FER2_USTMA
ID FER2_USTMA Reviewed; 486 AA.
AC A1A652;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=High-affinity iron permease fer2 {ECO:0000303|PubMed:17138696};
DE AltName: Full=Fe-regulated protein 2 {ECO:0000303|PubMed:17138696};
GN Name=fer2 {ECO:0000303|PubMed:17138696}; ORFNames=UMAG_10023;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION, FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=521 / FGSC 9021;
RX PubMed=17138696; DOI=10.1105/tpc.106.043588;
RA Eichhorn H., Lessing F., Winterberg B., Schirawski J., Kamper J.,
RA Muller P., Kahmann R.;
RT "A ferroxidation/permeation iron uptake system is required for virulence in
RT Ustilago maydis.";
RL Plant Cell 18:3332-3345(2006).
CC -!- FUNCTION: Permease for high affinity iron uptake (PubMed:17138696).
CC {ECO:0000269|PubMed:17138696}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17138696};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression regulated by iron through the urbs1 transcription
CC factor (PubMed:17138696). During pathogenic development, expression is
CC confined to the phase of hyphal proliferation inside the plant
CC (PubMed:17138696). {ECO:0000269|PubMed:17138696}.
CC -!- DISRUPTION PHENOTYPE: Strongly reduces virulence (PubMed:17138696).
CC {ECO:0000269|PubMed:17138696}.
CC -!- SIMILARITY: Belongs to the oxidase-dependent Fe transporter (OFeT) (TC
CC 9.A.10.1) 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; CM003140; KIS71665.1; -; Genomic_DNA.
DR EMBL; BK004082; DAA04933.1; -; Genomic_DNA.
DR RefSeq; XP_011386613.1; XM_011388311.1.
DR AlphaFoldDB; A1A652; -.
DR STRING; 5270.UM00106P0; -.
DR EnsemblFungi; KIS71665; KIS71665; UMAG_10023.
DR GeneID; 23566099; -.
DR KEGG; uma:UMAG_10023; -.
DR VEuPathDB; FungiDB:UMAG_10023; -.
DR eggNOG; ENOG502QQWE; Eukaryota.
DR OrthoDB; 1158680at2759; -.
DR PHI-base; PHI:3918; -.
DR Proteomes; UP000000561; Chromosome 1.
DR GO; GO:0033573; C:high-affinity iron permease complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0034755; P:iron ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR004923; FTR1/Fip1/EfeU.
DR PANTHER; PTHR31632; PTHR31632; 1.
DR Pfam; PF03239; FTR1; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion transport; Iron; Iron transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Virulence.
FT CHAIN 1..486
FT /note="High-affinity iron permease fer2"
FT /id="PRO_0000441958"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 175..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 486 AA; 53084 MW; 3C34D86BBC22FC27 CRC64;
MSATGNKVFA PAIFFIAARE ALEASLVIGI LSGMLENLVV HTKSAEDLAA HDSLTESEKH
EVEQKKRALV RKLRKIVLLG ALTGLLIAFA IGAAFLAVFY TQVNDLYGKA EELWEGIFNL
VAVLLITPMS LAILRAGNSK RKWKRKLENA FSHQNIQPNH RRDEEGEATV VNANHSDDSA
SASSSSARQA AEEEAGTKTT RTEKLNPLEA VDVVPSMSGD QRRKRGGLRG LFSKPSGAVN
DLKLRMNRGT LALFTIPLIT TLREGLEGVV FIGGVSLGLP ATSIPLPAIV GLAVGLGIGF
LIFRSGNLVS VRIFLVFSTC FLLLIASGMA SRSVYYLQFY AYVQLVGDSA AESGDGPGSY
NSQGYIWHFN CCNPEANKGG TGWGILNSLV GWNNTATYGS VFMYIGYWFA VAGYLWYQIW
SEGRLALRFG GKTYWESNRS IQARQRKQEK AHQRQLREAD QEEHGHSSNS DKQQHPSEAG
PSTLSH
