FET3_CANGA
ID FET3_CANGA Reviewed; 635 AA.
AC Q96WT3; Q6FU48;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Iron transport multicopper oxidase FET3;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=FET3; OrderedLocusNames=CAGL0F06413g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cg1012;
RA Tatsuno K.;
RT "Cloning and characterizing a multicopper oxidase gene from Candida
RT glabrata.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; AB047078; BAB62813.1; -; Genomic_DNA.
DR EMBL; CR380952; CAG59170.1; -; Genomic_DNA.
DR RefSeq; XP_446246.1; XM_446246.1.
DR AlphaFoldDB; Q96WT3; -.
DR SMR; Q96WT3; -.
DR STRING; 5478.XP_446246.1; -.
DR PRIDE; Q96WT3; -.
DR EnsemblFungi; CAG59170; CAG59170; CAGL0F06413g.
DR GeneID; 2887784; -.
DR KEGG; cgr:CAGL0F06413g; -.
DR CGD; CAL0131028; FET3.
DR VEuPathDB; FungiDB:CAGL0F06413g; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_7_3_1; -.
DR InParanoid; Q96WT3; -.
DR OMA; VHYDDTM; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..635
FT /note="Iron transport multicopper oxidase FET3"
FT /id="PRO_0000002957"
FT TOPO_DOM 18..559
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..628
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..140
FT /note="Plastocyanin-like 1"
FT DOMAIN 190..292
FT /note="Plastocyanin-like 2"
FT DOMAIN 382..501
FT /note="Plastocyanin-like 3"
FT BINDING 77
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 79
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 122
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 124
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 413
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 416
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 418
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 483
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 484
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 485
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 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 CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 72020 MW; 6D6333BECFFD401F CRC64;
MMVPLLLSTY FITAVYGATH TFHWTTGWGN RNVDGIKERP VITCNGEYPW PDVRVAKGDR
IEVYLTNGFN NTNTSLHFHG MFQRGTNQMD GVPYLTQCPI GPGDTMLYNF TVDENVGTYW
YHSHTDGQYE DGMRGLFVIE DGENNKNFPY EYDEDVMLSI GEWYDTTVDV LTRKFLNLNN
PTGAEPIPQN LILNNTMNLT WEVQPDTTYL LRIVNVGGFV SQYFWIEDHE MEVVEVDGVY
VEKNTTNMLY ITVAQRYAVL VHTKNDTSKN FAIMQKFDDT MLDVIPKDLQ LNATSYLVYD
KSKPMPEQNY VDSIDDYLDD FYLVPMDKEE LYPEADHVIT IDVIMDNLIN GVNYAFFNNI
TYTTPKVPTL LTVLSAGQDA LNPFIYGTNT NTFVLKKGEV VDLIVNNQDT GKHPFHLHGH
VFQTILRDRE FDDAKGEKPH SFNDSDHAAY PSIPMKRDTV YLNPQSNMVL RFKADNPGVW
FFHCHIEWHL LQGLAVVMVE DPISIQNTAS QHLTANGLQV CGNVKVPTQG NAAANDSDFF
NLEGQNVQHK SIPTGFTKKG IIAMTFSCLA GVLGITMIAI YGFSEIPEPE IKVMRNLHLN
PEDVLEKTSS SSVISASNSS SLEDSRNQKK KFIFF
