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Identification
NameFerric/cupric reductase transmembrane component 7
Synonyms
  • Ferric-chelate reductase 7
Gene NameFRE7
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionCell surface metalloreductase. May be involved in copper homeostasis
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
catalytic activity
oxidoreductase activity
Process
metabolic process
oxidation reduction
Gene Properties
Chromosome Locationchromosome 15
LocusYOL152W
Gene Sequence>YOL152W FRE7 SGDID:S000005512, Chr XV from 40748-42610, Verified ORF, "Putative ferric reductase with similarity to Fre2p; expression induced by low copper levels" ATGATTGAAGAAAGAGATTTGGTTTTAAGCAATGGTATCCATTGTATTGCTGACATCCAC TCCGAACTATACGCCAGGTTAAAAAAAGAATCGCAGGCAGCGACACCATGGGTGTACCAA AAACAATACGGAAAATTCGTCACTTACTTTGTCGCTGTGATAATTTTTTTGTCTTTGATA AAAAAGCTGGCATTTATGTATTATGATTCCAGTGAGGAATTTCTTCCAGAAAAGAAGAAC TCGCCGACTACCCCTTCTGTATTCCTTGCTCGAATAATGACGAAACTTGTCGCATTCAAC AGATACATTTGCTACAGGAAATTTCCCACGTTGATATTTTCTTATTTAGGTATTCCGACA TCTGTGGGTACTTTTTTAGTAGTAATGGCTACCACTTTATACACACTTCTATACTGCTTT GTTCCTCATCCATTCTACAGACCTTGTGCAGGATTTGGTTCGCCGCCTTTGTCTGTTCGT GCAGGCATAATGGCAATATCTTTGGTTCCGTTTGTATTCTCACTTTCCGGGAAGATCAAC GTTATAGGTTGGTTGGTTGGGCTTTCGTATGAAAAAATCAACATATACCACCAATGGGCA TCCATTCTTTGTTTATTCTTTAGCTGGGTTCATGTCATTCCCTTCCTACGTCAAGCACGA CATGAGGGAGGATATGAAAGAATGCATCAACGGTGGAAGGCATCCGACATGTGGAGGAGT GGTGTCCCACCCATCTTATTTTTGAATCTGCTATGGTTATCTTCGCTGCCTATTGCTAGA AGACATTTTTATGAGATTTTTTTGCAACTTCATTGGATTTTAGCTGTTGGATTTTACATT AGTTTGTTCTATCATGTATATCCCGAATTGAATTCCCATATGTATCTGGTTGCTACAATT GTGGTTTGGTTTGCACAACTGTTTTACAGACTAGCTGTGAAGGGTTATTTAAGACCTGGT AGAAGTTTCATGGCCTCGACCATTGCAAATGTCAGCATAGTCGGCGAAGGATGCGTAGAA TTGATCGTCAAAGATGTGGAAATGGCCTATTCCCCAGGTCAACACATATTCGTGAGAACT ATTGATAAGGGCATCATTTCCAACCATCCATTTTCTATCTTTCCGAGTGCAAAGTATCCC GGAGGAATAAAAATGCTGATTAGAGCCCAGAAAGGGTTTTCTAAAAGGCTATACGAAAGT AATGACGACATGAAGAAAATTCTTATTGATGGGCCTTATGGTGGAATCGAGAGAGATATT AGAAGTTTTACCAATGTCTACTTGATTTGCTCTGGTTCAGGTATATCTACATGCTTACCT TTCCTGCAAAAATATGGCCCCATACTCCATAAGACAAACTTAGAAGTTATTACATTGGAC TGGGTGGTAAGACATAGGGAGGATATATCATGGATTAGAGATGAAATGTGTACCCTCTCA AATAATTTGCGCCAGTTATTTTTAGATGGGAAAATTGTGGTTAGAATTTACGTCTGCTCG GACAGTACCGTCCCTGGTATTATTAAAACTTTCCCTCAAACAATAGACACCGCCAGTGAC CAATCTGATTTAGCTAAAAGAGAAAAAGATACCGAATTCGGCCAGGATGATACTGAGTCA AATTCAACTTTCGACAAATCCAATAACGAATATAAAGGTCTCATCACCATTATTCCTTCC AAACCTGATTTGAATCAGGTCATTAATGATTACCAAATTGGGTTCAGGAACTGCTTCATT TGTTCAGGTTCTGACAGCCTAAGGTATACCGTCGGAAATTCCGTGGCAGGTTTACAGGCC AAGGTTTTTTCTAACAAAAATGTCGAAGAGTGCTATTTACACAGCGAGAGTTTTGGCTAC TAG
