RSB1_YEAS8
ID RSB1_YEAS8 Reviewed; 382 AA.
AC C8ZI10;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Sphingoid long-chain base transporter RSB1;
GN Name=RSB1; ORFNames=EC1118_1O4_2476g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
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; FN394216; CAY86335.1; -; Genomic_DNA.
DR AlphaFoldDB; C8ZI10; -.
DR EnsemblFungi; CAY86335; CAY86335; EC1118_1O4_2476g.
DR HOGENOM; CLU_033465_6_3_1; -.
DR Proteomes; UP000000286; Chromosome XV, Scaffold EC1118_1O4.
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_0000393318"
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; 43221 MW; 6D416E973F79C38C CRC64;
MSNATNNTLG SLLPQLEAAA NSNSLYGGMV PNLRFNITMI VIWGILLTIH VVQLLMRQYW
FSIAFICTGI LEVLGYIGRT 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