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Identification
NameFerric reductase transmembrane component 4
Synonyms
  • Ferric-chelate reductase 4
Gene NameFRE4
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionSiderophore-iron reductase responsible for reducing extracellular iron prior to import. Catalyzes the reductive uptake of Fe(3+) bound to dihydroxamate rhodotorulic acid. 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
Cellular LocationCell membrane; Multi-pass membrane protein (Probable)
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
intrinsic to membrane
integral to membrane
cell part
membrane part
Function
transition metal ion binding
iron ion binding
oxidoreductase activity
binding
nucleoside binding
electron carrier activity
purine nucleoside binding
adenyl nucleotide binding
FAD or FADH2 binding
catalytic activity
ion binding
cation binding
metal ion binding
Process
oxidation reduction
metabolic process
Gene Properties
Chromosome Locationchromosome 14
LocusYNR060W
Gene Sequence>2160 bp ATGTTGTTGGTACATATTATATCTTTCCTTCTGTTCTTCCAGCTTTCGGCCGCAAAGGCC CCACCCAGTAAAACGTCTCTAATAAATACTCATGAGAGAAGGTCGATATATTCATGCTAC GTTGGTTTACGTAAAGAAACATGGGGGTTCAATGGGTCCGCTATATGTCGGTATGAACCA GCAATCCAATCGATGCTTTACTGTCTTTACGAAGACACGCATGAGAAAGGGTATTCAAAT AAAACTTTGGAGAAAGGTTTTGAAGAAATGAGACAATTTTGCTATACACCAAAGTTTTTG AACATGACTGATGCCGAGTTTTACACCTCATTGGATAATGGAACATACTATATACAAGAT CAACCTAAAGCTGGCATCAATATCACTTATCCTATCAGACTGAACACTACACTAAGAAAA GCATACTATGATGCATACTATGGTTACTACTATAACCATGACATTCCGTATTATTTCGGG GGCATTATCTGTGCATACTTTGTGGGTGTCATGTTGCTTGCAGGTTTAATTCGTTTTTTG AATTATACCCCAATAAAAAAGATTATGTTTCAGCAAAAGCTAGTCAATTACGTGAGAGGT TATACTACTCTACCCACTCTTTATGAAAAGCATGCAGAGCCCTTCTCGTACTTAAAAGTG ATAACAGGCTATCTTCCTACTAGGTTTGAAACGTTGGTTATTTTAGGCTACCTCATACTT CATACCATTTTCATGGCCTACAAATATCAATATGATCCATACCACATCATATTTGCCGCT CATAGAGCAGAAGTGGCACATTTTGTTGCGTACAGAAGCGGTATACTTTCTTTTGCACAC CTGCCACTCATTGTTTTATTTGCGGGAAGAAATAACTTTCTCCAACTTATTTCTGGCTTG AAGCATACCTCATTCATTGTGTTCCATAAGTGGCTGGGAAGAATGATGTTTCTTGATGCA ATAATTCATGCTGCCGGCTTTACGAACTATTATTTGTATTATAAAAAATGGAATACGGTT AGATTAAGAGTCTACTGGAAATTCGGTATTGCTACCACCTGTTTAGCGGGAATGTTAATT TTCTTTTCCATCGCAGCATTTAGAAGACACTACTATGAAACGTTTATGGCCCTCCATATA GTATTCGCAGCACTATTTCTCTATACTTGTTGGGAGCATGTTACTAACTTCAGCGGTATC GAATGGATTTACGCGGCAATAGCAATTTGGGGAGTTGATAGAATTGTACGTATCACCAGA ATTGCACTCTTAGGATTTCCTAAAGCAGATCTACAACTGGTTGGATCTGATTTGGTCCGT GTAACGGTTAAAAAACCAAAGAAGTTTTGGAAGGCAAAACCAGGCCAATACGTTTTCGTT TCCTTCTTGCGTCCATTGTGCTTCTGGCAGTCGCATCCATTTACAGTGATGGATTCTTGC GTAAACGATAGAGAATTGGTCATCGTTCTGAAAGCAAAGAAAGGTGTGACAAAACTGGTA AGAAACTTTGTTGAACGTAAAGGCGGCAAGGCATCCATGAGATTAGCTATCGAAGGCCCT TATGGCTCCAAGTCCACCGCCCATCGCTTTGATAATGTATTATTGTTGGCAGGTGGCTCA GGGCTTCCCGGTCCAATTTCTCATGCCCTTGAATTAGGAAAGACAACAGCTGCAAGCGGT AAAAACTTTGTACAGTTAGTCATAGCAGTAAGAGGACTAGACATGCTCAACGCGTGTAAG AAAGAACTAATGGCATTAAAGGGCTTGAATGTTCAAGTTCACATTTATAATTCTAAGCAA GAGCTAGCTTCGGCTGAAAAAATTTCCTCAAATGAAGTCAAAAACGGTGAAACGACAGCA GAGAAGGCCCCATCTAGTCTAAGCAATTCAGAAAAAGCTCCTTCTGAAAGTGAAAATACA GAACTACCTCTTTCCCTGAATGACACGTCTATCTCCGATTTAGAATTTGCCACTTTCCAT GTTGGAAGGCCAAATGTTGAAGAAATACTAAATGAATCTGTTAACCATTCTGGTTCACTT GCCGTCGTATGTTGCGGACCACCTATTTTCGTCGACACCGCTAGAAATCAAACTGCCAAA GCTGTTATCAGAAACCCATCAAGAATGATTGAATACTTGGAGGAATACCAAGCCTGGTGA
