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Ferric/cupric reductase transmembrane component 1 (EC 1.16.1.9) (Ferric-chelate reductase 1)

 FRE1_CANAL              Reviewed;         760 AA.
Q5A446; A0A1D8PME9;
07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 2.
07-NOV-2018, entry version 94.
RecName: Full=Ferric/cupric reductase transmembrane component 1 {ECO:0000250|UniProtKB:P32791};
EC=1.16.1.9 {ECO:0000250|UniProtKB:P32791};
AltName: Full=Ferric-chelate reductase 1 {ECO:0000250|UniProtKB:P32791};
Flags: Precursor;
Name=CFL1 {ECO:0000303|PubMed:10784045}; Synonyms=FRE1;
OrderedLocusNames=CAALFM_C405770CA; ORFNames=CaO19.1263, CaO19.8848;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
FUNCTION, AND INDUCTION.
PubMed=10784045;
Hammacott J.E., Williams P.H., Cashmore A.M.;
"Candida albicans CFL1 encodes a functional ferric reductase activity
that can rescue a Saccharomyces cerevisiae fre1 mutant.";
Microbiology 146:869-876(2000).
[5]
INDUCTION.
PubMed=12760852; DOI=10.1128/AAC.47.6.1805-1817.2003;
Niewerth M., Kunze D., Seibold M., Schaller M., Korting H.C., Hube B.;
"Ciclopirox olamine treatment affects the expression pattern of
Candida albicans genes encoding virulence factors, iron metabolism
proteins, and drug resistance factors.";
Antimicrob. Agents Chemother. 47:1805-1817(2003).
[6]
INDUCTION.
PubMed=15917516; DOI=10.1128/AAC.49.6.2226-2236.2005;
Liu T.T., Lee R.E., Barker K.S., Lee R.E., Wei L., Homayouni R.,
Rogers P.D.;
"Genome-wide expression profiling of the response to azole, polyene,
echinocandin, and pyrimidine antifungal agents in Candida albicans.";
Antimicrob. Agents Chemother. 49:2226-2236(2005).
[7]
INDUCTION.
PubMed=15790671; DOI=10.1093/jac/dki089;
Sigle H.C., Thewes S., Niewerth M., Korting H.C., Schafer-Korting M.,
Hube B.;
"Oxygen accessibility and iron levels are critical factors for the
antifungal action of ciclopirox against Candida albicans.";
J. Antimicrob. Chemother. 55:663-673(2005).
[8]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=25130162; DOI=10.1111/1567-1364.12194;
Yu Q., Dong Y., Xu N., Qian K., Chen Y., Zhang B., Xing L., Li M.;
"A novel role of the ferric reductase Cfl1 in cell wall integrity,
mitochondrial function, and invasion to host cells in Candida
albicans.";
FEMS Yeast Res. 14:1037-1047(2014).
-!- FUNCTION: Ferric reductase 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. Also participates
in Cu(2+) reduction and Cu(+) uptake (By similarity). Involved in
maintenance of cell wall integrity (CWI), mitochondrial function,
and interaction between the pathogen and the host.
{ECO:0000250|UniProtKB:P32791, ECO:0000269|PubMed:10784045,
ECO:0000269|PubMed:25130162}.
-!- CATALYTIC ACTIVITY: 2 Fe(II)-siderophore + NADP(+) + H(+) = 2
Fe(III)-siderophore + NADPH. {ECO:0000250|UniProtKB:P32791}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:P32791};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:P32791};
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P32791}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P32791}.
-!- INDUCTION: Transcription is negatively regulated by SFU1, copper,
amphotericin B, and caspofungin; and induced by ciclopirox
olamine. {ECO:0000269|PubMed:10784045,
ECO:0000269|PubMed:12760852, ECO:0000269|PubMed:15790671,
ECO:0000269|PubMed:15917516}.
-!- DISRUPTION PHENOTYPE: Leads to abnormal cell wall composition,
decreased ability of adhesion, and hypersensitivity to cell wall
stresses. Increases mitochondrial activity and shows abnormal
mitochondrial morphology. Results also in up-regulation of the
expression of the cell wall integrity (CWI) genes PGA13 and CRH11,
enhanded secretion, and decreased ability to invade HeLa cells.
{ECO:0000269|PubMed:25130162}.
-!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP017626; AOW29307.1; -; Genomic_DNA.
RefSeq; XP_716571.2; XM_711478.2.
ProteinModelPortal; Q5A446; -.
SMR; Q5A446; -.
EnsemblFungi; AOW29307; AOW29307; CAALFM_C405770CA.
