ID   EBS1_YEAST              Reviewed;         884 AA.
AC   Q03466; D6VSI7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Nonsense-mediated mRNA decay factor EBS1 {ECO:0000305};
DE   AltName: Full=EST1-like BCY1 suppressor 1 {ECO:0000303|PubMed:10688642};
GN   Name=EBS1 {ECO:0000303|PubMed:10688642};
GN   OrderedLocusNames=YDR206W {ECO:0000312|SGD:S000002614};
GN   ORFNames=YD8142.03;
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=10688642; DOI=10.1128/mcb.20.6.1947-1955.2000;
RA   Zhou J., Hidaka K., Futcher B.;
RT   "The Est1 subunit of yeast telomerase binds the Tlc1 telomerase RNA.";
RL   Mol. Cell. Biol. 20:1947-1955(2000).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH CDC33.
RX   PubMed=16467471; DOI=10.1128/ec.5.2.301-312.2006;
RA   Ford A.S., Guan Q., Neeno-Eckwall E., Culbertson M.R.;
RT   "Ebs1p, a negative regulator of gene expression controlled by the Upf
RT   proteins in the yeast Saccharomyces cerevisiae.";
RL   Eukaryot. Cell 5:301-312(2006).
RN   [5]
RP   FUNCTION, INTERACTION WITH UPF1, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17984081; DOI=10.1093/nar/gkm912;
RA   Luke B., Azzalin C.M., Hug N., Deplazes A., Peter M., Lingner J.;
RT   "Saccharomyces cerevisiae Ebs1p is a putative ortholog of human Smg7 and
RT   promotes nonsense-mediated mRNA decay.";
RL   Nucleic Acids Res. 35:7688-7697(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=29897761; DOI=10.1021/acs.jproteome.8b00032;
RA   He C., Jia C., Zhang Y., Xu P.;
RT   "Enrichment-based proteogenomics identifies microproteins, missing
RT   proteins, and novel smORFs in Saccharomyces cerevisiae.";
RL   J. Proteome Res. 17:2335-2344(2018).
CC   -!- FUNCTION: Plays a role in nonsense-mediated mRNA decay (NMD)
CC       (PubMed:16467471, PubMed:17984081). Recruits UPF1 to cytoplasmic mRNA
CC       decay bodies (P-bodies) (PubMed:17984081). Negative regulator of gene
CC       expression. Inhibits translation most likely through effects on eIF-4E
CC       (CDC33) (PubMed:16467471). Involved in telomere maintenance
CC       (PubMed:10688642). {ECO:0000269|PubMed:10688642,
CC       ECO:0000269|PubMed:16467471, ECO:0000269|PubMed:17984081}.
CC   -!- SUBUNIT: Interacts with NMD helicase UPF1 (PubMed:17984081). Interacts
CC       with CDC33 (PubMed:16467471). {ECO:0000269|PubMed:16467471,
CC       ECO:0000269|PubMed:17984081}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
CC       {ECO:0000305}. Cytoplasm, P-body {ECO:0000269|PubMed:17984081}.
CC   -!- DISRUPTION PHENOTYPE: Results in stabilization of NMD targets.
CC       {ECO:0000269|PubMed:17984081}.
CC   -!- SIMILARITY: Belongs to the EST1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z68194; CAA92345.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12047.1; -; Genomic_DNA.
DR   PIR; S61569; S61569.
DR   RefSeq; NP_010492.3; NM_001180514.3.
DR   AlphaFoldDB; Q03466; -.
DR   SMR; Q03466; -.
DR   BioGRID; 32256; 106.
DR   DIP; DIP-1297N; -.
DR   IntAct; Q03466; 15.
DR   MINT; Q03466; -.
DR   STRING; 4932.YDR206W; -.
DR   iPTMnet; Q03466; -.
DR   MaxQB; Q03466; -.
DR   PaxDb; 4932-YDR206W; -.
DR   PeptideAtlas; Q03466; -.
DR   EnsemblFungi; YDR206W_mRNA; YDR206W; YDR206W.
