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Protein

Ferric/cupric reductase transmembrane component 7

Gene

FRE7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface metalloreductase. May be involved in copper homeostasis.2 Publications

Catalytic activityi

2 Fe(II)-siderophore + NADP+ + H+ = 2 Fe(III)-siderophore + NADPH.

Cofactori

FADCurated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi197 – 1971Iron (heme 1 axial ligand)By similarity
Metal bindingi211 – 2111Iron (heme 2 axial ligand)By similarity
Metal bindingi271 – 2711Iron (heme 1 axial ligand)By similarity
Metal bindingi285 – 2851Iron (heme 2 axial ligand)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi369 – 3757FADSequence analysis
Nucleotide bindingi411 – 4144NADPSequence analysis
Nucleotide bindingi578 – 5792NADPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • copper ion import Source: SGD
  • iron ion homeostasis Source: UniProtKB-KW
  • iron ion transport Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Copper transport, Electron transport, Ion transport, Iron transport, Transport

Keywords - Ligandi

Copper, FAD, Flavoprotein, Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciYEAST:G3O-33540-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferric/cupric reductase transmembrane component 7 (EC:1.16.1.9)
Alternative name(s):
Ferric-chelate reductase 7
Gene namesi
Name:FRE7
Ordered Locus Names:YOL152W
ORF Names:AOB629
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL152W.
SGDiS000005512. FRE7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4545ExtracellularBy similarityAdd
BLAST
Transmembranei46 – 6621Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini67 – 10741CytoplasmicBy similarityAdd
BLAST
Transmembranei108 – 12821Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini129 – 16739ExtracellularBy similarityAdd
BLAST
Transmembranei168 – 18821Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini189 – 1946CytoplasmicBy similarity
Transmembranei195 – 21521Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini216 – 23722ExtracellularBy similarityAdd
BLAST
Transmembranei238 – 25821Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini259 – 2657CytoplasmicBy similarity
Transmembranei266 – 28621Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini287 – 2926ExtracellularBy similarity
Transmembranei293 – 31321Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini314 – 620307CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Ferric/cupric reductase transmembrane component 7PRO_0000210150Add
BLAST

Proteomic databases

MaxQBiQ12333.

PTM databases

iPTMnetiQ12333.

Expressioni

Inductioni

By transription factor MAC1 upon copper deprivation.3 Publications

Interactioni

Protein-protein interaction databases

BioGridi34266. 21 interactions.
DIPiDIP-3837N.
MINTiMINT-526087.

Structurei

3D structure databases

ProteinModelPortaliQ12333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini161 – 320160Ferric oxidoreductaseAdd
BLAST
Domaini321 – 41999FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ferric reductase (FRE) family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 ferric oxidoreductase domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000007891.
HOGENOMiHOG000248882.
InParanoidiQ12333.
KOiK00521.
OMAiVYPELNS.
OrthoDBiEOG722JJ9.

Family and domain databases

InterProiIPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR030155. FRE7.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR11972:SF38. PTHR11972:SF38. 3 hits.
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12333-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEERDLVLS NGIHCIADIH SELYARLKKE SQAATPWVYQ KQYGKFVTYF
60 70 80 90 100
VAVIIFLSLI KKLAFMYYDS SEEFLPEKKN SPTTPSVFLA RIMTKLVAFN
110 120 130 140 150
RYICYRKFPT LIFSYLGIPT SVGTFLVVMA TTLYTLLYCF VPHPFYRPCA
160 170 180 190 200
GFGSPPLSVR AGIMAISLVP FVFSLSGKIN VIGWLVGLSY EKINIYHQWA
210 220 230 240 250
SILCLFFSWV HVIPFLRQAR HEGGYERMHQ RWKASDMWRS GVPPILFLNL
260 270 280 290 300
LWLSSLPIAR RHFYEIFLQL HWILAVGFYI SLFYHVYPEL NSHMYLVATI
310 320 330 340 350
VVWFAQLFYR LAVKGYLRPG RSFMASTIAN VSIVGEGCVE LIVKDVEMAY
360 370 380 390 400
SPGQHIFVRT IDKGIISNHP FSIFPSAKYP GGIKMLIRAQ KGFSKRLYES
410 420 430 440 450
NDDMKKILID GPYGGIERDI RSFTNVYLIC SGSGISTCLP FLQKYGPILH
460 470 480 490 500
KTNLEVITLD WVVRHREDIS WIRDEMCTLS NNLRQLFLDG KIVVRIYVCS
510 520 530 540 550
DSTVPGIIKT FPQTIDTASD QSDLAKREKD TEFGQDDTES NSTFDKSNNE
560 570 580 590 600
YKGLITIIPS KPDLNQVIND YQIGFRNCFI CSGSDSLRYT VGNSVAGLQA
610 620
KVFSNKNVEE CYLHSESFGY
Length:620
Mass (Da):70,905
Last modified:May 20, 2008 - v2
Checksum:iDDBEADEBD71C27BF
GO

