PIL1_YEAST
ID PIL1_YEAST Reviewed; 339 AA.
AC P53252; D6VUL8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Sphingolipid long chain base-responsive protein PIL1;
GN Name=PIL1; OrderedLocusNames=YGR086C;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 45-56; 85-103; 166-192 AND 197-221, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND THR-233, AND
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-230 AND THR-233, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-16; SER-45; SER-98;
RP SER-163; THR-233 AND SER-299, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Negative regulator of cell wall integrity (CWI) in unstressed
CC cells, probably by inhibiting protein kinase PKH1/PHK2 activity and
CC regulating their downstream CWI pathways PKC1-MAP kinase pathway and
CC protein kinase YPK1 pathway. Activity may be regulated by the transient
CC increase of sphingolipid long chain bases (LCBs) during heat stress.
CC {ECO:0000269|PubMed:15016821}.
CC -!- INTERACTION:
CC P53252; Q05050: EIS1; NbExp=3; IntAct=EBI-23225, EBI-28061;
CC P53252; Q12230: LSP1; NbExp=6; IntAct=EBI-23225, EBI-34978;
CC P53252; P35719: MRP8; NbExp=3; IntAct=EBI-23225, EBI-16255;
CC P53252; Q03407: PKH1; NbExp=4; IntAct=EBI-23225, EBI-32467;
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated by PKH1 and PKH2. Phosphorylation is inhibited by
CC sphingolipid long chain bases (LCBs). {ECO:0000269|PubMed:15016821}.
CC -!- MISCELLANEOUS: Present with 2157 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z72871; CAA97088.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08179.1; -; Genomic_DNA.
DR PIR; S64381; S64381.
DR RefSeq; NP_011600.3; NM_001181215.3.
DR AlphaFoldDB; P53252; -.
DR SMR; P53252; -.
DR BioGRID; 33328; 294.
DR DIP; DIP-4618N; -.
DR IntAct; P53252; 45.
DR MINT; P53252; -.
DR STRING; 4932.YGR086C; -.
DR TCDB; 8.A.148.1.1; the plasma membrane organizing center, eisosome (eisosome) family.
DR iPTMnet; P53252; -.
DR MaxQB; P53252; -.
DR PaxDb; P53252; -.
DR PRIDE; P53252; -.
DR EnsemblFungi; YGR086C_mRNA; YGR086C; YGR086C.
DR GeneID; 852977; -.
DR KEGG; sce:YGR086C; -.
DR SGD; S000003318; PIL1.
DR VEuPathDB; FungiDB:YGR086C; -.
DR eggNOG; ENOG502QQ1T; Eukaryota.
DR GeneTree; ENSGT00940000176685; -.
DR HOGENOM; CLU_046464_0_0_1; -.
DR InParanoid; P53252; -.
DR OMA; WGEGCDD; -.
DR BioCyc; YEAST:G3O-30798-MON; -.
DR PRO; PR:P53252; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53252; 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:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
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; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:0097446; P:protein localization to eisosome filament; 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 Direct protein sequencing; Isopeptide bond; Lipid droplet; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..339
FT /note="Sphingolipid long chain base-responsive protein
FT PIL1"
FT /id="PRO_0000058441"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:17761666,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 339 AA; 38349 MW; C86AE5ABB508EA03 CRC64;
MHRTYSLRNS RAPTASQLQN PPPPPSTTKG RFFGKGGLAY SFRRSAAGAF GPELSRKLSQ
LVKIEKNVLR SMELTANERR DAAKQLSIWG LENDDDVSDI TDKLGVLIYE VSELDDQFID
RYDQYRLTLK SIRDIEGSVQ PSRDRKDKIT DKIAYLKYKD PQSPKIEVLE QELVRAEAES
LVAEAQLSNI TRSKLRAAFN YQFDSIIEHS EKIALIAGYG KALLELLDDS PVTPGETRPA
YDGYEASKQI IIDAESALNE WTLDSAQVKP TLSFKQDYED FEPEEGEEEE EEDGQGRWSE
DEQEDGQIEE PEQEEEGAVE EHEQVGHQQS ESLPQQTTA
