FRE7_YEAST
ID FRE7_YEAST Reviewed; 620 AA.
AC Q12333; D6W1R8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ferric/cupric reductase transmembrane component 7;
DE EC=1.16.1.9;
DE AltName: Full=Ferric-chelate reductase 7;
GN Name=FRE7; OrderedLocusNames=YOL152W; ORFNames=AOB629;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553699; DOI=10.1002/yea.320111308;
RA Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J.,
RA Gancedo C., Arino J.;
RT "DNA sequence analysis of a 13 kbp fragment of the left arm of yeast
RT chromosome XV containing seven new open reading frames.";
RL Yeast 11:1281-1288(1995).
RN [2]
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 [3]
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 [4]
RP INDUCTION.
RX PubMed=9200812;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<621::aid-yea121>3.0.co;2-u;
RA Casas C., Aldea M., Espinet C., Gallego C., Gil R., Herrero E.;
RT "The AFT1 transcriptional factor is differentially required for expression
RT of high-affinity iron uptake genes in Saccharomyces cerevisiae.";
RL Yeast 13:621-637(1997).
RN [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION AS A REDUCTASE, AND SUBCELLULAR LOCATION.
RX PubMed=17553781; DOI=10.1074/jbc.m703397200;
RA Rees E.M., Thiele D.J.;
RT "Identification of a vacuole-associated metalloreductase and its role in
RT Ctr2-mediated intracellular copper mobilization.";
RL J. Biol. Chem. 282:21629-21638(2007).
RN [9]
RP FUNCTION AS A REDUCTASE.
RX PubMed=17681937; DOI=10.1074/jbc.m703398200;
RA Singh A., Kaur N., Kosman D.J.;
RT "The metalloreductase Fre6p in Fe-efflux from the yeast vacuole.";
RL J. Biol. Chem. 282:28619-28626(2007).
CC -!- FUNCTION: Cell surface metalloreductase. May be involved in copper
CC homeostasis. {ECO:0000269|PubMed:17553781,
CC ECO:0000269|PubMed:17681937}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17553781};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17553781}.
CC -!- INDUCTION: By transcription factor MAC1 upon copper deprivation.
CC {ECO:0000269|PubMed:10341420, ECO:0000269|PubMed:9200812,
CC ECO:0000269|PubMed:9726978}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA88276.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA99174.1; Type=Frameshift; Evidence={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; Z48239; CAA88276.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z74894; CAA99174.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006948; DAA10634.1; -; Genomic_DNA.
DR PIR; S60385; S60385.
DR RefSeq; NP_014489.2; NM_001183406.1.
DR AlphaFoldDB; Q12333; -.
DR SMR; Q12333; -.
DR BioGRID; 34266; 67.
DR DIP; DIP-3837N; -.
DR MINT; Q12333; -.
DR STRING; 4932.YOL152W; -.
DR iPTMnet; Q12333; -.
DR MaxQB; Q12333; -.
DR PaxDb; Q12333; -.
DR PRIDE; Q12333; -.
DR EnsemblFungi; YOL152W_mRNA; YOL152W; YOL152W.
DR GeneID; 854013; -.
DR KEGG; sce:YOL152W; -.
DR SGD; S000005512; FRE7.
DR VEuPathDB; FungiDB:YOL152W; -.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000176662; -.
DR HOGENOM; CLU_010365_7_2_1; -.
DR InParanoid; Q12333; -.
DR OMA; PWLDQPV; -.
DR BioCyc; YEAST:G3O-33540-MON; -.
DR PRO; PR:Q12333; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12333; protein.
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; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015677; P:copper ion import; IGI:SGD.
DR GO; GO:0006826; P:iron ion transport; IGI:SGD.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
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; IPR030155; FRE7.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF89; PTHR11972:SF89; 1.
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; Copper; Copper transport; Electron transport; FAD;
KW Flavoprotein; Heme; Ion transport; Iron; Iron transport; Membrane;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..620
FT /note="Ferric/cupric reductase transmembrane component 7"
FT /id="PRO_0000210150"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 46..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 108..128
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..167
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 168..188
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 195..215
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..237
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 238..258
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 266..286
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..292
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 293..313
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 161..320
FT /note="Ferric oxidoreductase"
FT DOMAIN 321..419
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 519..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197
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 211
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 271
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 285
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 369..375
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 411..414
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 578..579
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 620 AA; 70905 MW; DDBEADEBD71C27BF CRC64;
MIEERDLVLS NGIHCIADIH SELYARLKKE SQAATPWVYQ KQYGKFVTYF VAVIIFLSLI
KKLAFMYYDS SEEFLPEKKN SPTTPSVFLA RIMTKLVAFN RYICYRKFPT LIFSYLGIPT
SVGTFLVVMA TTLYTLLYCF VPHPFYRPCA GFGSPPLSVR AGIMAISLVP FVFSLSGKIN
VIGWLVGLSY EKINIYHQWA SILCLFFSWV HVIPFLRQAR HEGGYERMHQ RWKASDMWRS
GVPPILFLNL LWLSSLPIAR RHFYEIFLQL HWILAVGFYI SLFYHVYPEL NSHMYLVATI
VVWFAQLFYR LAVKGYLRPG RSFMASTIAN VSIVGEGCVE LIVKDVEMAY SPGQHIFVRT
IDKGIISNHP FSIFPSAKYP GGIKMLIRAQ KGFSKRLYES NDDMKKILID GPYGGIERDI
RSFTNVYLIC SGSGISTCLP FLQKYGPILH KTNLEVITLD WVVRHREDIS WIRDEMCTLS
NNLRQLFLDG KIVVRIYVCS DSTVPGIIKT FPQTIDTASD QSDLAKREKD TEFGQDDTES
NSTFDKSNNE YKGLITIIPS KPDLNQVIND YQIGFRNCFI CSGSDSLRYT VGNSVAGLQA
KVFSNKNVEE CYLHSESFGY