DR   GeneID; 851787; -.
DR   KEGG; sce:YDR206W; -.
DR   AGR; SGD:S000002614; -.
DR   SGD; S000002614; EBS1.
DR   VEuPathDB; FungiDB:YDR206W; -.
DR   eggNOG; KOG2162; Eukaryota.
DR   GeneTree; ENSGT00940000176623; -.
DR   HOGENOM; CLU_010068_0_0_1; -.
DR   InParanoid; Q03466; -.
DR   OMA; EIIEYYF; -.
DR   OrthoDB; 1978355at2759; -.
DR   BioCyc; YEAST:G3O-29790-MONOMER; -.
DR   Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 851787; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q03466; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q03466; Protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0000932; C:P-body; IDA:SGD.
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:0006310; P:DNA recombination; IMP:SGD.
DR   GO; GO:0017148; P:negative regulation of translation; IMP:SGD.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:SGD.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR018834; DNA/RNA-bd_Est1-type.
DR   InterPro; IPR019458; Est1-like_N.
DR   InterPro; IPR045153; Est1/Ebs1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR15696:SF0; PINC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR15696; SMG-7 SUPPRESSOR WITH MORPHOLOGICAL EFFECT ON GENITALIA PROTEIN 7; 1.
DR   Pfam; PF10374; EST1; 1.
DR   Pfam; PF10373; EST1_DNA_bind; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Cytoplasm; Nonsense-mediated mRNA decay; Nucleus;
KW   Reference proteome; Telomere.
FT   CHAIN           1..884
FT                   /note="Nonsense-mediated mRNA decay factor EBS1"
FT                   /id="PRO_0000086907"
FT   REGION          596..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          755..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..645
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   884 AA;  100000 MW;  14482D64E32A1860 CRC64;
     MEPSNTQKED LPTAFNGIKS QLNSILKSNQ LFQDYALLNG FLAFVHSKLN AAILTSIESQ
     CGKSFAADLD SFDQSSISSI LDFSWESVHY PIFKWFQMWR NYILFEKENK KQQTKFIDFR
     KMNSKMLKFF KTVQNFYVNV INTVYKKYDI SVLLPKRIIQ DLKLSDIENT TNVGDILAVK
     TFNSSSPLAH LIPTLFHRCL LFLGTAYRYK TLLEEISNKY SISNFKKSLD FFRLASLVLP
     SAGETYSQAG AIFLQTGNLG IAVFNFVKGM MTKMPSPVSI KNFGALMVDN KSSLNRSLHT
     TIMNTYLQES KGPRTPAKEI LEFYFLGLFG SVWSPTSWRD DTKPNQLNNG IKLRHLENAL
     YETMSARYLN NIKTIFHNLI ITIGGFHLLL KRRSDVSAKT LKDLRSNELD YLNFAFKYIA
     HILNDIVKES WSENPEVSEI LGMVRIINCW IKANPMVLQY SQSNLEFVNA LAYLINDIVK
     KKPSPSFSIT EHIPKRTYWF EEDLMVKGLS FVNFQLSDFD DYEKILEMDH SLDRLIGNPP
     LCDKLSASSE MLLRLQAVVN ISSQLLQNNN CGVEWSDNKS RYIFNKKIGF KETVKNSMKT
     SKQSNEKAKL QRKNKPSTTN GSISMADLER QMRSSSLDSF SPTMGYSGSS VPMAPDTFNV
     KPSGTITGNK VNVELLKIEL SGQNADGAIT NISPGYSNAA ISSSNSTDES SFDLNNILSS
     MQQKHAEKSF AKSMQGVNEQ IPANDVCHQA QRPMQGGLYS SQQPSSMSSL NSAYQNASMP
     PSASMVSYPY PFLNQQGQGV FPPYNAQNLQ WQSEAYSLKS MNFANPTWLG DQYQTSAPSS
     AYAQAQRQMF QQPMQQDVGK YMQFPFDAQS NTDSMRGNSR NNMF
//