "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." Yeast 10 Suppl A:S81-S91.8091865
  • Dujon, B., Alexandraki, D., Andre, B., Ansorge, W., Baladron, V., Ballesta, J. P., Banrevi, A., Bolle, P. A., Bolotin-Fukuhara, M., Bossier, P., et, a. l. .. (1994). "Complete DNA sequence of yeast chromosome XI." Nature 369:371-378.8196765
  • Georgatsou, E., Alexandraki, D. (1994). "Two distinctly regulated genes are required for ferric reduction, the first step of iron uptake in Saccharomyces cerevisiae." Mol Cell Biol 14:3065-3073.8164662
  • Yamaguchi-Iwai, Y., Dancis, A., Klausner, R. D. (1995). "AFT1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae." EMBO J 14:1231-1239.7720713
  • Georgatsou, E., Mavrogiannis, L. A., Fragiadakis, G. S., Alexandraki, D. (1997). "The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Mac1p activator." J Biol Chem 272:13786-13792.9153234
  • Casas, C., Aldea, M., Espinet, C., Gallego, C., Gil, R., Herrero, E. (1997). "The AFT1 transcriptional factor is differentially required for expression of high-affinity iron uptake genes in Saccharomyces cerevisiae." Yeast 13:621-637.9200812
  • Martins, L. J., Jensen, L. T., Simon, J. R., Keller, G. L., Winge, D. R. (1998). "Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae." J Biol Chem 273:23716-23721.9726978
  • Georgatsou, E., Alexandraki, D. (1999). "Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu reductase related genes." Yeast 15:573-584.10341420
  • Yun, C. W., Bauler, M., Moore, R. E., Klebba, P. E., Philpott, C. C. (2001). "The role of the FRE family of plasma membrane reductases in the uptake of siderophore-iron in Saccharomyces cerevisiae." J Biol Chem 276:10218-10223.11120744
  • Courel, M., Lallet, S., Camadro, J. M., Blaiseau, P. L. (2005). "Direct activation of genes involved in intracellular iron use by the yeast iron-responsive transcription factor Aft2 without its paralog Aft1." Mol Cell Biol 25:6760-6771.16024809
  • Kim, H., Melen, K., Osterberg, M., von Heijne, G. (2006). "A global topology map of the Saccharomyces cerevisiae membrane proteome." Proc Natl Acad Sci U S A 103:11142-11147.16847258