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Sphingoid long-chain base transporter RSB1

 RSB1_YEAST              Reviewed;         382 AA.
Q08417; D6W2B5;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 3.
12-SEP-2018, entry version 104.
RecName: Full=Sphingoid long-chain base transporter RSB1;
Name=RSB1; OrderedLocusNames=YOR049C; ORFNames=O2787;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=12034738; DOI=10.1074/jbc.M203385200;
Kihara A., Igarashi Y.;
"Identification and characterization of a Saccharomyces cerevisiae
gene, RSB1, involved in sphingoid long-chain base release.";
J. Biol. Chem. 277:30048-30054(2002).
[4]
INDUCTION.
PubMed=15342785; DOI=10.1091/mbc.E04-06-0458;
Kihara A., Igarashi Y.;
"Cross talk between sphingolipids and glycerophospholipids in the
establishment of plasma membrane asymmetry.";
Mol. Biol. Cell 15:4949-4959(2004).
[5]
IDENTIFICATION OF FRAMESHIFT, SUBCELLULAR LOCATION, GLYCOSYLATION AT
ASN-3 AND ASN-6, INDUCTION, AND MUTAGENESIS OF ASN-3 AND ASN-6.
STRAIN=ATCC 96099 / S288c / SEY6210;
PubMed=16407254; DOI=10.1074/jbc.M512115200;
Panwar S.L., Moye-Rowley W.S.;
"Long chain base tolerance in Saccharomyces cerevisiae is induced by
retrograde signals from the mitochondria.";
J. Biol. Chem. 281:6376-6384(2006).
[6]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
-!- FUNCTION: Catalyzes the ATP-dependent translocation of sphingoid
long-chain bases (LCBs) from the cytoplasmic site toward the
extracytoplasmic side of the membrane (flip-flop). Involved in the
establishment of the functional lipid asymmetry of the plasma
membrane. Regulates intracellular levels of LCBs, sphingolipid
precursors that are growth inhibitory at increased levels.
{ECO:0000269|PubMed:12034738}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16407254};
Multi-pass membrane protein {ECO:0000269|PubMed:16407254}.
-!- INDUCTION: In response to loss of mitochondrial DNA in a
transcription factor PDR3-dependent manner. Induced in response to
altered glycerophospholipid asymmetry of the plasma membrane in a
transcription factor PDR1-dependent manner.
{ECO:0000269|PubMed:15342785, ECO:0000269|PubMed:16407254}.
-!- SIMILARITY: Belongs to the lipid-translocating exporter (LTE) (TC
9.A.26.1) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA99241.1; Type=Frameshift; Positions=22; Evidence={ECO:0000305};
Sequence=DAA10831.1; Type=Frameshift; Positions=22; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Z74957; CAA99241.1; ALT_FRAME; Genomic_DNA.
EMBL; BK006948; DAA10831.1; ALT_FRAME; Genomic_DNA.
PIR; S66923; S66923.
RefSeq; NP_014692.1; NM_001183468.1.
BioGrid; 34450; 97.
DIP; DIP-3834N; -.
MINT; Q08417; -.
STRING; 4932.YOR049C; -.
SwissLipids; SLP:000000354; -.
TCDB; 9.A.26.1.2; the lipid-translocating exporter (lte) family.
iPTMnet; Q08417; -.
MaxQB; Q08417; -.
PaxDb; Q08417; -.
PRIDE; Q08417; -.
GeneID; 854214; -.
KEGG; sce:YOR049C; -.
EuPathDB; FungiDB:YOR049C; -.
SGD; S000005575; RSB1.
HOGENOM; HOG000111206; -.
InParanoid; Q08417; -.
OrthoDB; EOG092C3EMZ; -.
BioCyc; YEAST:G3O-33593-MONOMER; -.
PRO; PR:Q08417; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0071944; C:cell periphery; IDA:SGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IDA:SGD.
GO; GO:0045332; P:phospholipid translocation; IMP:SGD.
GO; GO:0006950; P:response to stress; IEA:InterPro.
GO; GO:1905329; P:sphingoid long-chain base transport; IMP:SGD.
InterPro; IPR007568; RTA1.
PANTHER; PTHR31465; PTHR31465; 1.
Pfam; PF04479; RTA1; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Glycoprotein; Lipid transport;
Membrane; Reference proteome; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 382 Sphingoid long-chain base transporter
RSB1.
/FTId=PRO_0000262738.
TOPO_DOM 1 34 Extracellular. {ECO:0000255}.
TRANSMEM 35 55 Helical. {ECO:0000255}.
TOPO_DOM 56 57 Cytoplasmic. {ECO:0000255}.
TRANSMEM 58 78 Helical. {ECO:0000255}.
TOPO_DOM 79 90 Extracellular. {ECO:0000255}.
TRANSMEM 91 111 Helical. {ECO:0000255}.
TOPO_DOM 112 135 Cytoplasmic. {ECO:0000255}.
TRANSMEM 136 156 Helical. {ECO:0000255}.
TOPO_DOM 157 171 Extracellular. {ECO:0000255}.
TRANSMEM 172 192 Helical. {ECO:0000255}.
TOPO_DOM 193 241 Cytoplasmic. {ECO:0000255}.
TRANSMEM 242 262 Helical. {ECO:0000255}.
TOPO_DOM 263 281 Extracellular. {ECO:0000255}.
TRANSMEM 282 302 Helical. {ECO:0000255}.
TOPO_DOM 303 382 Cytoplasmic. {ECO:0000255}.
CARBOHYD 3 3 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16407254}.
CARBOHYD 6 6 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16407254}.
MUTAGEN 3 3 N->Q: Increases sensitivity towards LCBs.
{ECO:0000269|PubMed:16407254}.
MUTAGEN 6 6 N->Q: Increases sensitivity towards LCBs.
{ECO:0000269|PubMed:16407254}.
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


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