MIRC_ASPFU
ID MIRC_ASPFU Reviewed; 611 AA.
AC Q4WHE1;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=MFS siderochrome iron transporter C {ECO:0000303|PubMed:28367141};
GN Name=mirC {ECO:0000303|PubMed:28367141}; ORFNames=AFUA_2G05730;
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, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=28367141; DOI=10.3389/fmicb.2017.00418;
RA Mulvihill E.D., Moloney N.M., Owens R.A., Dolan S.K., Russell L., Doyle S.;
RT "Functional investigation of iron-responsive microsomal proteins, including
RT MirC, in Aspergillus fumigatus.";
RL Front. Microbiol. 8:418-418(2017).
CC -!- FUNCTION: Major facilitator transporter that contributes to the
CC maintenance of intracellular siderophore ferricrocin (FC) levels
CC (PubMed:28367141). Plays a role in conidiation and confers protection
CC against oxidative stress (PubMed:28367141). Contributes also to fungal
CC virulence in the Galleria mellonella animal model system
CC (PubMed:28367141). Does not appear to play a role in either siderophore
CC export or uptake (PubMed:28367141). {ECO:0000269|PubMed:28367141}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Note=localizes intracellularly, possibly to
CC vacuole-like structures, but not found in the plasma membrane or at the
CC nucleus (PubMed:28367141). {ECO:0000269|PubMed:28367141}.
CC -!- INDUCTION: Expression is induced under iron limitation
CC (PubMed:28367141). {ECO:0000269|PubMed:28367141}.
CC -!- DISRUPTION PHENOTYPE: Reduces growth under iron limitation and
CC increases sensitivity to hydrogen peroxide (PubMed:28367141). Decreases
CC intracellular ferricrocin level under iron limitation
CC (PubMed:28367141). Leads to increased abundance of siderophore
CC biosynthetic enzymes and of hapX (PubMed:28367141). Finally, decreases
CC the virulence in the Galleria mellonella animal model system
CC (PubMed:28367141). {ECO:0000269|PubMed:28367141}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AAHF01000008; EAL87664.2; -; Genomic_DNA.
DR RefSeq; XP_749702.2; XM_744609.2.
DR AlphaFoldDB; Q4WHE1; -.
DR SMR; Q4WHE1; -.
DR STRING; 746128.CADAFUBP00002223; -.
DR EnsemblFungi; EAL87664; EAL87664; AFUA_2G05730.
DR GeneID; 3507165; -.
DR KEGG; afm:AFUA_2G05730; -.
DR VEuPathDB; FungiDB:Afu2g05730; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_012970_2_0_1; -.
DR InParanoid; Q4WHE1; -.
DR OMA; CIAVSIY; -.
DR OrthoDB; 641071at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015343; F:siderophore transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IEP:AspGD.
DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion transport; Iron; Iron transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..611
FT /note="MFS siderochrome iron transporter C"
FT /id="PRO_0000444408"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 611 AA; 67058 MW; DA786DC6CAD0C9EB CRC64;
MPFLDHRTGP SYGTIDQMEQ HSDDEGERFL QEQCDTGRFS SDITSISEDS VQEGVRKIEA
INLTWTARSL VIAYVSIFLM SFCTSLEGQT VMSLGAYATS AFSKHSLIST VLVVQNVVNA
VIKPPMAKVA DVFGRFEAFC VSILIYVLGY IQMAASTNVQ TYASAQIFYS AGSTGLQILQ
QVFIADSSNL LNRAFLALLP EFPFLVTVWI GPTIADAVLK HASWRWGYGM WSIILPASFL
PLALSLLLNQ RKARRLNLIK PKSRPRGGVF AVLRRTWYDL DMGGLILLSA AVTLILVPLT
LAANSKNGWK SDSIVAMIVV GLFCLIALPF WESSKRLAPK PLLSLHLLKQ RTALAGCTLA
FWYFMAFYFS VQPYFYSYLQ VVQGYDVATA GRVTQTFAFT STIAAFAVSI LIKYTRRYRA
FVIAGCVVYI IGMVLMMVTR HEGSTPAQIL VTQVVVGIGG GLLNVPVQLG VQASASHQEV
AAATAMFLTS MEMGGAVGAA LSGAVWTHNI PRKLRLYLPE ENKGDADAIF GKITKALSYP
LGSPVRVAIN QAYQETFKKL LILALIAIIP LVPLSLAMED YKLDKMSEEP LVDPVPAEEG
EIEPNRHVKR T
