EST1_YEAST
ID EST1_YEAST Reviewed; 699 AA.
AC P17214; D6VYN3; Q05997;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Telomere elongation protein EST1;
DE AltName: Full=Ever shorter telomeres protein 1;
GN Name=EST1; OrderedLocusNames=YLR233C; ORFNames=L8083.15;
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].
RX PubMed=2655926; DOI=10.1016/0092-8674(89)90132-3;
RA Lundblad V., Szostak J.W.;
RT "A mutant with a defect in telomere elongation leads to senescence in
RT yeast.";
RL Cell 57:633-643(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
RP PUTATIVE SIMILARITY TO REVERSE TRANSCRIPTASES.
RX PubMed=2406024; DOI=10.1016/0092-8674(90)90653-v;
RA Lundblad V., Blackburn E.H.;
RT "RNA-dependent polymerase motifs in EST1: tentative identification of a
RT protein component of an essential yeast telomerase.";
RL Cell 60:529-530(1990).
RN [5]
RP SHOWS THAT THIS SIMILARITY IS DOUBTFUL.
RX PubMed=1669287;
RA Henikoff S.;
RT "Playing with blocks: some pitfalls of forcing multiple alignments.";
RL New Biol. 3:1148-1154(1991).
RN [6]
RP FUNCTION, AND INTERACTION WITH CDC13.
RX PubMed=11390652; DOI=10.1128/mcb.21.13.4233-4245.2001;
RA Meier B., Driller L., Jaklin S., Feldmann H.M.;
RT "New function of CDC13 in positive telomere length regulation.";
RL Mol. Cell. Biol. 21:4233-4245(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH MPS3.
RX PubMed=17245108; DOI=10.4161/cc.6.1.3647;
RA Antoniacci L.M., Kenna M.A., Skibbens R.V.;
RT "The nuclear envelope and spindle pole body-associated Mps3 protein bind
RT telomere regulators and function in telomere clustering.";
RL Cell Cycle 6:75-79(2007).
CC -!- FUNCTION: Directly involved in telomere replication. Associates with
CC telomerase and during its interaction with CDC13, telomerase activity
CC is promoted. {ECO:0000269|PubMed:11390652,
CC ECO:0000269|PubMed:17245108}.
CC -!- SUBUNIT: Interacts with CDC13 and MPS3. {ECO:0000269|PubMed:11390652,
CC ECO:0000269|PubMed:17245108}.
CC -!- INTERACTION:
CC P17214; P32797: CDC13; NbExp=3; IntAct=EBI-6684, EBI-4187;
CC P17214; Q06163: EST2; NbExp=4; IntAct=EBI-6684, EBI-3764464;
CC P17214; P47069: MPS3; NbExp=3; IntAct=EBI-6684, EBI-25811;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EST1 family. {ECO:0000305}.
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DR EMBL; J04849; AAA66908.1; -; Genomic_DNA.
DR EMBL; U19027; AAB67418.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09549.1; -; Genomic_DNA.
DR PIR; S51454; S51454.
DR RefSeq; NP_013334.1; NM_001182120.1.
DR AlphaFoldDB; P17214; -.
DR SMR; P17214; -.
DR BioGRID; 31502; 715.
DR ComplexPortal; CPX-3298; Telomerase holoenzyme complex.
DR DIP; DIP-1306N; -.
DR IntAct; P17214; 36.
DR MINT; P17214; -.
DR STRING; 4932.YLR233C; -.
DR iPTMnet; P17214; -.
DR MaxQB; P17214; -.
DR PaxDb; P17214; -.
DR PRIDE; P17214; -.
DR EnsemblFungi; YLR233C_mRNA; YLR233C; YLR233C.
DR GeneID; 850934; -.
DR KEGG; sce:YLR233C; -.
DR SGD; S000004223; EST1.
DR VEuPathDB; FungiDB:YLR233C; -.
DR eggNOG; KOG2162; Eukaryota.
DR GeneTree; ENSGT00940000176623; -.
DR HOGENOM; CLU_394378_0_0_1; -.
DR InParanoid; P17214; -.
DR OMA; EFSCVNF; -.
DR BioCyc; YEAST:G3O-32344-MON; -.
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P17214; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P17214; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IPI:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:0071919; P:G-quadruplex DNA formation; IDA:SGD.
DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IDA:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IDA:SGD.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR018834; DNA/RNA-bd_Est1-type.
DR InterPro; IPR045153; Est1/Ebs1-like.
DR InterPro; IPR019458; Est1_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR15696; PTHR15696; 1.
DR Pfam; PF10374; EST1; 1.
DR Pfam; PF10373; EST1_DNA_bind; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..699
FT /note="Telomere elongation protein EST1"
FT /id="PRO_0000087072"
FT REGION 641..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 49
FT /note="R -> C (in Ref. 1; AAA66908)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="L -> V (in Ref. 1; AAA66908)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="D -> N (in Ref. 1; AAA66908)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="M -> I (in Ref. 1; AAA66908)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="V -> M (in Ref. 1; AAA66908)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="Y -> H (in Ref. 1; AAA66908)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="N -> D (in Ref. 1; AAA66908)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="I -> M (in Ref. 1; AAA66908)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="R -> K (in Ref. 1; AAA66908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 81800 MW; 9CF552AFDA6BDEDE CRC64;
MDNEEVNEEC MRLFFKNARA HLDKHLTSRL TCDENAYITF RCFLDGIHRK STRFLEELLL
KQENMYHNNN YERINDSVIP LVLKLLWLQI HEPTLQWFEH WFHDIMRLSN RRKFRVFRIF
QKKMIQFFKI THRYYYDIIE HLCAKYDMNS VISNALFAKL NLMQYTDGLS THEKIILNTS
NPLTFSIVIS LQRCVINLGS THFYKTLLNK PSNKPKSVEG FEKSIRYLNI ASLYLPAVGD
TYFQRAKIYL ITGKFSLYFF ELVRGALVRI PSKCALNNLK DFILTPDFPE RRRLMKKLAI
LVSKDLKGEK SFFEGQIVLQ FLSIVEHTLV PQSWNASRAS NCWLLKEHLQ MAALKYHSGN
INVILENLAA TMGSFDLMFT TRKSKEQKNK LKYADLSERQ VFFLDLSFDF IANIIDVVIK
PSWQKNMEDF RYLAIIRLLM CWIKSYRSIL QYTHRHRKFC TSFALLLNDL INSPLNCSGN
IYSHRPKRSY LFREDIIFRE FSCINFALTD FNDDYVYDSP DMINNIIGCP TLTKVLSPKE
ECVLRIRSII FSGMKFLEKN DTGVIWNASK YKFDLISPNI KIKRQIALSE ISSKINVKTQ
QERVVSSRKV EAKRDEQQRK RAGKIAVTEL EKQFANVRRT KKLSPLPEKD GVSSELVKHA
ASRGRKTITG PLSSDFLSYP DEAIDADEDI TVQVPDTPT