FTRA_ASPFU
ID FTRA_ASPFU Reviewed; 370 AA.
AC E9QT42;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=High affinity iron permease ftrA {ECO:0000303|PubMed:15504822};
GN Name=ftrA {ECO:0000303|PubMed:15504822}; ORFNames=AFUA_5G03800;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=15504822; DOI=10.1084/jem.20041242;
RA Schrettl M., Bignell E., Kragl C., Joechl C., Rogers T., Arst H.N. Jr.,
RA Haynes K., Haas H.;
RT "Siderophore biosynthesis but not reductive iron assimilation is essential
RT for Aspergillus fumigatus virulence.";
RL J. Exp. Med. 200:1213-1219(2004).
RN [3]
RP INDUCTION.
RX PubMed=18721228; DOI=10.1111/j.1365-2958.2008.06376.x;
RA Schrettl M., Kim H.S., Eisendle M., Kragl C., Nierman W.C., Heinekamp T.,
RA Werner E.R., Jacobsen I., Illmer P., Yi H., Brakhage A.A., Haas H.;
RT "SreA-mediated iron regulation in Aspergillus fumigatus.";
RL Mol. Microbiol. 70:27-43(2008).
RN [4]
RP INDUCTION.
RX PubMed=21062375; DOI=10.1111/j.1365-2958.2010.07389.x;
RA Liu H., Gravelat F.N., Chiang L.Y., Chen D., Vanier G., Ejzykowicz D.E.,
RA Ibrahim A.S., Nierman W.C., Sheppard D.C., Filler S.G.;
RT "Aspergillus fumigatus AcuM regulates both iron acquisition and
RT gluconeogenesis.";
RL Mol. Microbiol. 78:1038-1054(2010).
CC -!- FUNCTION: High affinity iron permease; part of the reductive iron
CC assimilatory system (RIA), a siderophore-independent high affinity iron
CC uptake mechanism (PubMed:15504822). {ECO:0000269|PubMed:15504822}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is up-regulated during iron starvation and is
CC controlled by the GATA-type transcription factor sreA and the Zinc
CC cluster transcription factor acuM (PubMed:15504822, PubMed:18721228,
CC PubMed:21062375). {ECO:0000269|PubMed:15504822,
CC ECO:0000269|PubMed:18721228, ECO:0000269|PubMed:21062375}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the virulence in a murine model
CC of invasive aspergillosis (PubMed:15504822). Displays an 8-fold
CC increase in external siderophore triacetylfusarinine C (TAFC)
CC production after 12h of growth in iron-depleted conditions
CC (PubMed:15504822). {ECO:0000269|PubMed:15504822}.
CC -!- SIMILARITY: Belongs to the oxidase-dependent Fe transporter (OFeT) (TC
CC 9.A.10.1) family. {ECO:0000305}.
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DR EMBL; AAHF01000011; EAL85926.2; -; Genomic_DNA.
DR RefSeq; XP_747964.2; XM_742871.2.
DR AlphaFoldDB; E9QT42; -.
DR SMR; E9QT42; -.
DR STRING; 746128.CADAFUBP00005120; -.
DR EnsemblFungi; EAL85926; EAL85926; AFUA_5G03800.
DR GeneID; 3505587; -.
DR KEGG; afm:AFUA_5G03800; -.
DR VEuPathDB; FungiDB:Afu5g03800; -.
DR eggNOG; ENOG502QQWE; Eukaryota.
DR HOGENOM; CLU_046738_0_1_1; -.
DR InParanoid; E9QT42; -.
DR OMA; ITMLKMD; -.
DR OrthoDB; 1158680at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
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:0061840; F:high-affinity ferrous iron transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IEP:AspGD.
DR GO; GO:0034755; P:iron ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0033215; P:reductive iron assimilation; IEA:EnsemblFungi.
DR InterPro; IPR004923; FTR1/Fip1/EfeU.
DR PANTHER; PTHR31632; PTHR31632; 1.
DR Pfam; PF03239; FTR1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Ion transport; Iron; Iron transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..370
FT /note="High affinity iron permease ftrA"
FT /id="PRO_0000444441"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 335..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 40476 MW; A6217725DEE6E8CF CRC64;
MAKDVFAVPI FFICFRECVE TSIIVSVLLS FIKQTLGQEQ DATTRKRLIR QVWWGVAIGL
FISVCIGAGM IGAFYGYGKD HFASTEDLWE GIFSLIASVI ITIMGAALLR VTKLQEKWRV
KLAQALEAKP LTGGTFKNNL KLWAEKYAMF LLPFITVLRE GLEAVVFIGG VSLSFPATAF
PLPVFTGILA GVAIGYLLYR GGNQASLQIF LIISTCILYL VAAGLFSRGV WYLENNTWNH
VIGGDAAETG AGPGSYDIRQ SVWHVNCCSP LVNGGGGWGI FNAILGWTNS ATYGSVLSYN
LYWIAVIVWF VAMRHKERHG RLPVVDPLLN RLRGRKSAEP GNGEQDVEVS TIPSDLQTES
KIPKSGASLV
