| Identification |
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| Name | Ferric/cupric reductase transmembrane component 2 |
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| Synonyms | - Ferric-chelate reductase 2
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| Gene Name | FRE2 |
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| Enzyme Class | |
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| Biological Properties |
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| General Function | Involved in oxidoreductase activity |
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| Specific Function | Metalloreductase 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 |
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| Cellular Location | Cell membrane; Multi-pass membrane protein |
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| SMPDB Pathways | Not Available |
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| KEGG Pathways | Not Available |
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| SMPDB Reactions | Not Available |
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| KEGG Reactions | Not Available |
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| Metabolites | | YMDB ID | Name | View |
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| YMDB00194 | Iron(3+) | Show | | YMDB00379 | Iron(2+) | Show | | YMDB00426 | NADPH | Show | | YMDB00427 | NADP | Show |
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| GO Classification | | Component |
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| cell part | | membrane part | | intrinsic to membrane | | integral to membrane | | Function |
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| ion binding | | cation binding | | 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 | | Process |
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| oxidation reduction | | metabolic process |
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| Gene Properties |
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| Chromosome Location | chromosome 11 |
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| Locus | YKL220C |
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| 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 |
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| Protein Properties |
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| Pfam Domain Function | |
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| Protein Residues | 711 |
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| Protein Molecular Weight | 80071.5 |
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| Protein Theoretical pI | 9.39 |
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| Signalling Regions | |
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| Transmembrane Regions | - 165-185
- 236-256
- 281-301
- 318-340
- 354-374
- 378-398
- 401-423
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| Protein Sequence | >Ferric/cupric reductase transmembrane component 2
MHWTSILSAILLFCLSGARASPAKTVIRNKVPLLVTNACTRIFQKVTWEYTSKSKRSSPV
CSYEPAFQSMLYCIYETLDEKGYSNKTLEKTFSTIKKNCASYSDALQNMTNSEFYDVLNN
GTRHMTPYVKGSANLTYPVEMDTQLRKAYYHALHGFYANLDVGNIYGGIICAYFVAIMAF
AGVLHCMNYTPFKTVLLKQKLVGYVRGYLTLPTIGSKHASDFSYFRIFTGYLPTRLEGII
ILGYLVLHTVFLAYGYEYDPENIIFKSRRVQVARYVADRSGVLAFAHFPLIVLFAGRNNF
LEYISGVKYTSFIMFHKWLGRMMFLDAMIHGSAYTSYTVANKTWATSKNRLYWQFGVAAL
CLAGTMVFFSFAVFRKYFYEAFLFLHIVLGAMFFYACWEHVVSLSGIEWIYTAIAIWIVD
RIIRIIKASYFGFPKASLQLIGDDLIRLTVKKPARPWRAKPGQYVFVSFLHPLYFWQSHP
FTVLDSVSKNGELVIILKEKKGVTRLVKKYVCRNGGKTSMRLAIEGPYGSSSPVNNYNNV
LLLTGGTGLPGPIAHAIKLGKTSAAAGKQSVKLVIAVRGFDVLEAYKPELMCLENLNVQL
HIYNTMEVPSLTPSDSLDISQQDEKADEKGTVVATTLEKSANPLGFDGVVFHCGRPNVKE
LLHEAAELSGSLSVVCCGPPIFVDKVRNETAKIVLDKSAKAIEYFEEYQCW |
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| References |
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| External Links | |
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| 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
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