Protein Properties
Pfam Domain Function
Protein Residues719
Protein Molecular Weight82014.60156
Protein Theoretical pI9.48
Signalling Regions
  • 1-18
Transmembrane Regions
  • 157-177
  • 229-249
  • 268-288
  • 305-325
  • 347-367
  • 374-394
  • 396-416
Protein Sequence>Ferric reductase transmembrane component 4 MLLVHIISFLLFFQLSAAKAPPSKTSLINTHERRSIYSCYVGLRKETWGFNGSAICRYEP AIQSMLYCLYEDTHEKGYSNKTLEKGFEEMRQFCYTPKFLNMTDAEFYTSLDNGTYYIQD QPKAGINITYPIRLNTTLRKAYYDAYYGYYYNHDIPYYFGGIICAYFVGVMLLAGLIRFL NYTPIKKIMFQQKLVNYVRGYTTLPTLYEKHAEPFSYLKVITGYLPTRFETLVILGYLIL HTIFMAYKYQYDPYHIIFAAHRAEVAHFVAYRSGILSFAHLPLIVLFAGRNNFLQLISGL KHTSFIVFHKWLGRMMFLDAIIHAAGFTNYYLYYKKWNTVRLRVYWKFGIATTCLAGMLI FFSIAAFRRHYYETFMALHIVFAALFLYTCWEHVTNFSGIEWIYAAIAIWGVDRIVRITR IALLGFPKADLQLVGSDLVRVTVKKPKKFWKAKPGQYVFVSFLRPLCFWQSHPFTVMDSC VNDRELVIVLKAKKGVTKLVRNFVERKGGKASMRLAIEGPYGSKSTAHRFDNVLLLAGGS GLPGPISHALELGKTTAASGKNFVQLVIAVRGLDMLNACKKELMALKGLNVQVHIYNSKQ ELASAEKISSNEVKNGETTAEKAPSSLSNSEKAPSESENTELPLSLNDTSISDLEFATFH VGRPNVEEILNESVNHSGSLAVVCCGPPIFVDTARNQTAKAVIRNPSRMIEYLEEYQAW
References
External Links
ResourceLink
Saccharomyces Genome Database FRE4
Uniprot IDP53746
Uniprot NameFRE4_YEAST
GenBank Gene IDZ71675
Genebank Protein ID1302584
General Reference
  • Philippsen, P., Kleine, K., Pohlmann, R., Dusterhoft, A., Hamberg, K., Hegemann, J. H., Obermaier, B., Urrestarazu, L. A., Aert, R., Albermann, K., Altmann, R., Andre, B., Baladron, V., Ballesta, J. P., Becam, A. M., Beinhauer, J., 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., Fleig, U., Floeth, M., Fritz, C., Gaillardin, C., Garcia-Cantalejo, J. M., Glansdorff, N. N., Goffeau, A., Gueldener, U., Herbert, C., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hinni, K., Iraqui Houssaini, I., Jacquet, M., Jimenez, A., Jonniaux, J. L., Karpfinger, L., Lanfranchi, G., Lepingle, A., Levesque, H., Lyck, R., Maftahi, M., Mallet, L., Maurer, K. C., Messenguy, F., Mewes, H. W., Mosti, 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., Revuelta, J. L., Rinke, M., Saiz, J. E., Sartorello, F., Scherens, B., Sen-Gupta, M., Soler-Mira, A., Urbanus, J. H., 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. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Nature 387:93-98.9169873
  • 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
  • Smolka, M. B., Albuquerque, C. P., Chen, S. H., Zhou, H. (2007). "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Proc Natl Acad Sci U S A 104:10364-10369.17563356