FET3_KLULA
ID FET3_KLULA Reviewed; 631 AA.
AC Q6CII3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Iron transport multicopper oxidase FET3;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=FET3; OrderedLocusNames=KLLA0F26400g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Iron transport multicopper ferroxidase required for Fe(2+)
CC high affinity uptake. Required to oxidize Fe(2+) and release it from
CC the transporter. Essential component of copper-dependent iron transport
CC (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; CR382126; CAG98964.1; -; Genomic_DNA.
DR RefSeq; XP_456256.1; XM_456256.1.
DR AlphaFoldDB; Q6CII3; -.
DR SMR; Q6CII3; -.
DR STRING; 28985.XP_456256.1; -.
DR EnsemblFungi; CAG98964; CAG98964; KLLA0_F26400g.
DR GeneID; 2894840; -.
DR KEGG; kla:KLLA0_F26400g; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_7_3_1; -.
DR InParanoid; Q6CII3; -.
DR OMA; VHYDDTM; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0033573; C:high-affinity iron permease complex; IEA:EnsemblFungi.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IEA:EnsemblFungi.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:1901684; P:arsenate ion transmembrane transport; IEA:EnsemblFungi.
DR GO; GO:0033215; P:reductive iron assimilation; IEA:EnsemblFungi.
DR GO; GO:0046688; P:response to copper ion; IEA:EnsemblFungi.
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; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..631
FT /note="Iron transport multicopper oxidase FET3"
FT /id="PRO_0000002958"
FT TOPO_DOM 26..564
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 50..148
FT /note="Plastocyanin-like 1"
FT DOMAIN 195..297
FT /note="Plastocyanin-like 2"
FT DOMAIN 387..506
FT /note="Plastocyanin-like 3"
FT REGION 610..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
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 87
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="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 132
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 488
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 489
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 490
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 494
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 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
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 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 631 AA; 71471 MW; DA491405555644C6 CRC64;
MKVSTHHFLP SLLVALWSWA TVAQAATHTF NWTTGWGNYN VDGNFERPVI TCNGEFPWPD
LKVKRGDRIQ VYLTNGFDDR NTSLHFHGLS QNGTNMMDGP EMITQCPIAP GDTMLYNFTI
DDNDGTYWYH SHTGGQYQDG MKGTLVVEPE DSLPFDYDEE VVVQLAEWYY DNVDTLDRKF
MNVYNPTGAE PIPQNLIINN TRNMTWNVEP DTTYLLRIVN TGGFVSQYFW IEDHDMTVVE
VDGVYVEKNT TSMLYITVAQ RYSVLIHTKN DTSKNYAIMQ KFDDTMLDVI PNDLMLNATS
YMMYDKDGEK PEQSYVDSID DFLDDFYLTP LDKVELYEDP DYTITVDVVM DNLKNGVNYA
FFNNLTFTAP KVPTLMTALS AGKDALNPLV YGTNTNAFVL KKDEIIEIVL NNNDTGKHPF
HLHGHIFQLV DRERGYDDAI GEGPHPFDPE DHNPFPDYPM MRDTVYVNPQ SSIVLRFKAD
NPGVWFFHCH IEWHLKQGLA LLLIEAPEEM QNTESQQLTD NHKQVCENVG LSWEGNAAGN
TNDFLDLVGQ NVQVANIPDG FTAKGIVAMT FSCLAGVLGL ISLSTYGLMG VKKSEEEIIR
DLGMDPDAVE KVDVSDINSD EDSSRTSKNI E
