RSB1_YEAST
ID RSB1_YEAST Reviewed; 382 AA.
AC Q08417; D6W2B5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Sphingoid long-chain base transporter RSB1;
GN Name=RSB1; OrderedLocusNames=YOR049C; ORFNames=O2787;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=12034738; DOI=10.1074/jbc.m203385200;
RA Kihara A., Igarashi Y.;
RT "Identification and characterization of a Saccharomyces cerevisiae gene,
RT RSB1, involved in sphingoid long-chain base release.";
RL J. Biol. Chem. 277:30048-30054(2002).
RN [4]
RP INDUCTION.
RX PubMed=15342785; DOI=10.1091/mbc.e04-06-0458;
RA Kihara A., Igarashi Y.;
RT "Cross talk between sphingolipids and glycerophospholipids in the
RT establishment of plasma membrane asymmetry.";
RL Mol. Biol. Cell 15:4949-4959(2004).
RN [5]
RP IDENTIFICATION OF FRAMESHIFT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-3
RP AND ASN-6, INDUCTION, AND MUTAGENESIS OF ASN-3 AND ASN-6.
RC STRAIN=ATCC 96099 / S288c / SEY6210;
RX PubMed=16407254; DOI=10.1074/jbc.m512115200;
RA Panwar S.L., Moye-Rowley W.S.;
RT "Long chain base tolerance in Saccharomyces cerevisiae is induced by
RT retrograde signals from the mitochondria.";
RL J. Biol. Chem. 281:6376-6384(2006).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
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.
CC {ECO:0000269|PubMed:12034738}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16407254};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16407254}.
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. {ECO:0000269|PubMed:15342785,
CC ECO:0000269|PubMed:16407254}.
CC -!- SIMILARITY: Belongs to the lipid-translocating exporter (LTE) (TC
CC 9.A.26.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA99241.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=DAA10831.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z74957; CAA99241.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006948; DAA10831.1; ALT_FRAME; Genomic_DNA.
DR PIR; S66923; S66923.
DR RefSeq; NP_014692.1; NM_001183468.1.
DR AlphaFoldDB; Q08417; -.
DR BioGRID; 34450; 98.
DR DIP; DIP-3834N; -.
DR MINT; Q08417; -.
DR STRING; 4932.YOR049C; -.
DR SwissLipids; SLP:000000354; -.
DR TCDB; 9.A.26.1.2; the lipid-translocating exporter (lte) family.
DR iPTMnet; Q08417; -.
DR MaxQB; Q08417; -.
DR PaxDb; Q08417; -.
DR PRIDE; Q08417; -.
DR GeneID; 854214; -.
DR KEGG; sce:YOR049C; -.
DR SGD; S000005575; RSB1.
DR eggNOG; ENOG502QU4U; Eukaryota.
DR HOGENOM; CLU_033465_6_3_1; -.
DR InParanoid; Q08417; -.
DR BioCyc; YEAST:G3O-33593-MON; -.
DR PRO; PR:Q08417; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08417; protein.
DR GO; GO:0071944; C:cell periphery; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0045332; P:phospholipid translocation; IMP:SGD.
DR GO; GO:1905329; P:sphingoid long-chain base transport; IDA:SGD.
DR InterPro; IPR007568; RTA1.
DR PANTHER; PTHR31465; PTHR31465; 1.
DR Pfam; PF04479; RTA1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Lipid transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..382
FT /note="Sphingoid long-chain base transporter RSB1"
FT /id="PRO_0000262738"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..171
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16407254"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16407254"
FT MUTAGEN 3
FT /note="N->Q: Increases sensitivity towards LCBs."
FT /evidence="ECO:0000269|PubMed:16407254"
FT MUTAGEN 6
FT /note="N->Q: Increases sensitivity towards LCBs."
FT /evidence="ECO:0000269|PubMed:16407254"
SQ SEQUENCE 382 AA; 43187 MW; 3D49E28D16CC5908 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 ITVAVLTIFT RCCYRLAELV VGWDGYLITH EWYFIILDAL MMAIATVTLT
IFHPGFAFKG RSTSIPITPG HVDPETLPHT DDVEDILDTS DSKQFDIEKE EFQASMKYPI
STFKQFMSKI ANLFSSKKKA KL
