ID   RSB1_YEAS1              Reviewed;         382 AA.
AC   B3LJA1;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Sphingoid long-chain base transporter RSB1;
GN   Name=RSB1; ORFNames=SCRG_01451;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent translocation of sphingoid long-
CC       chain bases (LCBs) from the cytoplasmic site toward the
CC       extracytoplasmic side of the membrane (flip-flop). Involved in the
CC       establishment of the functional lipid asymmetry of the plasma membrane.
CC       Regulates intracellular levels of LCBs, sphingolipid precursors that
CC       are growth inhibitory at increased levels (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein.
CC   -!- INDUCTION: In response to loss of mitochondrial DNA in a transcription
CC       factor PDR3-dependent manner. Induced in response to altered
CC       glycerophospholipid asymmetry of the plasma membrane in a transcription
CC       factor PDR1-dependent manner (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lipid-translocating exporter (LTE) (TC
CC       9.A.26.1) family. {ECO:0000305}.
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DR   EMBL; CH408045; EDV10654.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LJA1; -.
DR   EnsemblFungi; EDV10654; EDV10654; SCRG_01451.
DR   HOGENOM; CLU_033465_6_3_1; -.
DR   Proteomes; UP000008335; 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:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007568; RTA1.
DR   PANTHER; PTHR31465; PTHR31465; 1.
DR   Pfam; PF04479; RTA1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Lipid transport; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..382
FT                   /note="Sphingoid long-chain base transporter RSB1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000393314"
FT   TOPO_DOM        1..34
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..90
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..171
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        193..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..281
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..382
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   382 AA;  43205 MW;  3D4CF68EC2CA9908 CRC64;
     MSNATNNTLG SLLPQLEAAA NSNSLYGGMV PNLRFNITMI VIWGILLTIH VVQLLMRQYW
     FSIAFICTGI LEVLGFIGRT WSHSNVADMD AFLLNMICLT IAPVFTMGGI YYQLAKLIEV
     YGHRFSLLPS PMAYSFIFIC SDIVSLVVQA VGGGLCGVAV TDGTSTTTGN HVFIAGLAIQ
     VASMAIFLML WFHFLFRIYI SVRWEHINSR PISLSLLKIS QTEVDYLYRE KFHFLRLEPK
     RWVFHYFNLA MTVAVLTIFT RCCYRLAELV VGWDGYLITH EWYFIILDAL MMAIATVTLT
     IFHPGFAFKG RSTSIPITPG HVDPETLPHT DDVEDILDTS DSKQFDIEKE EFQASMKYPI
     STFKQFMSKI ANLFSSKKKA KL