LRE1_YEAST
ID LRE1_YEAST Reviewed; 583 AA.
AC P25579; D6VQW5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Laminarase-resistance protein LRE1;
GN Name=LRE1; OrderedLocusNames=YCL051W; ORFNames=YCL51W;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=11580836; DOI=10.1046/j.1365-2958.2001.02590.x;
RA Versele M., Thevelein J.M.;
RT "Lre1 affects chitinase expression, trehalose accumulation and heat
RT resistance through inhibition of the Cbk1 protein kinase in Saccharomyces
RT cerevisiae.";
RL Mol. Microbiol. 41:1311-1326(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
RP SEQUENCE REVISION TO 511; 554 AND C-TERMINUS.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP CHARACTERIZATION.
RX PubMed=9090049;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<199::aid-yea76>3.0.co;2-z;
RA Lai M.H., Silverman S.J., Gaughran J.P., Kirsch D.R.;
RT "Multiple copies of PBS2, MHP1 or LRE1 produce glucanase resistance and
RT other cell wall effects in Saccharomyces cerevisiae.";
RL Yeast 13:199-213(1997).
RN [6]
RP FUNCTION.
RX PubMed=11532139; DOI=10.1046/j.1365-2958.2001.02549.x;
RA Alonso-Monge R., Real E., Wojda I., Bebelman J.-P., Mager W.H.,
RA Siderius M.;
RT "Hyperosmotic stress response and regulation of cell wall integrity in
RT Saccharomyces cerevisiae share common functional aspects.";
RL Mol. Microbiol. 41:717-730(2001).
RN [7]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-398 AND SER-552, 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).
CC -!- FUNCTION: Overexpression affects chitinase expression, cell separation
CC and budding pattern, and increases trehalose accumulation and heat
CC resistance by inhibiting protein kinase CBK1. Overexpression also
CC suppresses temperature-induced hyperosmosensitivity and sensitivity to
CC cell wall degrading enzymes. Overexpression of both LRE1 and PBN1
CC confers resistance to laminarinase. {ECO:0000269|PubMed:11532139,
CC ECO:0000269|PubMed:11580836}.
CC -!- PTM: Phosphorylated by CDC28/CDK1. {ECO:0000269|PubMed:14574415}.
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DR EMBL; X59720; CAA42393.2; -; Genomic_DNA.
DR EMBL; BK006937; DAA07434.1; -; Genomic_DNA.
DR PIR; S19381; S19381.
DR RefSeq; NP_009879.2; NM_001178696.1.
DR AlphaFoldDB; P25579; -.
DR BioGRID; 30934; 80.
DR DIP; DIP-3880N; -.
DR IntAct; P25579; 4.
DR MINT; P25579; -.
DR STRING; 4932.YCL051W; -.
DR iPTMnet; P25579; -.
DR MaxQB; P25579; -.
DR PaxDb; P25579; -.
DR PRIDE; P25579; -.
DR EnsemblFungi; YCL051W_mRNA; YCL051W; YCL051W.
DR GeneID; 850306; -.
DR KEGG; sce:YCL051W; -.
DR SGD; S000000556; LRE1.
DR VEuPathDB; FungiDB:YCL051W; -.
DR eggNOG; ENOG502RXFV; Eukaryota.
DR GeneTree; ENSGT00940000176546; -.
DR HOGENOM; CLU_026385_0_0_1; -.
DR InParanoid; P25579; -.
DR OMA; NINAQSM; -.
DR BioCyc; YEAST:G3O-29305-MON; -.
DR PRO; PR:P25579; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25579; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:SGD.
PE 1: Evidence at protein level;
KW Phosphoprotein; Protein kinase inhibitor; Reference proteome.
FT CHAIN 1..583
FT /note="Laminarase-resistance protein LRE1"
FT /id="PRO_0000084482"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 583 AA; 64792 MW; AD851526EEEC7D8F CRC64;
MPNTHTQHVQ ISEPNPVNTL STPSKRGHRH RRSLAISGDF DFLKQPAAIV NLPPPQAAEN
CPSTAPTAVS STLSPIRYNR FPCKTNEDAG TLDLPEPRFY PLSPKNNLQT PSPRFFISEE
PSFSSPVKGV PDAIINLDDA LKTRPRSFKS HRRSESAPPD LEVMVDKGNC AAGSNSMIKE
EEDSLIEPES KNEYYEQKLP TALLSPLRPS LCVSEQAIDV DDSALNGSPT HHNHGMQNAN
ARNSNTFNSL KIKGQKQRYY HYTKQLPLTV GCDSQSPKEQ RSAASMTINQ AMTPSSLAYT
PSKLASTPAT PVSFYDSNAD INLESDNFPL KDNPRYAKDG YPKKCGNSQL NRVLDSDKRQ
DFSGESRRRR SGSPISHMQH RNLIDNMKGR RNSNTINSIF NYKSQHYEMP YDDMMKNENI
NAQSMPFSVN GVNNENSIGG VITRADDAPL QHSVVKSCTP DGKEEMNRLK SNDSNEYSKS
EGQIRTNSQL SKDILMGEPG DMVDLSSFVN AQRKASNETG DLVFSLSQDD DALKTFHASN
SAATSNESWC ISDDALGKQA QDSEVRRKRK SKLGLFRHIF SRK
