ID   RIBJ_TRYCC              Reviewed;         472 AA.
AC   Q4D3E8;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=Tc00.1047053509885.70 {ECO:0000312|EMBL:EAN87055.1};
OS   Trypanosoma cruzi (strain CL Brener).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=353153 {ECO:0000312|Proteomes:UP000002296};
RN   [1] {ECO:0000312|Proteomes:UP000002296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL Brener {ECO:0000312|Proteomes:UP000002296};
RX   PubMed=16020725; DOI=10.1126/science.1112631;
RA   El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA   Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA   Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA   Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA   Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA   da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA   Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA   Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA   Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA   Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA   Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA   Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA   Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA   Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA   Andersson B.;
RT   "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT   disease.";
RL   Science 309:409-415(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; AAHK01001096; EAN87055.1; -; Genomic_DNA.
DR   RefSeq; XP_808906.1; XM_803813.1.
DR   AlphaFoldDB; Q4D3E8; -.
DR   SMR; Q4D3E8; -.
DR   STRING; 5693.XP_808906.1; -.
DR   PaxDb; Q4D3E8; -.
DR   EnsemblProtists; EAN87055; EAN87055; Tc00.1047053509885.70.
DR   GeneID; 3539434; -.
DR   KEGG; tcr:509885.70; -.
DR   eggNOG; KOG2504; Eukaryota.
DR   OMA; EFKTAWV; -.
DR   OrthoDB; 916876at2759; -.
DR   Proteomes; UP000002296; Unassembled WGS sequence.
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:0032218; P:riboflavin transport; IDA:UniProtKB.
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   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..472
FT                   /note="Riboflavin transporter RibJ"
FT                   /id="PRO_0000442705"
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..179
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        180..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..315
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..341
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..365
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        387..399
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        400..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        421..434
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        435..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        456..472
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          200..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   472 AA;  51218 MW;  EF42ED0D12DD4774 CRC64;
     MLPCFTRKPV DHPLGFLVAL SGLLMQLMSY GIDNSYSIFS DDMHKDPSLG YPSVTTISLG
     NSVSLGLSPA FGVLCGFLVD RVPPRLMMAV STLMLFAGLW LSSTFAHNVT AVTFSYCLLA
     SISSACMLSP GAAATSSWFN RYQGLAMGIN FSGGGVGSAI IPSLAGKWVV AYGWRKTFRL
     MSAFCAIGVV ATLLSARRAP PKKEEAGPSE YDEGQERQEQ GEEEQAHTDE ENRNNNNSNG
     ETTPARRGLH THKLNPWELF LTMFSRAFLG NFFCWLIFSW AFYSLIYVAV PYVSSMGKAG
     TVYADISPIP TDIASTLFTF YGVFQIVGSI LVGWLATGTT NEFAYVLCAT IGGIFCAFLG
     FCRSYVAFAL LLCVIGFCMA GMFAVMPALI AERLYGPNLG FYMGAVFLAG VVGGFSAPPI
     QAELQQRHYG NYTYVCVFMS ACMTLAAAVC YITMWRDKRV RIVSAAAEAK LA