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|---|---|
| Accession Number: | P32791 |
| Protein Name: | Fre1p aka FRE1 aka YLR214W aka L8167.2 |
| Length: | 686 |
| Molecular Weight: | 78854.00 |
| Species: | Saccharomyces cerevisiae (Baker's yeast) [4932] |
| Number of TMSs: | 9 |
| Location1 / Topology2 / Orientation3: | Cell membrane1 / Multi-pass membrane protein2 |
| Substrate | electron |
Cross database links:
| DIP: | DIP-5349N |
|---|---|
| RefSeq: | NP_013315.1 |
| Entrez Gene ID: | 850911 |
| Pfam: | PF08022 PF01794 PF08030 |
| KEGG: | sce:YLR214W |
Gene Ontology
GO:0016021
C:integral to membrane
GO:0005624
C:membrane fraction
GO:0005886
C:plasma membrane
GO:0009055
F:electron carrier activity
GO:0050660
F:FAD binding
GO:0000293
F:ferric-chelate reductase activity
GO:0005506
F:iron ion binding
GO:0005515
F:protein binding
GO:0015677
P:copper ion import
GO:0022900
P:electron transport chain
GO:0006826
P:iron ion transport
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References (19)[1] “Ferric reductase of Saccharomyces cerevisiae: molecular characterization, role in iron uptake, and transcriptional control by iron.” Dancis A.et.al. 1570306 [2] “The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.” Johnston M.et.al. 9169871 [3] “Ferric iron reduction and iron assimilation in Saccharomyces cerevisiae.” Anderson G.J.et.al. 1431884 [4] “AFT1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae.” Yamaguchi-Iwai Y.et.al. 7720713 [5] “Evidence for Cu(II) reduction as a component of copper uptake by Saccharomyces cerevisiae.” Hassett R.et.al. 7814363 [6] “Evidence for the Saccharomyces cerevisiae ferrireductase system being a multicomponent electron transport chain.” Lesuisse E.et.al. 8662826 [7] “The FRE1 ferric reductase of Saccharomyces cerevisiae is a cytochrome b similar to that of NADPH oxidase.” Shatwell K.P.et.al. 8662973 [8] “Intramembrane bis-heme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase.” Finegold A.A.et.al. 8940093 [9] “The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Mac1p activator.” Georgatsou E.et.al. 9153234 [10] “The AFT1 transcriptional factor is differentially required for expression of high-affinity iron uptake genes in Saccharomyces cerevisiae.” Casas C.et.al. 9200812 [11] “Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae.” Martins L.J.et.al. 9726978 [12] “Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu reductase related genes.” Georgatsou E.et.al. 10341420 [13] “The role of the FRE family of plasma membrane reductases in the uptake of siderophore-iron in Saccharomyces cerevisiae.” Yun C.-W.et.al. 11120744 [14] “Fre1p Cu2+ reduction and Fet3p Cu1+ oxidation modulate copper toxicity in Saccharomyces cerevisiae.” Shi X.et.al. 12954629 [15] “Global analysis of protein expression in yeast.” Ghaemmaghami S.et.al. 14562106 [16] “Inhibition of the yeast metal reductase heme protein fre1 by nitric oxide (NO): a model for inhibition of NADPH oxidase by NO.” Shinyashiki M.et.al. 15288128 [17] “Azo reductase activity of intact Saccharomyces cerevisiae cells is dependent on the Fre1p component of plasma membrane ferric reductase.” Ramalho P.A.et.al. 16000801 [18] “Direct activation of genes involved in intracellular iron use by the yeast iron-responsive transcription factor Aft2 without its paralog Aft1.” Courel M.et.al. 16024809 [19] “Probing the membrane environment of the TOR kinases reveals functional interactions between TORC1, actin, and membrane trafficking in Saccharomyces cerevisiae.” Aronova S.et.al. 17507646
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External Searches:
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Analyze:
| Predict TMSs (Predict number of transmembrane segments) | ||||
| FASTA formatted sequence |
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1: MVRTRVLFCL FISFFATVQS SATLISTSCI SQAALYQFGC SSKSKSCYCK NINWLGSVTA 61: CAYENSKSNK TLDSALMKLA SQCSSIKVYT LEDMKNIYLN ASNYLRAPEK SDKKTVVSQP 121: LMANETAYHY YYEENYGIHL NLMRSQWCAW GLVFFWVAVL TAATILNILK RVFGKNIMAN 181: SVKKSLIYPS VYKDYNERTF YLWKRLPFNF TTRGKGLVVL IFVILTILSL SFGHNIKLPH 241: PYDRPRWRRS MAFVSRRADL MAIALFPVVY LFGIRNNPFI PITGLSFSTF NFYHKWSAYV 301: CFMLAVVHSI VMTASGVKRG VFQSLVRKFY FRWGIVATIL MSIIIFQSEK VFRNRGYEIF 361: LLIHKAMNIM FIIAMYYHCH TLGWMGWIWS MAGILCFDRF CRIVRIIMNG GLKTATLSTT 421: DDSNVIKISV KKPKFFKYQV GAFAYMYFLS PKSAWFYSFQ SHPFTVLSER HRDPNNPDQL 481: TMYVKANKGI TRVLLSKVLS APNHTVDCKI FLEGPYGVTV PHIAKLKRNL VGVAAGLGVA 541: AIYPHFVECL RLPSTDQLQH KFYWIVNDLS HLKWFENELQ WLKEKSCEVS VIYTGSSVED 601: TNSDESTKGF DDKEESEITV ECLNKRPDLK ELVRSEIKLS ELENNNITFY SCGPATFNDD 661: FRNAVVQGID SSLKIDVELE EESFTW