LSP1_YEAST
ID LSP1_YEAST Reviewed; 341 AA.
AC Q12230; D6W408;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Sphingolipid long chain base-responsive protein LSP1;
GN Name=LSP1; OrderedLocusNames=YPL004C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 PROTEIN SEQUENCE OF 36-43; 166-175; 197-207 AND 222-238, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, AND PHOSPHORYLATION BY PKH1 AND PHK2.
RX PubMed=15016821; DOI=10.1074/jbc.m400299200;
RA Zhang X., Lester R.L., Dickson R.C.;
RT "Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent
RT protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p
RT and Ypk1p.";
RL J. Biol. Chem. 279:22030-22038(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16496001; DOI=10.1038/nature04472;
RA Walther T.C., Brickner J.H., Aguilar P.S., Bernales S., Pantoja C.,
RA Walter P.;
RT "Eisosomes mark static sites of endocytosis.";
RL Nature 439:998-1003(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Together with PIL1, main component of eisosomes, structures
CC at the cell periphery underneath the plasma membrane that mark the site
CC of endocytosis. Negative regulator of cell wall integrity (CWI) in
CC unstressed cells, probably by inhibiting protein kinase PKH1/PHK2
CC activity and regulating their downstream CWI pathways PKC1-MAP kinase
CC pathway and protein kinase YPK1 pathway. Activity may be regulated by
CC the transient increase of sphingolipid long chain bases (LCBs) during
CC heat stress. {ECO:0000269|PubMed:15016821}.
CC -!- INTERACTION:
CC Q12230; P53252: PIL1; NbExp=6; IntAct=EBI-34978, EBI-23225;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16496001}.
CC Note=Localizes at eisosomes, structures which colocalize with sites of
CC protein and lipid endocytosis.
CC -!- PTM: Phosphorylated by PKH1 and PKH2. Phosphorylation is stimulated by
CC sphingolipid long chain bases (LCBs). {ECO:0000269|PubMed:15016821}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 104485 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; U33335; AAB68101.1; -; Genomic_DNA.
DR EMBL; Z48483; CAA88382.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95037.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11424.1; -; Genomic_DNA.
DR PIR; S52527; S52527.
DR RefSeq; NP_015321.1; NM_001183818.1.
DR PDB; 3PLT; X-ray; 2.90 A; A/B/C=36-267.
DR PDBsum; 3PLT; -.
DR AlphaFoldDB; Q12230; -.
DR SMR; Q12230; -.
DR BioGRID; 36173; 187.
DR DIP; DIP-3993N; -.
DR IntAct; Q12230; 56.
DR MINT; Q12230; -.
DR STRING; 4932.YPL004C; -.
DR TCDB; 8.A.148.1.1; the plasma membrane organizing center, eisosome (eisosome) family.
DR iPTMnet; Q12230; -.
DR MaxQB; Q12230; -.
DR PaxDb; Q12230; -.
DR PRIDE; Q12230; -.
DR TopDownProteomics; Q12230; -.
DR EnsemblFungi; YPL004C_mRNA; YPL004C; YPL004C.
DR GeneID; 856103; -.
DR KEGG; sce:YPL004C; -.
DR SGD; S000005925; LSP1.
DR VEuPathDB; FungiDB:YPL004C; -.
DR eggNOG; ENOG502QQ1T; Eukaryota.
DR GeneTree; ENSGT00940000176685; -.
DR HOGENOM; CLU_046464_0_0_1; -.
DR InParanoid; Q12230; -.
DR OMA; WGYDNDD; -.
DR BioCyc; YEAST:G3O-33923-MON; -.
DR EvolutionaryTrace; Q12230; -.
DR PRO; PR:Q12230; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12230; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0032126; C:eisosome; IDA:SGD.
DR GO; GO:0036286; C:eisosome filament; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0070941; P:eisosome assembly; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:SGD.
DR GO; GO:0009408; P:response to heat; IMP:SGD.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR028245; PIL1/LSP1.
DR PANTHER; PTHR31962; PTHR31962; 1.
DR Pfam; PF13805; Pil1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..341
FT /note="Sphingolipid long chain base-responsive protein
FT LSP1"
FT /id="PRO_0000084505"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:3PLT"
FT HELIX 56..91
FT /evidence="ECO:0007829|PDB:3PLT"
FT HELIX 95..159
FT /evidence="ECO:0007829|PDB:3PLT"
FT HELIX 165..224
FT /evidence="ECO:0007829|PDB:3PLT"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3PLT"
FT HELIX 244..260
FT /evidence="ECO:0007829|PDB:3PLT"
SQ SEQUENCE 341 AA; 38071 MW; 6FCEE022ECC9778C CRC64;
MHRTYSLRNQ RAPTAAELQA PPPPPSSTKS KFFGKASIAS SFRKNAAGNF GPELARKLSQ
LVKTEKGVLR AMEVVASERR EAAKQLSLWG ADNDDDVSDV TDKLGVLIYE LGELQDQFID
KYDQYRVTLK SIRNIEASVQ PSRDRKEKIT DEIAHLKYKD PQSTKIPVLE QELVRAEAES
LVAEAQLSNI TREKLKAAYS YMFDSLRELS EKFALIAGYG KALLELLDDS PVTPGEARPA
YDGYEASRQI IMDAESALES WTLDMAAVKP TLSFHQTVDD VYEDEDGEEE EEPEIQNGDI
PGQVVEEEEV EWTTEVPVDD EAHEADHHVS QNGHTSGSEN I
