FET3_GIBZE
ID FET3_GIBZE Reviewed; 622 AA.
AC I1RMG9;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Iron transport multicopper oxidase FET3 {ECO:0000250|UniProtKB:P38993};
DE EC=1.-.-.- {ECO:0000305|PubMed:20507510};
DE AltName: Full=Cell surface ferroxidase FET3 {ECO:0000303|PubMed:20507510};
DE Flags: Precursor;
GN Name=FET3 {ECO:0000303|PubMed:20507510};
GN ORFNames=FG05159, FGRAMPH1_01T17241;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20507510; DOI=10.1111/j.1364-3703.2007.00401.x;
RA Greenshields D.L., Liu G., Feng J., Selvaraj G., Wei Y.;
RT "The siderophore biosynthetic gene SID1, but not the ferroxidase gene FET3,
RT is required for full Fusarium graminearum virulence.";
RL Mol. Plant Pathol. 8:411-421(2007).
CC -!- FUNCTION: Cell surface ferroxidase; part of the reductive iron
CC assimilatory system (RIA), a siderophore-independent iron acquisition
CC process (PubMed:20507510). Required to oxidize Fe(2+) and release it
CC from the transporter (By similarity). Seems not to be involved in
CC virulence (PubMed:20507510). {ECO:0000250|UniProtKB:P38993,
CC ECO:0000269|PubMed:20507510}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P38993};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P38993};
CC Extracellular side {ECO:0000250|UniProtKB:P38993}.
CC -!- INDUCTION: Expression is up-regulated during iron starvation
CC (PubMed:20507510). {ECO:0000269|PubMed:20507510}.
CC -!- DISRUPTION PHENOTYPE: Produces wild-type amounts of siderophores and
CC growth at the same rate as the wild-type under iron limitation, but
CC accumulates high levels of free intracellular iron (PubMed:20507510).
CC Does not affect the virulence (PubMed:20507510).
CC {ECO:0000269|PubMed:20507510}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; HG970334; CEF85934.1; -; Genomic_DNA.
DR RefSeq; XP_011323662.1; XM_011325360.1.
DR AlphaFoldDB; I1RMG9; -.
DR SMR; I1RMG9; -.
DR STRING; 5518.FGSG_05159P0; -.
DR GeneID; 23552351; -.
DR KEGG; fgr:FGSG_05159; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G17241; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_7_3_1; -.
DR InParanoid; I1RMG9; -.
DR PHI-base; PHI:1011; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..622
FT /note="Iron transport multicopper oxidase FET3"
FT /evidence="ECO:0000255"
FT /id="PRO_5010124403"
FT TOPO_DOM 23..553
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 575..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..146
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 156..303
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 363..498
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT REGION 597..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 84
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 126
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 128
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 414
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 417
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 419
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 479
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 480
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 481
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 485
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 622 AA; 68712 MW; 925E52E307C71F54 CRC64;
MRPKLLSVEA ALFLALPELA RAATRKFDFE IGWVRANPDN AFERPVIGIN GQWPIPTIEV
DIGDRVIINA HNNLGNQSTS LHFHGLYMNG STHMDGPAGV SQCPIIPGTS FTYNFTVDQP
GTYWYHSHTA AQYPDGLRGP FIVHDKDFPY AKKYDEEVVL TLSDWYHDEM RSLIPQFMAK
SNPSGAEPVP KNALMNETTN FTMSVQPEKT YLFRVINVGA FAGQYLWFEG HKMQIVEVDG
IYTEEAEAEM IYISAAQRVS FLLTTKKDTS KNFPIVASMD TTLFDVLPPD LKYNSTGWLV
YDKKAEKPVP ATVDSLNPFD DMTLVPYDKM EILGKPDKEV VLDVKMDNLK DGKNYAFFND
ITYTEAKVPT LYTALSAGKD AEDPAVYGTY THSMVLKKNE IVQLVVNNLD SGRHPFHLHG
HAFQSVYRSE EEAGIWADAN VTEKNLPKTP MRRDTLVIYP NGNIVMRFKA DNPGVWLFHC
HIEWHVISGL IATFVEDPLA LQETIEIPKN HLDACAAANM PTKGNAAANT EDFLDLTGEN
KPANTLPPGF TPRGIVALVF SCICGILGVA VVAWYGFSAP VGSTSAGALS AGLVENDSGD
VHSAQKGPQE TVVSPTGDAR SH
