MFS1_CERS8
ID MFS1_CERS8 Reviewed; 521 AA.
AC M2R8W9;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=MFS siderochrome iron transporter 1 {ECO:0000303|PubMed:28842536};
GN Name=mfs1 {ECO:0000303|PubMed:28842536}; ORFNames=CERSUDRAFT_116654;
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B;
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
RN [2]
RP INDUCTION, AND FUNCTION.
RC STRAIN=B;
RX PubMed=28842536; DOI=10.1128/aem.01478-17;
RA Brandenburger E., Gressler M., Leonhardt R., Lackner G., Habel A.,
RA Hertweck C., Brock M., Hoffmeister D.;
RT "A highly conserved basidiomycete peptide synthetase produces a trimeric
RT hydroxamate siderophore.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
CC -!- FUNCTION: Major facilitator transporter probably involved in
CC siderophore basidioferrin transmembrane transport (PubMed:28842536).
CC {ECO:0000305|PubMed:28842536}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced under iron-depleted conditions
CC (PubMed:28842536). {ECO:0000269|PubMed:28842536}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; KB445801; EMD35186.1; -; Genomic_DNA.
DR AlphaFoldDB; M2R8W9; -.
DR SMR; M2R8W9; -.
DR EnsemblFungi; EMD35186; EMD35186; CERSUDRAFT_116654.
DR HOGENOM; CLU_001265_52_4_1; -.
DR OrthoDB; 724235at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..521
FT /note="MFS siderochrome iron transporter 1"
FT /id="PRO_0000444318"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 521 AA; 56014 MW; 144321E37D822530 CRC64;
MDKTASLTSQ DAEKHDPDAL RKERATDPPD LFEHGALDPV YQAKAHLIAS AIQEIGMGKY
QWGLFVVAGF GWFSDSVWPL MGSLILSPVV NEFQFNSPFL SLALNAGLLA GAIFWAFGCD
IWGRRWSFNL SLLIAGAFGL AAGGTQNFVA LACLFAVVGF GVGGNMPVDS AVFLDFVPGS
YQYLLTILSI WWSIGQLVAS LIAWPLIANF SCPIGSTTCT RADNMGWRYL LFTLGGMTLL
LWAIRFFVFP LMESPRFLVG RGRDAEAIAV IQRIAQFNGR PSSLTLEELA MVAEKAAPKD
AVATQRRQVL SQSSDFSTDH VKGLFATPKL AWSTSLLIAL WGIIGLASTL YNSFLPFLLA
NRGAEFGDSS YFITYRNQVI IAVLGVPGAF LAGWAVEQPY LGRKGTLAIS AGLTGVFLFA
TTTARSSNAL LGWNCGYAFH SNIMYGVLYA ISPEVFPAKD RGTGNGLTAT ATRVFGLIAP
VIALYANLST AVPVYVSGAL IIASGAMALL LPYEPRGRAS L
