FRE8_YEAST
ID FRE8_YEAST Reviewed; 686 AA.
AC Q12209; D6VY49;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable ferric reductase transmembrane component 8;
DE EC=1.16.1.7;
DE AltName: Full=Ferric-chelate reductase 8;
GN Name=FRE8; OrderedLocusNames=YLR047C; ORFNames=L2114;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=14534306; DOI=10.1074/jbc.m212308200;
RA De Freitas J.M., Kim J.H., Poynton H., Su T., Wintz H., Fox T., Holman P.,
RA Loguinov A., Keles S., van der Laan M., Vulpe C.;
RT "Exploratory and confirmatory gene expression profiling of mac1Delta.";
RL J. Biol. Chem. 279:4450-4458(2004).
RN [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Required for the uptake of Fe(3+) ions. May participate in
CC the transport of electrons from cytoplasm to an extracellular substrate
CC (Fe(3+) ion) via FAD and heme intermediates (By similarity). Involved
CC in iron homeostasis. {ECO:0000250, ECO:0000269|PubMed:14534306}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-
CC siderophore + NADH; Xref=Rhea:RHEA:15061, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.16.1.7;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Expression decreased by the copper-sensing transcription
CC factor MAC1. {ECO:0000269|PubMed:14534306}.
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DR EMBL; X94607; CAA64294.1; -; Genomic_DNA.
DR EMBL; Z73219; CAA97577.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09365.1; -; Genomic_DNA.
DR PIR; S61621; S61621.
DR RefSeq; NP_013148.1; NM_001181934.1.
DR AlphaFoldDB; Q12209; -.
DR BioGRID; 31322; 65.
DR IntAct; Q12209; 1.
DR STRING; 4932.YLR047C; -.
DR iPTMnet; Q12209; -.
DR MaxQB; Q12209; -.
DR PaxDb; Q12209; -.
DR PRIDE; Q12209; -.
DR EnsemblFungi; YLR047C_mRNA; YLR047C; YLR047C.
DR GeneID; 850736; -.
DR KEGG; sce:YLR047C; -.
DR SGD; S000004037; FRE8.
DR VEuPathDB; FungiDB:YLR047C; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_025685_0_0_1; -.
DR InParanoid; Q12209; -.
DR OMA; LLPIHKW; -.
DR BioCyc; YEAST:G3O-32203-MON; -.
DR PRO; PR:Q12209; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12209; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0140618; F:ferric-chelate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR GO; GO:0016722; F:oxidoreductase activity, acting on metal ions; IMP:SGD.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR GO; GO:0006875; P:cellular metal ion homeostasis; IMP:SGD.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR Pfam; PF01794; Ferric_reduct; 1.
PE 1: Evidence at protein level;
KW Electron transport; FAD; Flavoprotein; Glycoprotein; Ion transport; Iron;
KW Iron transport; Membrane; NAD; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..686
FT /note="Probable ferric reductase transmembrane component 8"
FT /id="PRO_0000239647"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..89
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 119..666
FT /note="Ferric oxidoreductase"
FT REGION 490..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 320..326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 442..450
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 686 AA; 78949 MW; 907EDDE10D7B9BA2 CRC64;
MNLKSIVSWF KEHLPSFDVD VDKHFRTLRV RKYSQICLLI SFIIICVIIP LMNYLLLTDK
FFKICHHLKH HVFNRRSWVH KTHMYHKQSL QLCLICFVFT SFFVIQGANG DLLEITKRMG
RISVALMPPL LFLTLRPSPL PHTLYLALLP LHKWISRIVV LESILHTWFY LYYMYINDTL
YVKMRKLPNI YGVIALGLFL LIAITSVRYA RRWSYRVFYY VHYVSTWLIL VFLHYHARPG
ISYYTTLNVL ILTGQIVYRL HITNVTRVTI VPISSSLSLL EFPLTDLPKK PILPGGHLRI
NIYHRNFLRR FFSHLIPFQH PFTIASIPSD NLVRLIIRNG HFPLRTNEKY YITGAFEPEL
SFISKPTVPF NITTKSSKNP FRNNSSALIN SPLNFLIKAQ RVFMCVGGSG ISFGLPLLRI
LNFNGVNVRL LWVSRDYKDL EVLNHFKNNF EGMEIYISGT EGNEQDIEID YIDYHDCAAD
INDEVRSISS SGRVSELGDN SMLSDGNPQP TEPNENTALL SKKSTLRNHH PPKTSDIPDI
NADDEIDFTY AFSRSKSRKN TAQGTLTTHS SFNGSSVFRQ PKIIEPPAQD PCLEAAPKKI
RIPAGVKVFF GRPTLGDKDY EWCLQTECDA ETDSIQCCRW ANQGRDHAEY LSQVWVLAAG
PRGLIESTKR WATDGGLHFH GESFAL
