FRE3_YEAST
ID FRE3_YEAST Reviewed; 711 AA.
AC Q08905; D6W373;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ferric reductase transmembrane component 3;
DE EC=1.16.1.9;
DE AltName: Full=Ferric-chelate reductase 3;
DE Flags: Precursor;
GN Name=FRE3; OrderedLocusNames=YOR381W; ORFNames=O6754;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 INDUCTION.
RX PubMed=9726978; DOI=10.1074/jbc.273.37.23716;
RA Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
RT "Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:23716-23721(1998).
RN [4]
RP ERRATUM OF PUBMED:9726978.
RA Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
RL J. Biol. Chem. 273:30056-30056(1998).
RN [5]
RP INDUCTION.
RX PubMed=10341420;
RX DOI=10.1002/(sici)1097-0061(199905)15:7<573::aid-yea404>3.0.co;2-7;
RA Georgatsou E., Alexandraki D.;
RT "Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu
RT reductase related genes.";
RL Yeast 15:573-584(1999).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11120744; DOI=10.1074/jbc.m010065200;
RA Yun C.-W., Bauler M., Moore R.E., Klebba P.E., Philpott C.C.;
RT "The role of the FRE family of plasma membrane reductases in the uptake of
RT siderophore-iron in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:10218-10223(2001).
RN [7]
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: Siderophore-iron reductase responsible for reducing
CC extracellular iron prior to import. Catalyzes the reductive uptake of
CC Fe(3+) bound to di- and trihydroxamate siderophores. Fe(3+) is reduced
CC to Fe(2+), which then dissociates from the siderophore and can be
CC imported by the high-affinity Fe(2+) transport complex in the plasma
CC membrane. {ECO:0000269|PubMed:11120744}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-
CC siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11120744};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11120744}.
CC -!- INDUCTION: By iron deprivation. {ECO:0000269|PubMed:10341420,
CC ECO:0000269|PubMed:9726978}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z75289; CAA99713.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11139.1; -; Genomic_DNA.
DR PIR; S67293; S67293.
DR RefSeq; NP_015026.1; NM_001183801.1.
DR AlphaFoldDB; Q08905; -.
DR SMR; Q08905; -.
DR BioGRID; 34762; 97.
DR DIP; DIP-4049N; -.
DR IntAct; Q08905; 1.
DR MINT; Q08905; -.
DR STRING; 4932.YOR381W; -.
DR PaxDb; Q08905; -.
DR PRIDE; Q08905; -.
DR EnsemblFungi; YOR381W_mRNA; YOR381W; YOR381W.
DR GeneID; 854563; -.
DR KEGG; sce:YOR381W; -.
DR SGD; S000005908; FRE3.
DR VEuPathDB; FungiDB:YOR381W; -.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000176303; -.
DR HOGENOM; CLU_010365_4_0_1; -.
DR InParanoid; Q08905; -.
DR OMA; AIEGSYG; -.
DR BioCyc; YEAST:YOR381W-MON; -.
DR PRO; PR:Q08905; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08905; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IGI:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0015677; P:copper ion import; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0015891; P:siderophore transport; IMP:SGD.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; FAD; Flavoprotein; Glycoprotein; Heme;
KW Ion transport; Iron; Iron transport; Membrane; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..711
FT /note="Ferric reductase transmembrane component 3"
FT /id="PRO_0000010139"
FT TOPO_DOM 21..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..341
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 280..414
FT /note="Ferric oxidoreductase"
FT DOMAIN 415..534
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 316
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 479..485
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 526..529
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 677..678
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 711 AA; 80589 MW; 362E18F7FA34C165 CRC64;
MYWVLLCGSI LLCCLSGASA SPAKTKMYGK LPLVLTDACM GVLGEVTWEY SSDDLYSSPA
CTYEPALQSM LYCIYESLNE KGYSNRTFEK TFAAIKEDCA YYTDNLQNMT NADFYNMLNN
GTTYIIQYSE GSANLTYPIE MDAQVRENYY YSYHGFYANY DIGHTYGGII CAYFVGVMIL
ASILHYLSYT PFKTALFKQR LVRYVRRYLT IPTIWGKHAS SFSYLKIFTG FLPTRSEGVI
ILGYLVLHTV FLAYGYQYDP YNLIFDSRRE QIARYVADRS GVLAFAHFPL IALFAGRNNF
LEFISGVKYT SFIMFHKWLG RMMFLDAVIH GAAYTSYSVF YKDWAASKEE TYWQFGVAAL
CIVGVMVFFS LAMFRKFFYE AFLFLHIVLG ALFFYTCWEH VVELSGIEWI YAAIAIWTID
RLIRIVRVSY FGFPKASLQL VGDDIIRVTV KRPVRLWKAK PGQYVFVSFL HHLYFWQSHP
FTVLDSIIKD GELTIILKEK KGVTKLVKKY VCCNGGKASM RLAIEGPYGS SSPVNNYDNV
LLLTGGTGLP GPIAHAIKLG KTSAATGKQF IKLVIAVRGF NVLEAYKPEL MCLEDLNVQL
HIYNTMEVPA LTPNDSLEIS QQDEKADGKG VVMATTLEQS PNPVEFDGTV FHHGRPNVEK
LLHEVGDLNG SLAVVCCGPP VFVDEVRDQT ANLVLEKPAK AIEYFEEYQS W
