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Protein

Iron transport multicopper oxidase FET3

Gene

FET3

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

Iron transport multicopper ferroxidase required for Fe2+ ion high affinity uptake. Required to oxidize Fe2+ and release it from the transporter. Essential component of copper-dependent iron transport.

Cofactori

Cu cationNote: Binds 4 Cu cations per monomer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi81 – 811Copper 1; type 2
Metal bindingi83 – 831Copper 2; type 3
Metal bindingi126 – 1261Copper 2; type 3
Metal bindingi128 – 1281Copper 3; type 3
Metal bindingi413 – 4131Copper 4; type 1
Metal bindingi416 – 4161Copper 1; type 2
Metal bindingi418 – 4181Copper 3; type 3
Metal bindingi483 – 4831Copper 3; type 3
Metal bindingi484 – 4841Copper 4; type 1
Metal bindingi485 – 4851Copper 2; type 3
Metal bindingi489 – 4891Copper 4; type 1

GO - Molecular functioni

  • copper ion binding Source: InterPro
  • ferroxidase activity Source: SGD

GO - Biological processi

  • arsenate ion transmembrane transport Source: SGD
  • high-affinity iron ion transmembrane transport Source: SGD
  • iron assimilation by reduction and transport Source: SGD
  • response to copper ion Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Copper, Iron, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YMR058W-MONOMER.
SABIO-RKP38993.

Protein family/group databases

TCDBi2.A.108.1.1. the iron/lead transporter (ilt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Iron transport multicopper oxidase FET3 (EC:1.-.-.-)
Gene namesi
Name:FET3
Ordered Locus Names:YMR058W
ORF Names:YM9796.11
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR058W.
SGDiS000004662. FET3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 559538ExtracellularSequence analysisAdd
BLAST
Transmembranei560 – 58425HelicalSequence analysisAdd
BLAST
Topological domaini585 – 63652CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • high-affinity iron permease complex Source: SGD
  • 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
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 636615Iron transport multicopper oxidase FET3PRO_0000002959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi27 – 271N-linked (GlcNAc...)1 Publication
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence analysis
Glycosylationi77 – 771N-linked (GlcNAc...)1 Publication
Glycosylationi88 – 881N-linked (GlcNAc...)1 Publication
Glycosylationi113 – 1131N-linked (GlcNAc...)1 Publication
Glycosylationi194 – 1941N-linked (GlcNAc...)1 Publication
Glycosylationi198 – 1981N-linked (GlcNAc...)1 Publication
Glycosylationi244 – 2441N-linked (GlcNAc...)1 Publication
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence analysis
Glycosylationi292 – 2921N-linked (GlcNAc...)
Glycosylationi300 – 3001N-linked (GlcNAc...)1 Publication
Glycosylationi359 – 3591N-linked (GlcNAc...)1 Publication
Glycosylationi381 – 3811N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP38993.
PeptideAtlasiP38993.

PTM databases

iPTMnetiP38993.

Expressioni

Inductioni

By iron deprivation. Repressed by iron excess.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
FTR1P400886EBI-6876,EBI-7138

Protein-protein interaction databases

BioGridi35233. 93 interactions.
DIPiDIP-5314N.
IntActiP38993. 3 interactions.
MINTiMINT-550704.

