FETC_EPIFE
ID FETC_EPIFE Reviewed; 622 AA.
AC K7NCS2;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Iron transport multicopper oxidase fetC {ECO:0000250|UniProtKB:P38993};
DE EC=1.-.-.- {ECO:0000305|PubMed:23658520};
DE AltName: Full=Cell surface ferroxidase fetC {ECO:0000303|PubMed:23658520};
DE Flags: Precursor;
GN Name=fetC {ECO:0000303|PubMed:23658520};
OS Epichloe festucae (strain E2368).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX NCBI_TaxID=696363;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=E2368;
RX PubMed=23658520; DOI=10.1371/journal.ppat.1003332;
RA Johnson L.J., Koulman A., Christensen M., Lane G.A., Fraser K.,
RA Forester N., Johnson R.D., Bryan G.T., Rasmussen S.;
RT "An extracellular siderophore is required to maintain the mutualistic
RT interaction of Epichloe festucae with Lolium perenne.";
RL PLoS Pathog. 9:E1003332-E1003332(2013).
CC -!- FUNCTION: Cell surface ferroxidase; part of the reductive iron
CC assimilatory system (RIA), a siderophore-independent high affinity iron
CC uptake mechanism (PubMed:23658520). Required to oxidize Fe(2+) and
CC release it from the transporter (By similarity).
CC {ECO:0000250|UniProtKB:P38993, ECO:0000305|PubMed:23658520}.
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 repressed by iron starvation and up-regulated
CC in the absence of the sidN siderophore synthetase (PubMed:23658520).
CC {ECO:0000269|PubMed:23658520}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JN132406; AET13878.1; -; Genomic_DNA.
DR AlphaFoldDB; K7NCS2; -.
DR SMR; K7NCS2; -.
DR PhylomeDB; K7NCS2; -.
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; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..622
FT /note="Iron transport multicopper oxidase fetC"
FT /evidence="ECO:0000255"
FT /id="PRO_5003909009"
FT TOPO_DOM 21..552
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..144
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 154..301
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 362..497
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT REGION 597..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80
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 82
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 124
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="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 412
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 415
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 417
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 478
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="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P38993"
FT BINDING 480
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 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|UniProtKB:P38993"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 622 AA; 68086 MW; 348940366064EEDB CRC64;
MARLVHLTAV LAASIRLAAA ATINHDFNVT WVRANPDGAF ERPVIGINGK WPIPTIECNL
GDRIVINLNN QLGNQSTSLH FHGLFQNGTN HMDGPSGVTQ CAVPPGSSVT YNFTVDQPGT
YWYHSHNDGQ YPDGLRGPLV VHDPEFPYKK EVDEEIVLTL SDWYHDEIQT LIPQFLSKTN
PTGAEPVPNA CLINDTQNIT VSVQPGKTYH VRVINIGAFA GQYLWFEGHK MRIVEVDGVY
TKDAEADMIY ITAAQRVSFL LTTRNDTNAN FPFMASMDKA LFDKLPADLN YNSTGWLSYD
KSKSYPDPAL VDELNPFDDM TLEAYDGMEL LPEPDQNVAL DVIMKNLGDG VNYAFFGNIT
YKSPKVPTLY SVLSSGDKAT DPAIYGEHTH PFVLKKNEIV QIVVNNLDEG RHPFHLHGHN
FQAIYRSNES AGTWEDGGGA AGKTFPKVPM RRDTLLIYPN GNMVLRFKAN NPGVWLFHCH
IEWHVISGLV ATFVEAPMDL QKSLAIPTDH LDACKAGNIP TEGNAAGNTK DLLDLSGQNT
PPDPLPAGFT TRGIVALVFS CVTGILGICV VAWYGMSQPL EEATAAVATL VREAQVTGSG
TSPNHDDGNA AATEAGVLRR RT
