ID   HTL1_YEAST              Reviewed;          78 AA.
AC   Q9URQ5; D6VR30;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=High temperature lethal protein 1;
DE   AltName: Full=Chromatin structure-remodeling complex protein HTL1;
GN   Name=HTL1; Synonyms=DRT1; OrderedLocusNames=YCR020W-B;
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].
RA   Davidov E., Jiang W., Bailey D.A.;
RT   "The DRT1 gene encodes a novel small ORF necessary for viability at 36
RT   degrees Celsius.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH RSC8.
RX   PubMed=12684875; DOI=10.1007/s00438-003-0835-1;
RA   Lu Y.-M., Lin Y.-R., Tsai A., Hsao Y.-S., Li C.-C., Cheng M.Y.;
RT   "Dissecting the pet18 mutation in Saccharomyces cerevisiae: HTL1 encodes a
RT   7-kDa polypeptide that interacts with components of the RSC complex.";
RL   Mol. Genet. Genomics 269:321-330(2003).
RN   [3]
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   [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   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   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE RSC COMPLEX.
RX   PubMed=12417720; DOI=10.1128/mcb.22.23.8165-8174.2002;
RA   Romeo M.J., Angus-Hill M.L., Sobering A.K., Kamada Y., Cairns B.R.,
RA   Levin D.E.;
RT   "HTL1 encodes a novel factor that interacts with the RSC chromatin
RT   remodeling complex in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 22:8165-8174(2002).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=11571756; DOI=10.1002/yea.778;
RA   Lanzuolo C., Ederle S., Pollice A., Russo F., Storlazzi A., Pulitzer J.F.;
RT   "The HTL1 gene (YCR020W-b) of Saccharomyces cerevisiae is necessary for
RT   growth at 37 degrees C, and for the conservation of chromosome stability
RT   and fertility.";
RL   Yeast 18:1317-1330(2001).
RN   [8]
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   [9]
RP   IDENTIFICATION IN THE RSC COMPLEX.
RX   PubMed=14729968; DOI=10.1128/mcb.24.3.1232-1244.2003;
RA   Baetz K.K., Krogan N.J., Emili A., Greenblatt J., Hieter P.;
RT   "The ctf13-30/CTF13 genomic haploinsufficiency modifier screen identifies
RT   the yeast chromatin remodeling complex RSC, which is required for the
RT   establishment of sister chromatid cohesion.";
RL   Mol. Cell. Biol. 24:1232-1244(2004).
RN   [10]
RP   FUNCTION, AND IDENTIFICATION IN THE RSC COMPLEX.
RX   PubMed=16204215; DOI=10.1534/genetics.105.047589;
RA   Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R.;
RT   "The RSC chromatin remodeling complex bears an essential fungal-specific
RT   protein module with broad functional roles.";
RL   Genetics 172:795-809(2006).
RN   [11]
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 cell cycle progression through G2/M transition
CC       at temperatures higher than 33 degrees Celsius. Component of the
CC       chromatin structure-remodeling complex (RSC), which is involved in
CC       transcription regulation and nucleosome positioning. RSC is responsible
CC       for the transfer of a histone octamer from a nucleosome core particle
CC       to naked DNA. The reaction requires ATP and involves an activated RSC-
CC       nucleosome intermediate. Remodeling reaction also involves DNA
CC       translocation, DNA twist and conformational change. As a reconfigurer
CC       of centromeric and flanking nucleosomes, RSC complex is required both
CC       for proper kinetochore function in chromosome segregation and, via a
CC       PKC1-dependent signaling pathway, for organization of the cellular
CC       cytoskeleton. When associated with the RSC complex, may act
CC       coordinately with PKC1 to regulate G2/M transition. Together with LDB7,
CC       NPL6, RSC3, RSC30 components, defines a fungal-specific module within
CC       the RSC complex that plays a role in many cellular functions including
CC       the maintenance of cell wall integrity. {ECO:0000269|PubMed:12417720,
CC       ECO:0000269|PubMed:12684875, ECO:0000269|PubMed:16204215}.
