FRE7_YEAS7
ID FRE7_YEAS7 Reviewed; 620 AA.
AC A6ZN61;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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; ORFNames=SCY_4929;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Cell surface metalloreductase. May be involved in copper
CC homeostasis (By similarity). {ECO:0000250}.
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:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: By transcription factor MAC1 upon copper deprivation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
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DR EMBL; AAFW02000030; EDN63726.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZN61; -.
DR SMR; A6ZN61; -.
DR EnsemblFungi; EDN63726; EDN63726; SCY_4929.
DR HOGENOM; CLU_010365_7_2_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IEA:UniProt.
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 3: Inferred from homology;
KW Cell membrane; Copper; Copper transport; Electron transport; FAD;
KW Flavoprotein; Heme; Ion transport; Iron; Iron transport; Membrane;
KW Metal-binding; NADP; Oxidoreductase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..620
FT /note="Ferric/cupric reductase transmembrane component 7"
FT /id="PRO_0000337758"
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..544
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"
SQ SEQUENCE 620 AA; 70880 MW; 9A8ABB097970E536 CRC64;
MIEERDLVLS NGIHCIADIH SELYARLKKE SQAVTPWVYQ KQYGKFVTYF VAVIIFLSLI
KKLAFMYYDS SEEFLPEKKN SPTTPSVFLA RIMTKLVAFN RYICYRKFPT LIFSYLGIPT
SVGTFLVVMA TTLYTLLYCF VPHPFYRPCA GFGSPPLSVR AGIMAISLVS FVFSLSGKIN
VIGWLVGLSY EKINIYHQWA SILCLFFSWV HVIPFLRQAR HEGGYERMHQ RWKASDMWRS
GVPPILFLNL LWLSSLPIAR RHFYEIFLQL HWILAVGFYI SLFYHVYPEL NSHMYLVATI
VVWFAQLFYR LAVKGYLRPG RSFMASTIAN VSIVGEGCVE LIVKDVDMAY SPGQHIFVRT
IDKDIISNHP FSIFPSAKYP GGIKMLIRAQ KGFSKRLYES NDDMKKILID GPYGGIERDI
RSFTNVYLIC SGSGISTCLP FLQKYGPILH KTNLEVITLD WVVRHREDIS WIRDEICTLS
NNLRQLFLDG TIVVRIYVCS DSTVPGIIKT FPQTADTASD QSDLAKREKD TEFGQDDTES
NSTFDKSNNE YKGLITIIPS KPDLNQVIND YQIGFRNCFI CSGSDSLRYT VGNSVAGLQA
KVFSNKNVEE CYLHSESFGY
