SEG1_YEAST
ID SEG1_YEAST Reviewed; 960 AA.
AC Q04279; D6VZQ9; Q6B304;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Eisosome protein SEG1;
DE AltName: Full=Stability of eisosomes guaranteed protein 1;
GN Name=SEG1; OrderedLocusNames=YMR086W; ORFNames=YM9582.10;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11914276; DOI=10.1101/gad.970902;
RA Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA Gerstein M., Roeder G.S., Snyder M.;
RT "Subcellular localization of the yeast proteome.";
RL Genes Dev. 16:707-719(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352; SER-816 AND SER-818, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-235; SER-238; THR-675
RP AND SER-758, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352; SER-461; SER-816 AND
RP SER-818, AND 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-319; SER-339;
RP SER-352; SER-434; SER-461; THR-467; SER-630; THR-675; SER-816; SER-818 AND
RP SER-855, AND 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 [10]
RP GENE NAME.
RX PubMed=22368779; DOI=10.3390/membranes1040394;
RA Douglas L.M., Wang H.X., Li L., Konopka J.B.;
RT "Membrane compartment occupied by Can1 (MCC) and eisosome subdomains of the
RT fungal plasma membrane.";
RL Membranes 1:394-411(2011).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=22869600; DOI=10.1083/jcb.201202097;
RA Moreira K.E., Schuck S., Schrul B., Frohlich F., Moseley J.B.,
RA Walther T.C., Walter P.;
RT "Seg1 controls eisosome assembly and shape.";
RL J. Cell Biol. 198:405-420(2012).
CC -!- FUNCTION: Important for the biogenesis of eisosomes, large cytoplasmic
CC protein assemblies that localize to specialized domains on the plasma
CC membrane to cluster specific proteins at sites of membrane
CC invaginations. Required for efficient incorporation of the eisosome
CC component PIL1 into eisosomes. {ECO:0000269|PubMed:22869600}.
CC -!- SUBUNIT: Component of eisosomes, large cytoplasmic protein assemblies
CC that localize to specialized domains termed MCCs on the plasma
CC membrane. {ECO:0000269|PubMed:22869600}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11914276,
CC ECO:0000269|PubMed:19269952, ECO:0000269|PubMed:22869600}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11914276,
CC ECO:0000269|PubMed:19269952, ECO:0000269|PubMed:22869600}; Cytoplasmic
CC side {ECO:0000269|PubMed:11914276, ECO:0000269|PubMed:19269952,
CC ECO:0000269|PubMed:22869600}. Note=Localizes to eisosomes.
CC -!- SIMILARITY: Belongs to the SEG1 family. {ECO:0000305}.
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DR EMBL; Z49259; CAA89232.1; -; Genomic_DNA.
DR EMBL; AY692576; AAT92595.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09983.1; -; Genomic_DNA.
DR PIR; S54461; S54461.
DR RefSeq; NP_013803.1; NM_001182586.1.
DR AlphaFoldDB; Q04279; -.
DR SMR; Q04279; -.
DR BioGRID; 35261; 71.
DR DIP; DIP-6346N; -.
DR IntAct; Q04279; 5.
DR MINT; Q04279; -.
DR STRING; 4932.YMR086W; -.
DR TCDB; 8.A.148.1.1; the plasma membrane organizing center, eisosome (eisosome) family.
DR CarbonylDB; Q04279; -.
DR iPTMnet; Q04279; -.
DR MaxQB; Q04279; -.
DR PaxDb; Q04279; -.
DR PRIDE; Q04279; -.
DR EnsemblFungi; YMR086W_mRNA; YMR086W; YMR086W.
DR GeneID; 855110; -.
DR KEGG; sce:YMR086W; -.
DR SGD; S000004692; SEG1.
DR VEuPathDB; FungiDB:YMR086W; -.
DR eggNOG; ENOG502S0GH; Eukaryota.
DR HOGENOM; CLU_018639_0_0_1; -.
DR InParanoid; Q04279; -.
DR OMA; RFNDSDE; -.
DR BioCyc; YEAST:G3O-32786-MON; -.
DR PRO; PR:Q04279; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04279; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070941; P:eisosome assembly; IMP:SGD.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..960
FT /note="Eisosome protein SEG1"
FT /id="PRO_0000203284"
FT REGION 30..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 467
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 675
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 167
FT /note="G -> E (in Ref. 3; AAT92595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 960 AA; 105874 MW; 05A4FA27129DB09B CRC64;
MFRRRTTAPE MEQADPTAVA AAASIGKLLM KKGNQSDNEQ RPTYRSASMT NLRKPSAPKR
MSSISSISSE SRRSDGKGRP GKINSLTQRS SMGKGDSLNS PLTKEPQHKT RSHNRTSSLP
NQRGQQSRNS SGLQRQKSKT HQRISYDEAQ RTFKDFGGPQ ARGILTGQHR TENPSGSIPL
RTTRKYIPGP NGLVAIEVPV EKPSNANTSK LLRRSNSAHS ALNARNGSLL RKKVSQESLH
SQPKKTSSLG NTSSTQAKKG QKAVQERNLA KKHPINSNVP LIETQVREET DQELKLDNSN
SSESETVVNS ENNLEKPSSL NIEKDDLSKL IHENIELESF IEEKGKEKPL NSDQEDVFIS
EKTVKGDVQW PKNNRQASTL EKTFNYDNEE KREGNKPVAE HPLPEAEVDD KSVEQLNNIS
SSGSYSAQGS VENSKPENGN KNLENDTTSS PTQDLDEKSR SIEEKDTLEG TESSKKVEKP
DNCCEKISGA NTSSKKGNVG DTKDEFFDTV EESDQKTSKS NSSKNTDHSN QTEPTPSLAQ
YLRTSNTYLS RKNQSKQAEQ EKFHKPEAPM VPVTKVVTPI KSALKKSSGS SNHDSSMYSD
NSPANGAYLS LTTAENTRLN AQMTMSDSVS RRASLKRSSI KRPQSVGQFR SIRSNSPSPP
EKINNKRHSA IPLGTPEKGK PKRNSVMASL SKNSQQIQEP ASVYESNGPN KPKNQINKNI
KRGSQIAQNN KPSTKDMNSI LYPKEPPPRK SSFEKTRSNE SHLGFKKLSL RNGNFEEALS
ESYNGQASQN STNVNRTDTA QEFFKYLGHS SRFADSDSED ESQFFNQGPS KYNTETEGNK
TSGNKNSNGG NGAFSLFKSK SKQKENNVVS PGVSSPNHTT TDPAITSKKV DKKFSGLSLR
AASEAEPAKN SNPSMTNRLR FSSNPENGES RLPQAQEVSV TKEKKGSFGK KLKKIFGRKK