Structurei

Secondary structure

1
636
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 3513Combined sources
Beta strandi37 – 404Combined sources
Beta strandi43 – 486Combined sources
Beta strandi51 – 533Combined sources
Beta strandi57 – 604Combined sources
Beta strandi64 – 707Combined sources
Beta strandi81 – 833Combined sources
Helixi91 – 933Combined sources
Turni97 – 993Combined sources
Beta strandi109 – 1157Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi129 – 1313Combined sources
Helixi132 – 1354Combined sources
Beta strandi138 – 1447Combined sources
Beta strandi153 – 16311Combined sources
Helixi168 – 1758Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi208 – 2158Combined sources
Beta strandi222 – 2265Combined sources
Beta strandi231 – 2366Combined sources
Beta strandi239 – 2479Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi256 – 2627Combined sources
Beta strandi271 – 2777Combined sources
Helixi279 – 2813Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi292 – 2998Combined sources
Helixi320 – 3223Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi336 – 34712Combined sources
Beta strandi353 – 3575Combined sources
Helixi369 – 3735Combined sources
Helixi377 – 3793Combined sources
Helixi383 – 3864Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi392 – 3954Combined sources
Beta strandi400 – 4078Combined sources
Beta strandi409 – 4113Combined sources
Beta strandi413 – 4175Combined sources
Beta strandi422 – 4276Combined sources
Helixi433 – 4353Combined sources
Beta strandi455 – 4628Combined sources
Beta strandi467 – 4737Combined sources
Beta strandi478 – 4847Combined sources
Helixi487 – 4915Combined sources
Beta strandi495 – 5006Combined sources
Helixi502 – 5076Combined sources
Helixi509 – 5113Combined sources
Helixi515 – 5239Combined sources
Beta strandi529 – 5335Combined sources
Beta strandi535 – 5373Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZPUX-ray2.80A/B/C/D/E/F22-555[»]
ProteinModelPortaliP38993.
SMRiP38993. Positions 22-550.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38993.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 14472Plastocyanin-like 1Add
BLAST
Domaini190 – 300111Plastocyanin-like 2Add
BLAST
Domaini382 – 500119Plastocyanin-like 3Add
BLAST

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000064508.
HOGENOMiHOG000159793.
InParanoidiP38993.
KOiK19791.
OrthoDBiEOG7VB2Q3.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38993-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNALLSIAV LLFSMLSLAQ AETHTFNWTT GWDYRNVDGL KSRPVITCNG
60 70 80 90 100
QFPWPDITVN KGDRVQIYLT NGMNNTNTSM HFHGLFQNGT ASMDGVPFLT
110 120 130 140 150
QCPIAPGSTM LYNFTVDYNV GTYWYHSHTD GQYEDGMKGL FIIKDDSFPY
160 170 180 190 200
DYDEELSLSL SEWYHDLVTD LTKSFMSVYN PTGAEPIPQN LIVNNTMNLT
210 220 230 240 250
WEVQPDTTYL LRIVNVGGFV SQYFWIEDHE MTVVEIDGIT TEKNVTDMLY
260 270 280 290 300
ITVAQRYTVL VHTKNDTDKN FAIMQKFDDT MLDVIPSDLQ LNATSYMVYN
310 320 330 340 350
KTAALPTQNY VDSIDNFLDD FYLQPYEKEA IYGEPDHVIT VDVVMDNLKN
360 370 380 390 400
GVNYAFFNNI TYTAPKVPTL MTVLSSGDQA NNSEIYGSNT HTFILEKDEI
410 420 430 440 450
VEIVLNNQDT GTHPFHLHGH AFQTIQRDRT YDDALGEVPH SFDPDNHPAF
460 470 480 490 500
PEYPMRRDTL YVRPQSNFVI RFKADNPGVW FFHCHIEWHL LQGLGLVLVE
510 520 530 540 550
DPFGIQDAHS QQLSENHLEV CQSCSVATEG NAAANTLDLT DLTGENVQHA
560 570 580 590 600
FIPTGFTKKG IIAMTFSCFA GILGIITIAI YGMMDMEDAT EKVIRDLHVD
610 620 630
PEVLLNEVDE NEERQVNEDR HSTEKHQFLT KAKRFF
Length:636
Mass (Da):72,360
Last modified:November 1, 1997 - v2
Checksum:i71CB4352B87746E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25090 Genomic DNA. Translation: AAA64929.1.
Z49703 Genomic DNA. Translation: CAA89768.1.
BK006946 Genomic DNA. Translation: DAA09956.1.
PIRiA55428.
RefSeqiNP_013774.1. NM_001182556.1.

Genome annotation databases

EnsemblFungiiYMR058W; YMR058W; YMR058W.
GeneIDi855080.
KEGGisce:YMR058W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25090 Genomic DNA. Translation: AAA64929.1.
Z49703 Genomic DNA. Translation: CAA89768.1.
BK006946 Genomic DNA. Translation: DAA09956.1.
PIRiA55428.
RefSeqiNP_013774.1. NM_001182556.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZPUX-ray2.80A/B/C/D/E/F22-555[»]
ProteinModelPortaliP38993.
SMRiP38993. Positions 22-550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35233. 93 interactions.
DIPiDIP-5314N.
IntActiP38993. 3 interactions.
MINTiMINT-550704.

