EIS1_YEAST
ID EIS1_YEAST Reviewed; 843 AA.
AC Q05050; D6VZK5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Eisosome protein 1;
GN Name=EIS1; OrderedLocusNames=YMR031C; ORFNames=YM9973.04C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2 AND SER-584, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-584, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-584, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-710; THR-720;
RP SER-816 AND SER-838, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, ASSOCIATION WITH THE EISOSOME, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19269952; DOI=10.1074/mcp.m800397-mcp200;
RA Deng C., Xiong X., Krutchinsky A.N.;
RT "Unifying fluorescence microscopy and mass spectrometry for studying
RT protein complexes in cells.";
RL Mol. Cell. Proteomics 8:1413-1423(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-182; SER-401;
RP SER-584; THR-720; SER-763; SER-775; SER-828; SER-829 AND SER-838, AND
RP IDENTIFICATION BY 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).
RN [12]
RP SUBCELLULAR LOCATION, ASSOCIATION WITH THE EISOSOME, AND FUNCTION.
RX PubMed=20526336; DOI=10.1038/nsmb.1829;
RA Aguilar P.S., Frohlich F., Rehman M., Shales M., Ulitsky I.,
RA Olivera-Couto A., Braberg H., Shamir R., Walter P., Mann M., Ejsing C.S.,
RA Krogan N.J., Walther T.C.;
RT "A plasma-membrane E-MAP reveals links of the eisosome with sphingolipid
RT metabolism and endosomal trafficking.";
RL Nat. Struct. Mol. Biol. 17:901-908(2010).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for normal formation of eisosomes, large cytoplasmic
CC protein assemblies that localize to specialized domains on plasma
CC membrane and mark the site of endocytosis.
CC {ECO:0000269|PubMed:20526336}.
CC -!- INTERACTION:
CC Q05050; P53252: PIL1; NbExp=3; IntAct=EBI-28061, EBI-23225;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Cell membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Localizes at the eisosomes.
CC -!- MISCELLANEOUS: Present with 5570 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EIS1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z49213; CAA89146.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09929.1; -; Genomic_DNA.
DR PIR; S53947; S53947.
DR RefSeq; NP_013744.1; NM_001182527.1.
DR AlphaFoldDB; Q05050; -.
DR SMR; Q05050; -.
DR BioGRID; 35203; 125.
DR DIP; DIP-7982N; -.
DR IntAct; Q05050; 9.
DR MINT; Q05050; -.
DR STRING; 4932.YMR031C; -.
DR TCDB; 8.A.148.1.1; the plasma membrane organizing center, eisosome (eisosome) family.
DR iPTMnet; Q05050; -.
DR MaxQB; Q05050; -.
DR PaxDb; Q05050; -.
DR PRIDE; Q05050; -.
DR EnsemblFungi; YMR031C_mRNA; YMR031C; YMR031C.
DR GeneID; 855047; -.
DR KEGG; sce:YMR031C; -.
DR SGD; S000004633; EIS1.
DR VEuPathDB; FungiDB:YMR031C; -.
DR eggNOG; ENOG502S8WV; Eukaryota.
DR GeneTree; ENSGT00940000176658; -.
DR HOGENOM; CLU_013228_0_0_1; -.
DR InParanoid; Q05050; -.
DR OMA; EHTFSGF; -.
DR BioCyc; YEAST:G3O-32736-MON; -.
DR PRO; PR:Q05050; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q05050; 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:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0070941; P:eisosome assembly; IMP:SGD.
DR InterPro; IPR024527; Eisosome1.
DR PANTHER; PTHR28298; PTHR28298; 1.
DR Pfam; PF12757; Eisosome1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Membrane; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..843
FT /note="Eisosome protein 1"
FT /id="PRO_0000203273"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17761666"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 720
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 843 AA; 93345 MW; 0068D65A229B941D CRC64;
MSLISAVEDR DIHNIGKTSG GGSRTSSITS SKKSLKHGSK SLRKPKVYQT TGEPLSREAL
YKAKLKYGVY QSPAQSYSIG VSDAHAASDK AANLAHDNQT TVEAYKRMFI DPNATKAASK
MGPKVVRNNS ITSATSKTSK ESQTKRKSKE SPGAAASKAY SMTMETTSLS SQTNSRSYSI
TSASSVLSGA SGSFNSTVNP KPKTLNLEKV LVGAEKKAES RIKERWEPEK TNFQYGVKTD
EHGNLNQFSF SNEMMNNIMA KVDAPKAQDL QKVKKVSAEK EAKSMKFALG AANAVKDMHP
GEDIDKSIAL KAQKRETYLS QLTSQQVLTL ARANVDRQLD IIEKSDMHRK LFTNMEYNKA
AVAVAQSNHQ KKTEFHNKIN MGGGLFLSPE DITKIASGLI SPVLGEVSER AEAQRAMDEE
IAERTEAYNK SSNEWETMER SIISNDAKVL TTTANRHQTE KKTSQEKIKA SFDALVARMD
TKVAERETLL EDTKSKEIEF KKQMQQELKD EKARLDQDLE EWGKKCEQDI TEARKEQEEL
LKPYHDDLAN AEAEHKTLVE ERDEINAEIS RLQDAIVDHK RKISGYGNDL DAQKNRNIRE
DDKLLELGQT KESLESHLND DVIILANKAK EQAELSTKEA RLKQLEVDSL INERKSELNA
TEIELKKEKL NLLEAMKDVA SARGDDKIDE EKVKKLIGMT SEEYLTQNKS VEKNVEDLPT
QLEKIEEGDE LKKEEIVGAE TKNSGGDGVP VSTAAKEATE TSSAVQTKEP EEKISIGNKS
SGKEDANDCK SAEHSKEISV SQKAGNNKSL GVSPDSLEHT FSGFSQGSSI EDDQDAISNQ
EKK