CC   -!- SUBUNIT: Interacts directly with RSC8. Component of the two forms of
CC       the RSC complex composed of at least either RSC1 or RSC2, and ARP7,
CC       ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1,
CC       STH1, HTL1 and probably RTT102. The complexes interact with histone and
CC       histone variant components of centromeric chromatin. Component of a
CC       fungal-specific module (HTL1-LDB7-NPL6-RSC3-RSC30) within the RSC
CC       complex. {ECO:0000269|PubMed:12417720, ECO:0000269|PubMed:12684875,
CC       ECO:0000269|PubMed:14729968, ECO:0000269|PubMed:16204215}.
CC   -!- INTERACTION:
CC       Q9URQ5; P43609: RSC8; NbExp=3; IntAct=EBI-8717, EBI-23005;
CC       Q9URQ5; P32597: STH1; NbExp=3; IntAct=EBI-8717, EBI-18410;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12417720}.
CC   -!- MISCELLANEOUS: Present with 3550 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; AF162267; AAD47275.1; -; Genomic_DNA.
DR   EMBL; X59720; CAC42974.1; -; Genomic_DNA.
DR   EMBL; AY558371; AAS56697.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07499.1; -; Genomic_DNA.
DR   PIR; S07696; S07696.
DR   RefSeq; NP_009949.1; NM_001184313.1.
DR   PDB; 6K15; EM; 3.40 A; E=1-78.
DR   PDB; 6KW3; EM; 7.13 A; E=1-78.
DR   PDB; 6KW4; EM; 7.55 A; E=1-78.
DR   PDB; 6KW5; EM; 10.13 A; E=1-78.
DR   PDB; 6TDA; EM; 15.00 A; Q=1-78.
DR   PDB; 6V8O; EM; 3.07 A; C=1-78.
DR   PDB; 6V92; EM; 20.00 A; C=1-78.
DR   PDBsum; 6K15; -.
DR   PDBsum; 6KW3; -.
DR   PDBsum; 6KW4; -.
DR   PDBsum; 6KW5; -.
DR   PDBsum; 6TDA; -.
DR   PDBsum; 6V8O; -.
DR   PDBsum; 6V92; -.
DR   AlphaFoldDB; Q9URQ5; -.
DR   SMR; Q9URQ5; -.
DR   BioGRID; 31003; 121.
DR   ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR   ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR   IntAct; Q9URQ5; 21.
DR   MINT; Q9URQ5; -.
DR   STRING; 4932.YCR020W-B; -.
DR   iPTMnet; Q9URQ5; -.
DR   MaxQB; Q9URQ5; -.
DR   PaxDb; Q9URQ5; -.
DR   PRIDE; Q9URQ5; -.
DR   EnsemblFungi; YCR020W-B_mRNA; YCR020W-B; YCR020W-B.
DR   GeneID; 850384; -.
DR   KEGG; sce:YCR020W-B; -.
DR   SGD; S000006439; HTL1.
DR   VEuPathDB; FungiDB:YCR020W-B; -.
DR   HOGENOM; CLU_195456_1_0_1; -.
DR   InParanoid; Q9URQ5; -.
DR   OMA; KTITAHQ; -.
DR   BioCyc; YEAST:G3O-29401-MON; -.
DR   PRO; PR:Q9URQ5; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; Q9URQ5; protein.
DR   GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016586; C:RSC-type complex; IDA:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IC:SGD.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IC:ComplexPortal.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IGI:UniProtKB.
DR   GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell cycle; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..78
FT                   /note="High temperature lethal protein 1"
FT                   /id="PRO_0000084085"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   HELIX           21..39
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           46..53
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           55..74
FT                   /evidence="ECO:0007829|PDB:6V8O"
SQ   SEQUENCE   78 AA;  9180 MW;  62308D5A1F6322C7 CRC64;
     MSQNNTISSM NPERAYNNVT LKNLTAFQLL SQRENICELL NLVESTERHN SIINPERQRM
     SLEEMKKMLD ALKNERKK