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Identification
NameFerric/cupric reductase transmembrane component 1
Synonyms
  • Ferric-chelate reductase 1
Gene NameFRE1
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
electron carrier activity
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
FAD or FADH2 binding
ion binding
cation binding
metal ion binding
transition metal ion binding
iron ion binding
oxidoreductase activity
catalytic activity
Process
oxidation reduction
metabolic process
Gene Properties
Chromosome Locationchromosome 12
LocusYLR214W
Gene Sequence>2061 bp ATGGTTAGAACCCGTGTATTATTCTGCTTATTTATATCTTTTTTTGCTACGGTTCAATCG AGTGCTACACTTATTAGCACTTCATGTATTTCCCAAGCTGCGCTATACCAATTTGGATGT TCTAGTAAATCTAAAAGTTGCTACTGTAAAAACATCAATTGGCTGGGTTCAGTGACAGCA TGTGCCTATGAGAATTCCAAATCTAACAAAACACTAGACAGCGCCTTAATGAAGTTAGCA TCCCAATGTTCAAGCATCAAAGTTTATACTTTAGAGGACATGAAGAATATTTATTTAAAT GCGTCAAATTATTTGAGAGCACCTGAGAAAAGTGATAAAAAAACCGTGGTTAGTCAACCG CTCATGGCGAACGAGACAGCGTATCATTATTATTATGAGGAAAATTATGGTATCCATCTT AACCTAATGCGCTCTCAATGGTGCGCTTGGGGTCTCGTCTTCTTCTGGGTGGCTGTGCTT ACTGCAGCCACTATCTTGAACATTCTGAAAAGGGTGTTTGGTAAGAACATCATGGCAAAC TCCGTCAAAAAATCACTTATTTATCCTTCTGTTTACAAAGATTATAATGAACGAACTTTT TATTTATGGAAGCGTCTACCATTTAATTTTACAACTCGAGGCAAGGGTCTCGTCGTATTA ATTTTTGTTATTTTGACTATATTATCTCTCAGTTTTGGTCATAATATTAAACTTCCACAC CCATATGATAGGCCCAGATGGAGAAGAAGTATGGCCTTTGTGAGTCGTAGAGCAGACTTG ATGGCCATTGCACTTTTCCCAGTAGTCTATCTATTCGGAATAAGAAATAATCCCTTCATC CCTATAACAGGGCTTTCCTTTTCTACATTTAATTTCTATCATAAATGGTCTGCCTACGTT TGTTTCATGTTGGCCGTTGTACACTCAATTGTCATGACCGCCTCGGGAGTGAAAAGAGGT GTGTTTCAAAGTCTGGTTAGGAAATTTTACTTTAGGTGGGGTATAGTGGCAACGATATTA ATGTCTATTATTATTTTCCAAAGTGAAAAAGTATTTAGAAATAGAGGGTATGAGATATTC CTTCTTATTCATAAAGCGATGAATATTATGTTCATTATTGCCATGTACTACCATTGTCAC ACCCTGGGCTGGATGGGTTGGATTTGGTCAATGGCTGGTATTTTATGCTTTGATAGATTC TGCAGGATTGTTAGAATAATCATGAATGGTGGCTTGAAAACTGCTACTTTGAGTACCACT GATGATTCTAATGTTATTAAAATTTCAGTAAAAAAACCAAAGTTTTTCAAGTACCAAGTA GGAGCTTTCGCATACATGTATTTCTTATCACCAAAAAGTGCATGGTTCTATAGTTTCCAA TCACATCCATTTACAGTATTATCGGAACGACACCGTGATCCAAACAATCCAGATCAATTG ACGATGTACGTAAAGGCAAATAAAGGTATCACTCGAGTTTTGTTATCGAAAGTTCTAAGT GCTCCAAATCATACTGTTGATTGTAAAATATTCCTTGAAGGCCCATATGGTGTAACGGTT CCACATATCGCTAAGCTAAAAAGAAATCTGGTAGGTGTAGCCGCTGGTTTGGGTGTTGCG GCTATTTATCCGCACTTTGTCGAATGTTTACGGTTACCATCTACTGATCAACTTCAGCAT AAATTTTACTGGATTGTTAATGACCTATCCCATTTGAAATGGTTTGAAAATGAATTGCAA TGGTTAAAGGAGAAAAGTTGTGAAGTCTCAGTCATATATACTGGTTCCAGTGTTGAGGAC ACAAATTCAGATGAGAGTACAAAAGGTTTTGATGATAAAGAAGAAAGCGAAATCACTGTT GAATGTCTCAATAAAAGACCTGATTTGAAAGAACTAGTGCGCTCGGAAATAAAACTCTCA GAACTAGAGAATAATAATATTACCTTTTATTCCTGCGGGCCAGCAACGTTTAACGACGAT TTTAGAAATGCAGTGGTCCAAGGTATAGACTCTTCCTTGAAGATTGACGTTGAACTAGAA GAAGAAAGTTTTACATGGTAA
Protein Properties
Pfam Domain Function
Protein Residues686
Protein Molecular Weight78853.0
Protein Theoretical pI9.49
Signalling Regions
  • 1-22
Transmembrane Regions
  • 149-169
  • 216-236
  • 260-280
  • 297-317
  • 329-349
  • 359-378
  • 384-401
Protein Sequence>Ferric/cupric reductase transmembrane component 1 MVRTRVLFCLFISFFATVQSSATLISTSCISQAALYQFGCSSKSKSCYCKNINWLGSVTA CAYENSKSNKTLDSALMKLASQCSSIKVYTLEDMKNIYLNASNYLRAPEKSDKKTVVSQP LMANETAYHYYYEENYGIHLNLMRSQWCAWGLVFFWVAVLTAATILNILKRVFGKNIMAN SVKKSLIYPSVYKDYNERTFYLWKRLPFNFTTRGKGLVVLIFVILTILSLSFGHNIKLPH PYDRPRWRRSMAFVSRRADLMAIALFPVVYLFGIRNNPFIPITGLSFSTFNFYHKWSAYV CFMLAVVHSIVMTASGVKRGVFQSLVRKFYFRWGIVATILMSIIIFQSEKVFRNRGYEIF LLIHKAMNIMFIIAMYYHCHTLGWMGWIWSMAGILCFDRFCRIVRIIMNGGLKTATLSTT DDSNVIKISVKKPKFFKYQVGAFAYMYFLSPKSAWFYSFQSHPFTVLSERHRDPNNPDQL TMYVKANKGITRVLLSKVLSAPNHTVDCKIFLEGPYGVTVPHIAKLKRNLVGVAAGLGVA AIYPHFVECLRLPSTDQLQHKFYWIVNDLSHLKWFENELQWLKEKSCEVSVIYTGSSVED TNSDESTKGFDDKEESEITVECLNKRPDLKELVRSEIKLSELENNNITFYSCGPATFNDD FRNAVVQGIDSSLKIDVELEEESFTW
