ID   ESL1_YEAST              Reviewed;        1118 AA.
AC   P40456; D6VVD6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=EST/SMG-like protein 1 {ECO:0000303|PubMed:23893744};
GN   Name=ESL1 {ECO:0000303|PubMed:23893744};
GN   OrderedLocusNames=YIL151C {ECO:0000312|SGD:S000001413};
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=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(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   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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-190, AND
RP   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   [5]
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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).
RN   [7]
RP   FUNCTION.
RX   PubMed=23893744; DOI=10.1534/g3.113.006924;
RA   Lai X., Beilharz T., Au W.C., Hammet A., Preiss T., Basrai M.A.,
RA   Heierhorst J.;
RT   "Yeast hEST1A/B (SMG5/6)-like proteins contribute to environment-sensing
RT   adaptive gene expression responses.";
RL   G3 (Bethesda) 3:1649-1659(2013).
CC   -!- FUNCTION: May be involved in the regulation of gene expression
CC       responses of environment-sensing pathways.
CC       {ECO:0000269|PubMed:23893744}.
CC   -!- MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z38059; CAA86127.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08402.1; -; Genomic_DNA.
DR   PIR; S48383; S48383.
DR   RefSeq; NP_012115.1; NM_001179499.1.
DR   AlphaFoldDB; P40456; -.
DR   SMR; P40456; -.
DR   BioGRID; 34841; 81.
DR   DIP; DIP-1904N; -.
DR   IntAct; P40456; 6.
DR   MINT; P40456; -.
DR   STRING; 4932.YIL151C; -.
DR   iPTMnet; P40456; -.
DR   MaxQB; P40456; -.
DR   PaxDb; 4932-YIL151C; -.
DR   PeptideAtlas; P40456; -.
DR   EnsemblFungi; YIL151C_mRNA; YIL151C; YIL151C.
DR   GeneID; 854655; -.
DR   KEGG; sce:YIL151C; -.
DR   AGR; SGD:S000001413; -.
DR   SGD; S000001413; ESL1.
DR   VEuPathDB; FungiDB:YIL151C; -.
DR   eggNOG; ENOG502QQKF; Eukaryota.
DR   GeneTree; ENSGT00940000176784; -.
DR   HOGENOM; CLU_006407_0_0_1; -.
DR   InParanoid; P40456; -.
DR   OMA; YHIATVQ; -.
DR   OrthoDB; 2516823at2759; -.
DR   BioCyc; YEAST:G3O-31400-MONOMER; -.
DR   Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 854655; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P40456; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40456; Protein.
DR   GO; GO:0005697; C:telomerase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0070034; F:telomerase RNA binding; IBA:GO_Central.
DR   GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   InterPro; IPR045153; Est1/Ebs1-like.
DR   InterPro; IPR002716; PIN_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR15696:SF39; EST_SMG-LIKE PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR15696; SMG-7 SUPPRESSOR WITH MORPHOLOGICAL EFFECT ON GENITALIA PROTEIN 7; 1.
DR   Pfam; PF13638; PIN_4; 1.
DR   SMART; SM00670; PINc; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..1118
FT                   /note="EST/SMG-like protein 1"
FT                   /id="PRO_0000202957"
FT   DOMAIN          947..1087
FT                   /note="PINc"
FT                   /evidence="ECO:0000255"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   1118 AA;  128735 MW;  4F80F3A5E95C6CC3 CRC64;
     MVDLMVPAND DPSNETDYSR SNNNHTHIVS DMRPTSAAFL HQKRHSSSSH NDTPESSFAK
     RRVPGIVDPV GKGFIDGITN SQISAQNTPS KTDDASRRPS ISRKVMESTP QVKTSSIPTM
     DVPKSPYYVN RTMLARNMKV VSRDTYEDNA NPQMRADEPL VASNGIYSNS QPQSQVTLSD
     IRRAPVVAAS PPPMIRQLPS AQPNQTFIKK LQEIYKIIVV QETELQQRCL YLTTSQTTEL
     KSLWAIYRLN TELIKNYINF IITALLTTQP INDLIMGQEI LDIYRIEKRL WVYGIITFLD
     VLKNFSNFMD PEVCCQFIIY AFISVSNMLE DIPLKYSILW RQRLGDLSRM AISLYPSGFI
     DWRLSAEYWY TESMKYIYGC GKLYYHIATV QQNSLEAFVN LGKSVFCQDP FTPSQQTLQL
     LIENIYQSAF IDRSSGSANN NEIAHRNSQL IDYLKHTEVM LLPSFLENMD LQHVVLMYFK
     DKFGKDFNGN DVFDTKDMFC QNPESLRYYF RHAPAFAESQ LLQLIGFGNP KNPFALLFQL
     PKYLKLKKDK REKKRSEATE TSSYTDPFDV QISSESYFQN IDALNSSFND IPTNLNIWLD
     SLNHINMTSI QCSIHVLTKF LHAPLVVALP HFLTWLHFIV AILKKLEMVN SKQVVAFWIH
     FLRRTMPWNS IVTLGNVLVC YMLDNLHPFL KKELEKFYSL ELDDLIEYYN ENENLPEIWK
     CWGTLWFDAI KKCDVMEIPG VQDHLFFDSP LDGIVFDEKD EVGEKFWMRS VRAVLLLKGI
     AKKFPDLGLK VSFQASVFCR RNDIPPDYFL KNLTFKLDAY DEDNYNDNNE LDDLYDTIEI
     NEEIEAVNMD PQATPNLSVV SGESIFEYTG YTRLAPDYHC FDKNGGFNSA FIYSQWSNVG
     NGVTLDVSGE SIYDVANNNL SLHWEKIFFD KIAAASKGSD ENYNCTLYFV IDATSWLRHF
     AHIFKLAKNN TLKFAICLTT FQELRYLRGS KDDTVVEAAT RSVITIRQLY DEKKIIPMRF
     TGNIATHVEE NLEFEEQITW KTHVDEFVID AIAKLNQRFQ AERLTDENKN KGKEFAVLVT
     DDDNMNQKAK DRMIKTCNTK YLFSLGSKLG INSGLCTN
//