Sequence cautioni

The sequence CAA88276.1 differs from that shown. Reason: Frameshift at position 597. Curated
The sequence CAA99174.1 differs from that shown. Reason: Frameshift at position 597. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48239 Genomic DNA. Translation: CAA88276.1. Frameshift.
Z74894 Genomic DNA. Translation: CAA99174.1. Frameshift.
BK006948 Genomic DNA. Translation: DAA10634.1.
PIRiS60385.
RefSeqiNP_014489.2. NM_001183406.1.

Genome annotation databases

EnsemblFungiiYOL152W; YOL152W; YOL152W.
GeneIDi854013.
KEGGisce:YOL152W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48239 Genomic DNA. Translation: CAA88276.1. Frameshift.
Z74894 Genomic DNA. Translation: CAA99174.1. Frameshift.
BK006948 Genomic DNA. Translation: DAA10634.1.
PIRiS60385.
RefSeqiNP_014489.2. NM_001183406.1.

3D structure databases

ProteinModelPortaliQ12333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34266. 21 interactions.
DIPiDIP-3837N.
MINTiMINT-526087.

PTM databases

iPTMnetiQ12333.

Proteomic databases

MaxQBiQ12333.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL152W; YOL152W; YOL152W.
GeneIDi854013.
KEGGisce:YOL152W.

Organism-specific databases

EuPathDBiFungiDB:YOL152W.
SGDiS000005512. FRE7.

Phylogenomic databases

GeneTreeiENSGT00390000007891.
HOGENOMiHOG000248882.
InParanoidiQ12333.
KOiK00521.
OMAiVYPELNS.
OrthoDBiEOG722JJ9.

Enzyme and pathway databases

BioCyciYEAST:G3O-33540-MONOMER.

Miscellaneous databases

NextBioi975532.
PROiQ12333.

Family and domain databases

InterProiIPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR030155. FRE7.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR11972:SF38. PTHR11972:SF38. 3 hits.
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence analysis of a 13 kbp fragment of the left arm of yeast chromosome XV containing seven new open reading frames."
    Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J., Gancedo C., Arino J.
    Yeast 11:1281-1288(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    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.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The AFT1 transcriptional factor is differentially required for expression of high-affinity iron uptake genes in Saccharomyces cerevisiae."
    Casas C., Aldea M., Espinet C., Gallego C., Gil R., Herrero E.
    Yeast 13:621-637(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae."
    Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.
    J. Biol. Chem. 273:23716-23721(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. Erratum
    Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.
    J. Biol. Chem. 273:30056-30056(1998)
  7. "Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu reductase related genes."
    Georgatsou E., Alexandraki D.
    Yeast 15:573-584(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Identification of a vacuole-associated metalloreductase and its role in Ctr2-mediated intracellular copper mobilization."
    Rees E.M., Thiele D.J.
    J. Biol. Chem. 282:21629-21638(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A REDUCTASE, SUBCELLULAR LOCATION.
  9. "The metalloreductase Fre6p in Fe-efflux from the yeast vacuole."
    Singh A., Kaur N., Kosman D.J.
    J. Biol. Chem. 282:28619-28626(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A REDUCTASE.

Entry informationi

Entry nameiFRE7_YEAST
AccessioniPrimary (citable) accession number: Q12333
Secondary accession number(s): D6W1R8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 20, 2008
Last modified: May 11, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.