References
External Links
ResourceLink
Saccharomyces Genome Database FRE1
Uniprot IDP32791
Uniprot NameFRE1_YEAST
GenBank Gene IDM86908
Genebank Protein ID171521
General Reference
  • Dancis, A., Roman, D. G., Anderson, G. J., Hinnebusch, A. G., Klausner, R. D. (1992). "Ferric reductase of Saccharomyces cerevisiae: molecular characterization, role in iron uptake, and transcriptional control by iron." Proc Natl Acad Sci U S A 89:3869-3873.1570306
  • Johnston, M., Hillier, L., Riles, L., Albermann, K., Andre, B., Ansorge, W., Benes, V., Bruckner, M., Delius, H., Dubois, E., Dusterhoft, A., Entian, K. D., Floeth, M., Goffeau, A., Hebling, U., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hilger, F., Kleine, K., Kotter, P., Louis, E. J., Messenguy, F., Mewes, H. W., Hoheisel, J. D., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Nature 387:87-90.9169871
  • Anderson, G. J., Lesuisse, E., Dancis, A., Roman, D. G., Labbe, P., Klausner, R. D. (1992). "Ferric iron reduction and iron assimilation in Saccharomyces cerevisiae." J Inorg Biochem 47:249-255.1431884
  • 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
  • Hassett, R., Kosman, D. J. (1995). "Evidence for Cu(II) reduction as a component of copper uptake by Saccharomyces cerevisiae." J Biol Chem 270:128-134.7814363
  • Lesuisse, E., Casteras-Simon, M., Labbe, P. (1996). "Evidence for the Saccharomyces cerevisiae ferrireductase system being a multicomponent electron transport chain." J Biol Chem 271:13578-13583.8662826
  • Shatwell, K. P., Dancis, A., Cross, A. R., Klausner, R. D., Segal, A. W. (1996). "The FRE1 ferric reductase of Saccharomyces cerevisiae is a cytochrome b similar to that of NADPH oxidase." J Biol Chem 271:14240-14244.8662973
  • Finegold, A. A., Shatwell, K. P., Segal, A. W., Klausner, R. D., Dancis, A. (1996). "Intramembrane bis-heme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase." J Biol Chem 271:31021-31024.8940093
  • 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
  • Shi, X., Stoj, C., Romeo, A., Kosman, D. J., Zhu, Z. (2003). "Fre1p Cu2+ reduction and Fet3p Cu1+ oxidation modulate copper toxicity in Saccharomyces cerevisiae." J Biol Chem 278:50309-50315.12954629
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Shinyashiki, M., Pan, C. J., Lopez, B. E., Fukuto, J. M. (2004). "Inhibition of the yeast metal reductase heme protein fre1 by nitric oxide (NO): a model for inhibition of NADPH oxidase by NO." Free Radic Biol Med 37:713-723.15288128
  • Ramalho, P. A., Paiva, S., Cavaco-Paulo, A., Casal, M., Cardoso, M. H., Ramalho, M. T. (2005). "Azo reductase activity of intact saccharomyces cerevisiae cells is dependent on the Fre1p component of plasma membrane ferric reductase." Appl Environ Microbiol 71:3882-3888.16000801
  • 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
  • Aronova, S., Wedaman, K., Anderson, S., Yates, J. 3rd, Powers, T. (2007). "Probing the membrane environment of the TOR kinases reveals functional interactions between TORC1, actin, and membrane trafficking in Saccharomyces cerevisiae." Mol Biol Cell 18:2779-2794.17507646