[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169871 [NCBI, ExPASy, EBI, Israel, Japan] Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; Nature 387:87-90(1997).
[2]	FUNCTION, AND INDUCTION. DOI=10.1074/jbc.M212308200; PubMed=14534306 [NCBI, ExPASy, EBI, Israel, Japan] De Freitas J.M., Kim J.H., Poynton H., Su T., Wintz H., Fox T., Holman P., Loguinov A., Keles S., van der Laan M., Vulpe C.; "Exploratory and confirmatory gene expression profiling of mac1Delta."; J. Biol. Chem. 279:4450-4458(2004).
[3]	TOPOLOGY [LARGE SCALE ANALYSIS]. DOI=10.1073/pnas.0604075103; PubMed=16847258 [NCBI, ExPASy, EBI, Israel, Japan] Kim H., Melen K., Oesterberg M., von Heijne G.; "A global topology map of the Saccharomyces cerevisiae membrane proteome."; Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).

Comments

FUNCTION: Required for the uptake of Fe(3+) ions. May participate in the transport of electrons from cytoplasm to an extracellular substrate (Fe(3+) ion) via FAD and heme intermediates (By similarity). Involved in iron homeostasis.
CATALYTIC ACTIVITY: 2 Fe²⁺ + NAD⁺ = 2 Fe³⁺ + NADH.
COFACTOR: FAD (Probable).
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
INDUCTION: Expression decreased by the copper-sensing transcription factor MAC1.
SIMILARITY: Contains 1 ferric oxidoreductase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X94607; CAA64294.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73219; CAA97577.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S61621; S61621.

RefSeq

NP_013148.1; -.

3D structure databases

ModBase

Q12209.

Protein-protein interaction databases

IntAct

Q12209; 1.

Organism-specific databases

YLR047c; -.

S000004037; FRE8.

Gene expression databases

ArrayExpress

Q12209; -.

GermOnline

YLR047C; Saccharomyces cerevisiae.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0000293;	Molecular function: ferric-chelate reductase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0006875;	Biological process: cellular metal ion homeostasis (inferred from mutant phenotype from SGD).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006826;	Biological process: iron ion transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013130; Fe3_reduct_TM_N.
Graphical view of domain structure.

Pfam

PF01794; Ferric_reduct; 1.
Pfam graphical view of domain structure.

Genome annotation databases

Ensembl

YLR047C; Saccharomyces cerevisiae. [Contig view]

850736; -.

Y13138_GR; YLR047C.

sce:YLR047C; -.

fig|4932.3.peg.4139; -.

Phylogenomic databases

HOGENOM

Q12209; -.

Other

Q12209; -.

966840; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Electron transport; FAD; Glycoprotein; Ion transport; Iron; Iron transport; Membrane; NAD; Oxidoreductase; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 686`	`686`	`Probable ferric reductase transmembrane component 8.`	`PRO_0000239647`
`TOPO_DOM`	`1 35`	`35`	`Cytoplasmic (Potential).`
`TRANSMEM`	`36 56`	`21`	`Potential.`
`TOPO_DOM`	`57 89`	`33`	`Extracellular (Potential).`
`TRANSMEM`	`90 110`	`21`	`Potential.`
`TOPO_DOM`	`111 128`	`18`	`Cytoplasmic (Potential).`
`TRANSMEM`	`129 149`	`21`	`Potential.`
`TOPO_DOM`	`150 157`	`8`	`Extracellular (Potential).`
`TRANSMEM`	`158 178`	`21`	`Potential.`
`TOPO_DOM`	`179 186`	`8`	`Cytoplasmic (Potential).`
`TRANSMEM`	`187 207`	`21`	`Potential.`
`TOPO_DOM`	`208 216`	`9`	`Extracellular (Potential).`
`TRANSMEM`	`217 237`	`21`	`Potential.`
`TOPO_DOM`	`238 267`	`30`	`Cytoplasmic (Potential).`
`TRANSMEM`	`268 288`	`21`	`Potential.`
`TOPO_DOM`	`289 402`	`114`	`Extracellular (Potential).`
`TRANSMEM`	`403 423`	`21`	`Potential.`
`TOPO_DOM`	`424 686`	`263`	`Cytoplasmic (Potential).`
`DOMAIN`	`119 666`	`548`	`Ferric oxidoreductase.`
`NP_BIND`	`320 326`	`7`	`FAD (Potential).`
`NP_BIND`	`442 450`	`9`	`NAD (Potential).`
`CARBOHYD`	`371 371`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`383 383`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`384 384`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 686 AA [This is the length of the unprocessed precursor]

Molecular weight: 78949 Da [This is the MW of the unprocessed precursor]

CRC64: 907EDDE10D7B9BA2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNLKSIVSWF KEHLPSFDVD VDKHFRTLRV RKYSQICLLI SFIIICVIIP LMNYLLLTDK 

        70         80         90        100        110        120 
FFKICHHLKH HVFNRRSWVH KTHMYHKQSL QLCLICFVFT SFFVIQGANG DLLEITKRMG 

       130        140        150        160        170        180 
RISVALMPPL LFLTLRPSPL PHTLYLALLP LHKWISRIVV LESILHTWFY LYYMYINDTL 

       190        200        210        220        230        240 
YVKMRKLPNI YGVIALGLFL LIAITSVRYA RRWSYRVFYY VHYVSTWLIL VFLHYHARPG 

       250        260        270        280        290        300 
ISYYTTLNVL ILTGQIVYRL HITNVTRVTI VPISSSLSLL EFPLTDLPKK PILPGGHLRI 

       310        320        330        340        350        360 
NIYHRNFLRR FFSHLIPFQH PFTIASIPSD NLVRLIIRNG HFPLRTNEKY YITGAFEPEL 

       370        380        390        400        410        420 
SFISKPTVPF NITTKSSKNP FRNNSSALIN SPLNFLIKAQ RVFMCVGGSG ISFGLPLLRI 

       430        440        450        460        470        480 
LNFNGVNVRL LWVSRDYKDL EVLNHFKNNF EGMEIYISGT EGNEQDIEID YIDYHDCAAD 

       490        500        510        520        530        540 
INDEVRSISS SGRVSELGDN SMLSDGNPQP TEPNENTALL SKKSTLRNHH PPKTSDIPDI 

       550        560        570        580        590        600 
NADDEIDFTY AFSRSKSRKN TAQGTLTTHS SFNGSSVFRQ PKIIEPPAQD PCLEAAPKKI 

       610        620        630        640        650        660 
RIPAGVKVFF GRPTLGDKDY EWCLQTECDA ETDSIQCCRW ANQGRDHAEY LSQVWVLAAG 

       670        680 
PRGLIESTKR WATDGGLHFH GESFAL

Q12209 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools