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2.A.108.1.1
High-affinity oxidase-dependent plasma membrane Fe2+-Fe3+ uptake transporter, Ftr1 of 404 aas and 7 TMSs in a 3 + 3 + 1 TMS arrangement with the N-terminus out and the C-termius in (Severance et al. 2004). There are two REXLE (Arg-Glu-Xaa-Leu-Glu) motifs in transmembrane domains 1 and 4, both essential for transport activity, implying the presence of a 3 TMS repeat ((Severance et al. 2004)). Ftr1 may be a "transceptor", combining transport and receptor functions (Diallinas 2017). Bacterial redox-dependent iron transporters with an emphasis on FtrABCD have been reviewed (Banerjee et al. 2022).

Accession Number:P38993
Protein Name:FET3 aka Fet3p aka YMR058W aka YM9796.11
Length:636
Molecular Weight:72360.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell membrane1 / Single-pass type I membrane protein2 / Extracellular side3
Substrate iron(2+), iron(3+)

Cross database links:

DIP: DIP-5314N
RefSeq: NP_013774.1   
Entrez Gene ID: 855080   
Pfam: PF00394    PF07731    PF07732   
KEGG: sce:YMR058W   

Gene Ontology

GO:0033573 C:high affinity iron permease complex
GO:0016021 C:integral to membrane
GO:0005507 F:copper ion binding
GO:0004322 F:ferroxidase activity
GO:0005515 F:protein binding
GO:0006827 P:high-affinity iron ion transport
GO:0033215 P:iron assimilation by reduction and transport
GO:0055114 P:oxidation reduction
GO:0046688 P:response to copper ion

References (10)

[1] “The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.”  Askwith C.et.al.   8293473
[2] “The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.”  Bowman S.et.al.   9169872
[3] “The FET3 gene product required for high affinity iron transport in yeast is a cell surface ferroxidase.”  de Silva D.M.et.al.   7836366
[4] “Spectral and kinetic properties of the Fet3 protein from Saccharomyces cerevisiae, a multinuclear copper ferroxidase enzyme.”  Hassett R.et.al.   9722559
[5] “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.et.al.   11389633
[6] “Spectroscopic characterization and O(2) reactivity of the trinuclear Cu cluster of mutants of the multicopper oxidase Fet3p.”  Palmer A.E.et.al.   12009907
[7] “Spectroscopic analysis of the trinuclear cluster in the Fet3 protein from yeast, a multinuclear copper oxidase.”  Blackburn N.J.et.al.   10694398
[8] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[9] “Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.”  Chi A.et.al.   17287358
[10] “The copper-iron connection in biology: structure of the metallo-oxidase Fet3p.”  Taylor A.B.et.al.   16230618
Structure:
1ZPU     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MTNALLSIAV LLFSMLSLAQ AETHTFNWTT GWDYRNVDGL KSRPVITCNG QFPWPDITVN 
61:	KGDRVQIYLT NGMNNTNTSM HFHGLFQNGT ASMDGVPFLT QCPIAPGSTM LYNFTVDYNV 
121:	GTYWYHSHTD GQYEDGMKGL FIIKDDSFPY DYDEELSLSL SEWYHDLVTD LTKSFMSVYN 
181:	PTGAEPIPQN LIVNNTMNLT WEVQPDTTYL LRIVNVGGFV SQYFWIEDHE MTVVEIDGIT 
241:	TEKNVTDMLY ITVAQRYTVL VHTKNDTDKN FAIMQKFDDT MLDVIPSDLQ LNATSYMVYN 
301:	KTAALPTQNY VDSIDNFLDD FYLQPYEKEA IYGEPDHVIT VDVVMDNLKN GVNYAFFNNI 
361:	TYTAPKVPTL MTVLSSGDQA NNSEIYGSNT HTFILEKDEI VEIVLNNQDT GTHPFHLHGH 
421:	AFQTIQRDRT YDDALGEVPH SFDPDNHPAF PEYPMRRDTL YVRPQSNFVI RFKADNPGVW 
481:	FFHCHIEWHL LQGLGLVLVE DPFGIQDAHS QQLSENHLEV CQSCSVATEG NAAANTLDLT 
541:	DLTGENVQHA FIPTGFTKKG IIAMTFSCFA GILGIITIAI YGMMDMEDAT EKVIRDLHVD 
601:	PEVLLNEVDE NEERQVNEDR HSTEKHQFLT KAKRFF