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Ferric reductase transmembrane component 5 (EC 1.16.1.9) (Ferric-chelate reductase 5)

 FRE5_YEAST              Reviewed;         694 AA.
Q08908; D6W377;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 149.
RecName: Full=Ferric reductase transmembrane component 5;
EC=1.16.1.9;
AltName: Full=Ferric-chelate reductase 5;
Flags: Precursor;
Name=FRE5; OrderedLocusNames=YOR384W; ORFNames=O6765;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
INDUCTION.
PubMed=9726978; DOI=10.1074/jbc.273.37.23716;
Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
"Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces
cerevisiae.";
J. Biol. Chem. 273:23716-23721(1998).
[5]
ERRATUM.
Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
J. Biol. Chem. 273:30056-30056(1998).
[6]
INDUCTION.
PubMed=10341420;
DOI=10.1002/(SICI)1097-0061(199905)15:7<573::AID-YEA404>3.3.CO;2-Z;
Georgatsou E., Alexandraki D.;
"Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p
Fe/Cu reductase related genes.";
Yeast 15:573-584(1999).
-!- FUNCTION: Metalloreductase responsible for reducing extracellular
iron and copper prior to import. Catalyzes the reductive uptake of
Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate
siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates
from the siderophore and can be imported by the high-affinity
Fe(2+) transport complex in the plasma membrane (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: 2 Fe(II)-siderophore + NADP(+) + H(+) = 2
Fe(III)-siderophore + NADPH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}.
-!- INDUCTION: By iron deprivation. {ECO:0000269|PubMed:10341420,
ECO:0000269|PubMed:9726978}.
-!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z75292; CAA99716.1; -; Genomic_DNA.
EMBL; AY692958; AAT92977.1; -; Genomic_DNA.
EMBL; BK006948; DAA11143.1; -; Genomic_DNA.
PIR; S67296; S67296.
RefSeq; NP_015029.1; NM_001183804.1.
ProteinModelPortal; Q08908; -.
SMR; Q08908; -.
BioGrid; 34765; 16.
DIP; DIP-2747N; -.
IntAct; Q08908; 1.
MINT; Q08908; -.
STRING; 4932.YOR384W; -.
PaxDb; Q08908; -.
PRIDE; Q08908; -.
EnsemblFungi; YOR384W; YOR384W; YOR384W.
GeneID; 854566; -.
KEGG; sce:YOR384W; -.
EuPathDB; FungiDB:YOR384W; -.
SGD; S000005911; FRE5.
GeneTree; ENSGT00390000007891; -.
HOGENOM; HOG000000805; -.
InParanoid; Q08908; -.
OMA; WIRRRFY; -.
OrthoDB; EOG092C04QA; -.
BioCyc; YEAST:G3O-33846-MONOMER; -.
PRO; PR:Q08908; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
GO; GO:0000293; F:ferric-chelate reductase activity; ISA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
GO; GO:0015677; P:copper ion import; IBA:GO_Central.
GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
Gene3D; 3.40.50.80; -; 1.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR039261; FNR_nucleotide-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
SUPFAM; SSF52343; SSF52343; 2.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Electron transport; FAD;
Flavoprotein; Glycoprotein; Heme; Ion transport; Iron; Membrane;
Metal-binding; NADP; Oxidoreductase; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 694 Ferric reductase transmembrane component
5.
/FTId=PRO_0000010141.
TOPO_DOM 20 163 Extracellular. {ECO:0000250}.
TRANSMEM 164 184 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 185 222 Cytoplasmic. {ECO:0000250}.
TRANSMEM 223 243 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 244 267 Extracellular. {ECO:0000250}.
TRANSMEM 268 288 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 289 311 Cytoplasmic. {ECO:0000250}.
TRANSMEM 312 334 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 335 347 Extracellular. {ECO:0000250}.
TRANSMEM 348 368 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 369 371 Cytoplasmic. {ECO:0000250}.
TRANSMEM 372 392 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 393 403 Extracellular. {ECO:0000250}.
TRANSMEM 404 424 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 425 694 Cytoplasmic. {ECO:0000250}.
DOMAIN 274 408 Ferric oxidoreductase.
DOMAIN 409 528 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 473 479 FAD. {ECO:0000255}.
NP_BIND 520 523 NADP. {ECO:0000255}.
NP_BIND 660 661 NADP. {ECO:0000255}.
COMPBIAS 362 368 Poly-Phe.
METAL 310 310 Iron (heme 1 axial ligand).
{ECO:0000250}.
METAL 324 324 Iron (heme 2 axial ligand).
{ECO:0000250}.
METAL 380 380 Iron (heme 1 axial ligand).
{ECO:0000250}.
METAL 394 394 Iron (heme 2 axial ligand).
{ECO:0000250}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 694 AA; 80292 MW; 44D7E941F19F7AA0 CRC64;
MLFARLVLLL VYLAPGSLAK PASTKKRTQW DQIAIDACAK ELESHKFDTD VKGRHATLCT
YEPALGSWLH CAKDVLDSRK KSKKIFEKTF SKINQYCHDY HKDEVVSNEE YYRIFANASL
FIRPLDEVKE NIRYPVTPNK ASLDRWVWAY FGPLDNIDKG NVYGVTICLY WIGVLFIAAV
YHFLNFSRLK QTVFKNKVSA FLRGHYVLPA LVHNHAMSVG RWFFIGLVPT RLETLVLFGY
VLLHGFLLSS YNFDHNELLS DRRSQVLIFL SDRAGILAFA HFPLIVLFGG KNSTMTWLTG
IRYTAFITYH KWLGRFMLVD CTIHAIGYTY HAYIENYWKY VKYSDLWTSG RHAMIIVGIL
VFFSFFFFRR HYYELFVITH IILAIGFFHA CWKHCYKLGW GEWIMACALF WIADRILRLI
KIAIFGMPWA KLKLCGESMI EVRISKSSKW WKAEPGQYIY LYFLRPKIFW QSHPFTVMDS
LVEDGELVVV ITVKNGLTKK LQEYLLESEG YTEMRVLAEG PYGQSTRTHL FESLLFIAGG
AGVPGPLSMA IKAGRQVKSN DSHQMIKFVW SVRNLDLLEV YRKEIMVLKE LNIDTKIYFT
GERKDESNTE EGAIANMSTE GRLLTTSKSA EMITDFGRPN IDEIIEEAVS GAKSLLVTCC
GSEGFVDKTR ELTAKRVLEH GDKWIEYVEE FQNW


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