Protein family/group databases

TCDBi2.A.108.1.1. the iron/lead transporter (ilt) family.

PTM databases

iPTMnetiP38993.

Proteomic databases

MaxQBiP38993.
PeptideAtlasiP38993.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR058W; YMR058W; YMR058W.
GeneIDi855080.
KEGGisce:YMR058W.

Organism-specific databases

EuPathDBiFungiDB:YMR058W.
SGDiS000004662. FET3.

Phylogenomic databases

GeneTreeiENSGT00530000064508.
HOGENOMiHOG000159793.
InParanoidiP38993.
KOiK19791.
OrthoDBiEOG7VB2Q3.

Enzyme and pathway databases

BioCyciYEAST:YMR058W-MONOMER.
SABIO-RKP38993.

Miscellaneous databases

EvolutionaryTraceiP38993.
PROiP38993.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake."
    Askwith C., Eide D., van Ho A., Bernard P.S., Li L., Davis-Kaplan S., Sipe D.M., Kaplan J.
    Cell 76:403-410(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 200060 / W303.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The FET3 gene product required for high affinity iron transport in yeast is a cell surface ferroxidase."
    de Silva D.M., Askwith C.C., Eide D., Kaplan J.
    J. Biol. Chem. 270:1098-1101(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Spectroscopic characterization of the Cu(II) sites in the Fet3 protein, the multinuclear copper oxidase from yeast required for high affinity iron uptake."
    Kosman D.J., Hassett R., Yuan D.S., McCracken J.
    J. Am. Chem. Soc. 120:4037-4038(1998)
    Cited for: EPR SPECTROSCOPY.
  6. "Spectral and kinetic properties of the Fet3 protein from Saccharomyces cerevisiae, a multinuclear copper ferroxidase enzyme."
    Hassett R., Yuan D.S., Kosman D.J.
    J. Biol. Chem. 273:23274-23282(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME KINETICS, ABSORPTION SPECTROSCOPY, EPR SPECTROSCOPY.
  7. "Spectroscopy and reactivity of the type 1 copper site in Fet3p from Saccharomyces cerevisiae: correlation of structure with reactivity in the multicopper oxidases."
    Machonkin T.E., Quintanar L., Palmer A.E., Hassett R., Severance S., Kosman D.J., Solomon E.I.
    J. Am. Chem. Soc. 123:5507-5517(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ABSORPTION SPECTROSCOPY, CIRCULAR DICHROISM ANALYSIS, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY, RESONANCE RAMAN SPECTROSCOPY.
  8. "Spectroscopic characterization and O(2) reactivity of the trinuclear Cu cluster of mutants of the multicopper oxidase Fet3p."
    Palmer A.E., Quintanar L., Severance S., Wang T.P., Kosman D.J., Solomon E.I.
    Biochemistry 41:6438-6448(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CIRCULAR DICHROISM ANALYSIS, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY OF MUTANTS.
  9. "Spectroscopic analysis of the trinuclear cluster in the Fet3 protein from yeast, a multinuclear copper oxidase."
    Blackburn N.J., Ralle M., Hassett R., Kosman D.J.
    Biochemistry 39:2316-2324(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF COPPER LIGANDS, ABSORPTION SPECTROSCOPY, EPR SPECTROSCOPY.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The copper-iron connection in biology: structure of the metallo-oxidase Fet3p."
    Taylor A.B., Stoj C.S., Ziegler L., Kosman D.J., Hart P.J.
    Proc. Natl. Acad. Sci. U.S.A. 102:15459-15464(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-555, COPPER-BINDING SITES, GLYCOSYLATION AT ASN-27; ASN-77; ASN-88; ASN-113; ASN-194; ASN-198; ASN-244; ASN-300; ASN-359 AND ASN-381.

Entry informationi

Entry nameiFET3_YEAST
AccessioniPrimary (citable) accession number: P38993
Secondary accession number(s): D6VZN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1050 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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