RIBJ_TRYB2
ID RIBJ_TRYB2 Reviewed; 547 AA.
AC Q57VW6; D6XFY5;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Riboflavin transporter RibJ {ECO:0000305};
DE AltName: Full=Riboflavin/flavin transporter {ECO:0000303|PubMed:28406895};
GN Name=RibJ {ECO:0000303|PubMed:28406895};
GN ORFNames=Tb927.5.470 {ECO:0000312|EMBL:AAX70248.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000312|Proteomes:UP000008524};
RN [1] {ECO:0000312|EMBL:AAZ11162.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=28406895; DOI=10.1371/journal.pntd.0005513;
RA Balcazar D.E., Vanrell M.C., Romano P.S., Pereira C.A., Goldbaum F.A.,
RA Bonomi H.R., Carrillo C.;
RT "The superfamily keeps growing: Identification in trypanosomatids of RibJ,
RT the first riboflavin transporter family in protists.";
RL PLoS Negl. Trop. Dis. 11:E0005513-E0005513(2017).
CC -!- FUNCTION: Transporter involved in riboflavin (vitamin B2) uptake. Also
CC transports FMN and FAD. {ECO:0000269|PubMed:28406895}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. RibJ family.
CC {ECO:0000305}.
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DR EMBL; AC159436; AAX70248.1; -; Genomic_DNA.
DR EMBL; CP000068; AAZ11162.1; -; Genomic_DNA.
DR RefSeq; XP_844721.1; XM_839628.1.
DR AlphaFoldDB; Q57VW6; -.
DR STRING; 5691.AAZ11162; -.
DR PaxDb; Q57VW6; -.
DR GeneID; 3657157; -.
DR KEGG; tbr:Tb927.5.470; -.
DR VEuPathDB; TriTrypDB:Tb927.5.470; -.
DR eggNOG; KOG2504; Eukaryota.
DR InParanoid; Q57VW6; -.
DR OMA; LVDIKWI; -.
DR Proteomes; UP000008524; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:GeneDB.
DR GO; GO:0032218; P:riboflavin transport; IDA:UniProtKB.
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; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..547
FT /note="Riboflavin transporter RibJ"
FT /id="PRO_0000442706"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..58
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..108
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..175
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..386
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..437
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..505
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 198..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 547 AA; 58490 MW; 37387620A6FB2D16 CRC64;
MLPSFTRKPA DHPIGYLVAL SGLLMQLMSY GIDNSYSIFS EDMHNDPSLG FPSITAISLG
NSVSLGLSPA FGVLAGFCVD RLPPRFMMAL STILLFTGLW ISSTLAANIY VVTFTYCLFA
SIGTACMLSP GAAATSSWFN RYQGLAMGIN FAGGGIGSAI IPPLAGKWVV AYGWRKAFQL
MSIFCAIGVL ATALSARRRE PKRDDSSADD ETREGNKSGN GSLVRRSNEP ATVGGEGAAN
NGHNEGKEDV REMGRKNGSH TNTSKVPPNG RGVGTNQQNG NDGEGLDVTE QSQRNNTFAS
AIDVDMDTSM DADEPQVIRS LHTHKLTPWE LFLSMFTLPF MGNFLCWFIY SWAFYSLIYA
AVPYISSMGK PGTVYAGVPP IPTDVAATLF TFYGVFQVVG SVLVGWLASL VTAEFAYVFC
ATVGGIGCGL LALGRSYVAF ALLLCIIGFC MAGMFAVMPT LIATHLYGPN LGFYFGAVFL
AGVVGGFVAP PMQATIQLRN NGSYAFVCVV MSVSMTLSAL VCYATLWRSK RSGIVLAARK
TKLVEIM
