MIRB_ASPFU
ID MIRB_ASPFU Reviewed; 612 AA.
AC Q4WF31;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=MFS siderochrome iron transporter B {ECO:0000303|PubMed:22903978};
GN Name=mirB {ECO:0000303|PubMed:22903978}; ORFNames=AFUA_3G03640;
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, MUTAGENESIS OF ALA-119; 241-ALA--GLY-248; TRP-245; TRP-247;
RP TYR-392; 461-GLY--TYR-466; 527-THR--ALA-540; 560-GLY--ALA-574; ARG-564 AND
RP TYR-571, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=22903978; DOI=10.1128/ec.00159-12;
RA Raymond-Bouchard I., Carroll C.S., Nesbitt J.R., Henry K.A., Pinto L.J.,
RA Moinzadeh M., Scott J.K., Moore M.M.;
RT "Structural requirements for the activity of the MirB ferrisiderophore
RT transporter of Aspergillus fumigatus.";
RL Eukaryot. Cell 11:1333-1344(2012).
CC -!- FUNCTION: Major facilitator transporter involved in triacetylfusarinine
CC C (TAFC) uptake (PubMed:22903978). Can also transport ferricrocin and
CC coprogen, but not ferrichrysin (PubMed:22903978).
CC {ECO:0000269|PubMed:22903978}.
CC -!- SUBCELLULAR LOCATION: Cell tip {ECO:0000269|PubMed:22903978}.
CC Cytoplasmic vesicle membrane {ECO:0000269|PubMed:22903978}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:22903978}. Cell membrane
CC {ECO:0000269|PubMed:22903978}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22903978}. Note=Localizes to vesicles which cycle
CC between the cytoplasm and the plasma membrane and is concentrated at
CC the hyphal tips (PubMed:22903978). {ECO:0000269|PubMed:22903978}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AAHF01000010; EAL86646.1; -; Genomic_DNA.
DR RefSeq; XP_748684.1; XM_743591.1.
DR AlphaFoldDB; Q4WF31; -.
DR STRING; 746128.CADAFUBP00004366; -.
DR EnsemblFungi; EAL86646; EAL86646; AFUA_3G03640.
DR GeneID; 3505886; -.
DR KEGG; afm:AFUA_3G03640; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_012970_1_0_1; -.
DR InParanoid; Q4WF31; -.
DR OMA; TAACYIP; -.
DR OrthoDB; 641071at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0051286; C:cell tip; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Ion transport; Iron; Iron transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..612
FT /note="MFS siderochrome iron transporter B"
FT /id="PRO_0000444407"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22903978"
FT TRANSMEM 87..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..127
FT /note="Extracellular"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..187
FT /note="Extracellular"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..246
FT /note="Extracellular"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..334
FT /note="Extracellular"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 371..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..409
FT /note="Extracellular"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..463
FT /note="Extracellular"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..575
FT /note="Extracellular"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:22903978"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 55..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 119
FT /note="A->D: Decreases the uptake of triacetylfusarinine C
FT (TAFC)."
FT /evidence="ECO:0000269|PubMed:22903978"
FT MUTAGEN 241..248
FT /note="Missing: In Loop3Del; decreases the uptake of
FT triacetylfusarinine C (TAFC)."
FT /evidence="ECO:0000269|PubMed:22903978"
FT MUTAGEN 245
FT /note="W->A: Decreases the uptake of triacetylfusarinine C
FT (TAFC); when associated with A-247."
FT /evidence="ECO:0000269|PubMed:22903978"
FT MUTAGEN 247
FT /note="W->A: Decreases the uptake of triacetylfusarinine C
FT (TAFC); when associated with A-245."
FT /evidence="ECO:0000269|PubMed:22903978"
FT MUTAGEN 392
FT /note="Y->A: Decreases the uptake of triacetylfusarinine C
FT (TAFC)."
FT /evidence="ECO:0000269|PubMed:22903978"
FT MUTAGEN 461..466
FT /note="Missing: In Loop6Del; decreases the uptake of
FT triacetylfusarinine C (TAFC)."
FT /evidence="ECO:0000269|PubMed:22903978"
FT MUTAGEN 527..540
FT /note="Missing: In Loop7Del1; decreases the uptake of
FT triacetylfusarinine C (TAFC)."
FT /evidence="ECO:0000269|PubMed:22903978"
FT MUTAGEN 560..574
FT /note="Missing: In Loop7Del2; decreases the uptake of
FT triacetylfusarinine C (TAFC)."
FT /evidence="ECO:0000269|PubMed:22903978"
FT MUTAGEN 564
FT /note="R->A: Decreases the uptake of triacetylfusarinine C
FT (TAFC)."
FT /evidence="ECO:0000269|PubMed:22903978"
FT MUTAGEN 571
FT /note="Y->A: Decreases the uptake of triacetylfusarinine C
FT (TAFC)."
FT /evidence="ECO:0000269|PubMed:22903978"
SQ SEQUENCE 612 AA; 66851 MW; 8D6E6EECE46C04D5 CRC64;
MLHVLSVGPS HAAFTVEAAM ATMKKFHSIV GEKPAQDAEA PSVDDPNVGQ IRADDKEAAH
APANAETNNE EANPSDGAQA GVKKIEAVTL SWTRGTAIWF LTLVNDFRLS MYTSLNAYAT
SSFLGHSLLT VINIVSYVMG GSVYIPMAKA LDLWGRAEGF LLMTFFCILG LILLASSQNL
PTYCAGQVFY KVGFGGLSYT WNVLAADVTN LRNRGLAFAF TSSPALISAF AGSKAASDLL
AHSTWRWGFG MWAIILPVVA LPIYGLLAYH LRQAEKKGVL VKETRDWSIT PKTVWWAIME
FDLPGVLLFA GGFVIFLLPF TLAATAPHGY QTDYIIAMIT LGLALIIAFG FYEMLVAPVP
FLNYKFLIDR TVLGACLLDM TYQVSYYCYA SYLPSFLQVV YELDVATAGY VTNTFSVVSF
VFLFFAGWLI RWTGRFKWIL WVCVPLYIFG LGLMIHFRQP GGYIGYIVMC EIFFSVAGSV
FILCVQLAVL ASVDHQHVAA VLALLFVMGS IGGSIGSAIC GAIWTSTFLS RLERNLPASA
MPDLSLIYSS LPTQLSYPVG SATRTAIVEA YGYAQARMLI AGTAFMVLGF IWVGMMRNLN
VKNMTQTKGN VV