Protein Properties
Pfam Domain Function
Protein Residues620
Protein Molecular Weight70904.70313
Protein Theoretical pI8.79
Signalling Regions
  • None
Transmembrane Regions
  • 46-66
  • 108-128
  • 168-188
  • 195-215
  • 238-258
  • 266-286
  • 293-313
Protein Sequence>Ferric/cupric reductase transmembrane component 7 MIEERDLVLSNGIHCIADIHSELYARLKKESQAATPWVYQKQYGKFVTYFVAVIIFLSLI KKLAFMYYDSSEEFLPEKKNSPTTPSVFLARIMTKLVAFNRYICYRKFPTLIFSYLGIPT SVGTFLVVMATTLYTLLYCFVPHPFYRPCAGFGSPPLSVRAGIMAISLVPFVFSLSGKIN VIGWLVGLSYEKINIYHQWASILCLFFSWVHVIPFLRQARHEGGYERMHQRWKASDMWRS GVPPILFLNLLWLSSLPIARRHFYEIFLQLHWILAVGFYISLFYHVYPELNSHMYLVATI VVWFAQLFYRLAVKGYLRPGRSFMASTIANVSIVGEGCVELIVKDVEMAYSPGQHIFVRT IDKGIISNHPFSIFPSAKYPGGIKMLIRAQKGFSKRLYESNDDMKKILIDGPYGGIERDI RSFTNVYLICSGSGISTCLPFLQKYGPILHKTNLEVITLDWVVRHREDISWIRDEMCTLS NNLRQLFLDGKIVVRIYVCSDSTVPGIIKTFPQTIDTASDQSDLAKREKDTEFGQDDTES NSTFDKSNNEYKGLITIIPSKPDLNQVINDYQIGFRNCFICSGSDSLRYTVGNSVAGLQA KVFSNKNVEECYLHSESFGY
References
External Links
ResourceLink
Saccharomyces Genome Database FRE7
Uniprot IDQ12333
Uniprot NameFRE7_YEAST
General Reference
  • Casamayor, A., Aldea, M., Casas, C., Herrero, E., Gamo, F. J., Lafuente, M. J., Gancedo, C., Arino, J. (1995). "DNA sequence analysis of a 13 kbp fragment of the left arm of yeast chromosome XV containing seven new open reading frames." Yeast 11:1281-1288.8553699
  • Dujon, B., Albermann, K., Aldea, M., Alexandraki, D., Ansorge, W., Arino, J., Benes, V., Bohn, C., Bolotin-Fukuhara, M., Bordonne, R., Boyer, J., Camasses, A., Casamayor, A., Casas, C., Cheret, G., Cziepluch, C., Daignan-Fornier, B., Dang, D. V., de Haan, M., Delius, H., Durand, P., Fairhead, C., Feldmann, H., Gaillon, L., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Nature 387:98-102.9169874
  • 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
  • Rees, E. M., Thiele, D. J. (2007). "Identification of a vacuole-associated metalloreductase and its role in Ctr2-mediated intracellular copper mobilization." J Biol Chem 282:21629-21638.17553781
  • Singh, A., Kaur, N., Kosman, D. J. (2007). "The metalloreductase Fre6p in Fe-efflux from the yeast vacuole." J Biol Chem 282:28619-28626.17681937
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956