GeneID; 3641810; -.
KEGG; cal:CAALFM_C405770CA; -.
CGD; CAL0000193490; CFL1.
InParanoid; Q5A446; -.
OrthoDB; EOG092C0RW5; -.
PRO; PR:Q5A446; -.
Proteomes; UP000000559; Chromosome 4.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IGI:CGD.
GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
GO; GO:0000293; F:ferric-chelate reductase activity; IGI:CGD.
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; IGI:CGD.
GO; GO:0006826; P:iron ion transport; IGI:CGD.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
Gene3D; 3.40.50.80; -; 1.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; FAD-bd_FR_type.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR039261; FNR_nucleotide-bd.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
SUPFAM; SSF52343; SSF52343; 1.
PROSITE; PS51384; FAD_FR; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Copper; Copper transport;
Electron transport; FAD; Flavoprotein; Glycoprotein; Heme;
Ion transport; Iron; Iron transport; Membrane; Metal-binding; NADP;
Oxidoreductase; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Transport; Virulence.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 760 Ferric/cupric reductase transmembrane
component 1. {ECO:0000255}.
/FTId=PRO_0000431507.
TOPO_DOM 19 212 Extracellular. {ECO:0000305}.
TRANSMEM 213 233 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 234 288 Cytoplasmic. {ECO:0000305}.
TRANSMEM 289 309 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 310 324 Extracellular. {ECO:0000305}.
TRANSMEM 325 345 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 346 371 Cytoplasmic. {ECO:0000305}.
TRANSMEM 372 392 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 393 403 Extracellular. {ECO:0000305}.
TRANSMEM 404 424 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 425 430 Cytoplasmic. {ECO:0000305}.
TRANSMEM 431 451 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 452 760 Extracellular. {ECO:0000305}.
DOMAIN 330 445 Ferric oxidoreductase. {ECO:0000255}.
DOMAIN 465 583 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 575 578 NADP. {ECO:0000255}.
NP_BIND 726 727 NADP. {ECO:0000255}.
COMPBIAS 154 168 Poly-Ser. {ECO:0000255}.
METAL 366 366 Iron (heme 1 axial ligand).
{ECO:0000250|UniProtKB:P32791}.
METAL 380 380 Iron (heme 2 axial ligand).
{ECO:0000250|UniProtKB:P32791}.
METAL 436 436 Iron (heme 1 axial ligand).
{ECO:0000250|UniProtKB:P32791}.
METAL 450 450 Iron (heme 2 axial ligand).
{ECO:0000250|UniProtKB:P32791}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 615 615 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 744 744 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
SEQUENCE 760 AA; 84888 MW; 330AF6BC42AD23F1 CRC64;
MKIQQLIVFL FAVVLIDART PKRYSELDIV MSTCTTFIGK YGTVCTSTGK RSTNWNCYCK
TDAGFGTISD CLVRGFNNNT NIISKFTESC NMTESKFHAK YDKIQAEFKT NGTEYAKMTT
KSSSGSKTSA SASKSSKSTG SSNASKSSTN AHGSNSSTSS TSSSSSKSGK GNSGTSTTET
ITTPLLIDYK KFTPYKDAYQ MSNNNFNLSI NYGSGLLGYW AGILAIAIFA NMIKKMFPSL
TNYLSGSISN LFRKHLFLPA TFRKKKAQEF SIGVYGFFDG LIPTRLETII VVIFVVLTGL
FSALHIHHVK DNPQYATKNA ELGHLIADRT GILGTFLIPL LILFGGRNNF LQWLTGWDFA
TFIMYHRWIS RVDVLLIIVH AITFSVSDKA TGKYNTRMKR DFMIWGTVST ICGGFILFQA
MLFFRRKCYE VFFLIHIVLV VFFVVGGYYH LESQGYGDFM WAAIAVWAFD RVVRLGRIFF
FGARKATVSI KGDDTLKIEV PKPKYWKSVA GGHAFIHFLK PTLFLQSHPF TFTTTESNDK
IVLYAKIKNG ITSNIAKYLS PLPGNTATIR VLVEGPYGEP SSAGRNCKNV VFVAGGNGIP
GIYSECVDLA KKSKNQSIKL IWIIRHWKSL SWFTEELEYL KKTNVQSTIY VTQPQDCSGL
ECFEHDVSFE KKSDEKDSVE SSQYSLISNI KQGLSHVEFI EGRPDISTQV EQEVKQADGA
IGFVTCGHPA MVDELRFAVT QNLNVSKHRV EYHEQLQTWA


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