FET5_YEAST
ID FET5_YEAST Reviewed; 622 AA.
AC P43561; D6VTI9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Iron transport multicopper oxidase FET5;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=FET5; OrderedLocusNames=YFL041W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9413439; DOI=10.1007/pl00008615;
RA Spizzo T., Byersdorfer C., Duesterhoeft S., Eide D.;
RT "The yeast FET5 gene encodes a FET3-related multicopper oxidase implicated
RT in iron transport.";
RL Mol. Gen. Genet. 256:547-556(1997).
RN [4]
RP INTERACTION WITH FTH1.
RX PubMed=10608875; DOI=10.1074/jbc.274.53.38061;
RA Urbanowski J.L., Piper R.C.;
RT "The iron transporter Fth1p forms a complex with the Fet5 iron oxidase and
RT resides on the vacuolar membrane.";
RL J. Biol. Chem. 274:38061-38070(1999).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Iron transport multicopper oxidase, which is required for
CC Fe(2+) high affinity uptake. May be required to oxidize Fe(2+) and
CC release it from the transporter. Essential component of copper-
CC dependent iron transport.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC -!- SUBUNIT: Interacts with FTH1. {ECO:0000269|PubMed:10608875}.
CC -!- INTERACTION:
CC P43561; P38310: FTH1; NbExp=7; IntAct=EBI-6891, EBI-20959;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; D50617; BAA09199.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12399.1; -; Genomic_DNA.
DR PIR; S56214; S56214.
DR RefSeq; NP_116612.1; NM_001179925.1.
DR AlphaFoldDB; P43561; -.
DR SMR; P43561; -.
DR BioGRID; 31105; 77.
DR ComplexPortal; CPX-869; FET5-FTH1 high affinity iron exporter complex.
DR DIP; DIP-6774N; -.
DR IntAct; P43561; 7.
DR MINT; P43561; -.
DR STRING; 4932.YFL041W; -.
DR CAZy; AA1; Auxiliary Activities 1.
DR TCDB; 2.A.108.1.4; the iron/lead transporter (ilt) family.
DR iPTMnet; P43561; -.
DR MaxQB; P43561; -.
DR PaxDb; P43561; -.
DR PRIDE; P43561; -.
DR TopDownProteomics; P43561; -.
DR EnsemblFungi; YFL041W_mRNA; YFL041W; YFL041W.
DR GeneID; 850502; -.
DR KEGG; sce:YFL041W; -.
DR SGD; S000001853; FET5.
DR VEuPathDB; FungiDB:YFL041W; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_7_3_1; -.
DR InParanoid; P43561; -.
DR OMA; QKCHSKT; -.
DR BioCyc; YEAST:YFL041W-MON; -.
DR PRO; PR:P43561; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43561; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0061841; C:high-affinity iron exporter complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IGI:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0034755; P:iron ion transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0006826; P:iron ion transport; IMP:SGD.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR CDD; cd13877; CuRO_2_Fet3p_like; 1.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR044130; CuRO_2_Fet3-like.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Copper; Glycoprotein; Ion transport; Iron; Iron transport;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..622
FT /note="Iron transport multicopper oxidase FET5"
FT /id="PRO_0000002960"
FT TOPO_DOM 19..573
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..146
FT /note="Plastocyanin-like 1"
FT DOMAIN 192..301
FT /note="Plastocyanin-like 2"
FT DOMAIN 392..514
FT /note="Plastocyanin-like 3"
FT BINDING 79
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 497
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 502
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 70880 MW; 961757A6C86B7FAF CRC64;
MLFYSFVWSV LAASVALAKT HKLNYTASWV TANPDGLHEK RMIGFNGEWP LPDIHVEKGD
RVELYLTNGF QDNTATSLHF HGLFQNTSLG NQLQMDGPSM VTQCPIVPGQ TYLYNFTVPE
QVGTFWYHAH MGAQYGDGMR GAFIIHDPEE PFEYDHERVI TLSDHYHENY KTVTKEFLSR
YNPTGAEPIP QNILFNNTMN VTLDFTPGET YLFRFLNVGL FVSQYIILED HEMSIVEVDG
VYVKPNFTDS IYLSAGQRMS VLIKAKDKMP TRNYAMMQIM DETMLDVVPP ELQLNQTIQM
RYGHSLPEAR ALNIEDCDLD RATNDFYLEP LIERDLLAHY DHQIVMDVRM VNLGDGVKYA
FFNNITYVTP KVPTLTTLLT SGKLASDPRI YGDNINAQLL KHNDIIEVVL NNYDSGRHPF
HLHGHNFQIV QKSPGFHVDE AYDESEQDEM TVPYNESAPL QPFPERPMVR DTVVLEPSGH
VVLRFRADNP GVWYFHCHVD WHLQQGLASV FIEAPVLLQE REKLNENYLD ICKAADIPVV
GNAAGHSNDW FDLKGLPRQP EPLPKGFTTE GYLALIISTI IGVWGLYSIA QYGIGEVIPN
DEKVYHTLRE ILAENEIEVS RG
