LRS4_YEAST
ID LRS4_YEAST Reviewed; 347 AA.
AC Q04087; D6VT66;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Monopolin complex subunit LRS4;
DE AltName: Full=Loss of rDNA silencing protein 4;
GN Name=LRS4; OrderedLocusNames=YDR439W; ORFNames=D9461.25;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION.
RX PubMed=10082585; DOI=10.1128/mcb.19.4.3184;
RA Smith J.S., Caputo E., Boeke J.D.;
RT "A genetic screen for ribosomal DNA silencing defects identifies multiple
RT DNA replication and chromatin-modulating factors.";
RL Mol. Cell. Biol. 19:3184-3197(1999).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE MONOPOLIN
RP COMPLEX.
RX PubMed=12689592; DOI=10.1016/s1534-5807(03)00086-8;
RA Rabitsch K.P., Petronczki M., Javerzat J.-P., Genier S., Chwalla B.,
RA Schleiffer A., Tanaka T.U., Nasmyth K.;
RT "Kinetochore recruitment of two nucleolar proteins is required for homolog
RT segregation in meiosis I.";
RL Dev. Cell 4:535-548(2003).
RN [5]
RP FUNCTION.
RX PubMed=12586695; DOI=10.1093/genetics/163.1.47;
RA Enyenihi A.H., Saunders W.S.;
RT "Large-scale functional genomic analysis of sporulation and meiosis in
RT Saccharomyces cerevisiae.";
RL Genetics 163:47-54(2003).
RN [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12717442; DOI=10.1038/ncb977;
RA Clyne R.K., Katis V.L., Jessop L., Benjamin K.R., Herskowitz I.,
RA Lichten M., Nasmyth K.;
RT "Polo-like kinase Cdc5 promotes chiasmata formation and cosegregation of
RT sister centromeres at meiosis I.";
RL Nat. Cell Biol. 5:480-485(2003).
RN [9]
RP SUBCELLULAR LOCATION, AND ASSOCIATION TO THE KINETOCHORE.
RX PubMed=15620644; DOI=10.1016/j.cub.2004.12.033;
RA Lee B.H., Kiburz B.M., Amon A.;
RT "Spo13 maintains centromeric cohesion and kinetochore coorientation during
RT meiosis I.";
RL Curr. Biol. 14:2168-2182(2004).
RN [10]
RP PHOSPHORYLATION.
RX PubMed=15620645; DOI=10.1016/j.cub.2004.12.020;
RA Katis V.L., Matos J., Mori S., Shirahige K., Zachariae W., Nasmyth K.;
RT "Spo13 facilitates monopolin recruitment to kinetochores and regulates
RT maintenance of centromeric cohesion during yeast meiosis.";
RL Curr. Biol. 14:2183-2196(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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: Component of the monopolin complex which promotes
CC monoorientation during meiosis I, required for chromosome segregation
CC during meiosis. Involved in rDNA silencing.
CC {ECO:0000269|PubMed:10082585, ECO:0000269|PubMed:12586695,
CC ECO:0000269|PubMed:12689592}.
CC -!- SUBUNIT: Component of the monopolin complex composed of at least CSM1,
CC LRS4 and MAM1. The complex associates with the kinetochore.
CC {ECO:0000269|PubMed:12689592}.
CC -!- INTERACTION:
CC Q04087; P32562: CDC5; NbExp=6; IntAct=EBI-32189, EBI-4440;
CC Q04087; P06243: CDC7; NbExp=5; IntAct=EBI-32189, EBI-4451;
CC Q04087; P25651: CSM1; NbExp=16; IntAct=EBI-32189, EBI-22001;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome, centromere.
CC Note=Transiently released from the nucleolus and localized to the
CC centromere regions during late pachytene. This relocation is CDC5
CC dependent.
CC -!- PTM: Phosphorylated by CDC5. This phosphorylation is required for the
CC location to the kinetochores during late pachytene.
CC {ECO:0000269|PubMed:15620645}.
CC -!- MISCELLANEOUS: Present with 1390 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U33007; AAB64867.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12276.1; -; Genomic_DNA.
DR PIR; S69719; S69719.
DR RefSeq; NP_010727.1; NM_001180747.1.
DR PDB; 3N7N; X-ray; 3.90 A; E/F=1-102.
DR PDBsum; 3N7N; -.
DR AlphaFoldDB; Q04087; -.
DR SMR; Q04087; -.
DR BioGRID; 32495; 452.
DR ComplexPortal; CPX-1681; Monopolin complex.
DR DIP; DIP-1416N; -.
DR IntAct; Q04087; 14.
DR MINT; Q04087; -.
DR STRING; 4932.YDR439W; -.
DR CarbonylDB; Q04087; -.
DR iPTMnet; Q04087; -.
DR MaxQB; Q04087; -.
DR PaxDb; Q04087; -.
DR PRIDE; Q04087; -.
DR EnsemblFungi; YDR439W_mRNA; YDR439W; YDR439W.
DR GeneID; 852049; -.
DR KEGG; sce:YDR439W; -.
DR SGD; S000002847; LRS4.
DR VEuPathDB; FungiDB:YDR439W; -.
DR HOGENOM; CLU_799749_0_0_1; -.
DR InParanoid; Q04087; -.
DR OMA; YESVIEC; -.
DR BioCyc; YEAST:G3O-29973-MON; -.
DR EvolutionaryTrace; Q04087; -.
DR PRO; PR:Q04087; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04087; protein.
DR GO; GO:0033551; C:monopolin complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0045143; P:homologous chromosome segregation; IMP:SGD.
DR GO; GO:0045132; P:meiotic chromosome segregation; IC:ComplexPortal.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IGI:SGD.
DR GO; GO:0034503; P:protein localization to nucleolar rDNA repeats; IMP:SGD.
DR GO; GO:0070550; P:rDNA chromatin condensation; IMP:SGD.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IDA:SGD.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD.
DR InterPro; IPR018479; Lrs4/Mde4.
DR Pfam; PF10422; LRS4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Centromere; Chromosome; Coiled coil; Meiosis;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..347
FT /note="Monopolin complex subunit LRS4"
FT /id="PRO_0000257808"
FT REGION 112..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 46..118
FT /evidence="ECO:0000255"
FT COMPBIAS 112..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 347 AA; 39354 MW; 60D880BA947B9005 CRC64;
MTTLLQLLSN YYKAKLDSER IYNEYVQSQY EFASLDKLNN NKGDPKKVVD ETLFLQRQIA
QLNKQLQLSF QENEKLLSVQ KNQKALYQSK LSSKDAFIDD LKLKLKVEQI SVDKHNKERT
PSTGRDEQQR NSKAAHTSKP TIHLLSPIVN RDKPNNQTND RGGNDPDSPT SQRRSRGLRS
LLSSGKNTIF DSISKNLDDE INENAHIRND TTSSKIAGKS PSRLSALQKS PELRKERNNM
ILKEHILRSK DDQNITSSRK LDNIELSSIG DSTAMTSRSS TVNANDILGN EENDGITKLK
RVNKLTSSPV KRDCSTNKKR KLTKQRIATL PNSDEELSNN LNVDEFV
