ESL2_YEAST
ID ESL2_YEAST Reviewed; 1195 AA.
AC P36168; D6VXF7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=EST/SMG-like protein 2 {ECO:0000303|PubMed:23893744};
GN Name=ESL2 {ECO:0000303|PubMed:23893744};
GN OrderedLocusNames=YKR096W {ECO:0000312|SGD:S000001804};
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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 [4]
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 [5]
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 [6]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22375831; DOI=10.1021/pr3000333;
RA Oeljeklaus S., Reinartz B.S., Wolf J., Wiese S., Tonillo J., Podwojski K.,
RA Kuhlmann K., Stephan C., Meyer H.E., Schliebs W., Brocard C., Erdmann R.,
RA Warscheid B.;
RT "Identification of core components and transient interactors of the
RT peroxisomal importomer by dual-track stable isotope labeling with amino
RT acids in cell culture analysis.";
RL J. Proteome Res. 11:2567-2580(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 -!- SUBUNIT: Transiently interacts with PEX14.
CC {ECO:0000269|PubMed:22375831}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Peroxisome
CC {ECO:0000269|PubMed:22375831}. Note=A fraction of the protein co-
CC localizes with peroxisomes. {ECO:0000269|PubMed:22375831}.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z28321; CAA82176.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09247.1; -; Genomic_DNA.
DR PIR; S38174; S38174.
DR RefSeq; NP_013022.1; NM_001179886.1.
DR AlphaFoldDB; P36168; -.
DR SMR; P36168; -.
DR BioGRID; 34227; 167.
DR DIP; DIP-1929N; -.
DR IntAct; P36168; 6.
DR MINT; P36168; -.
DR STRING; 4932.YKR096W; -.
DR iPTMnet; P36168; -.
DR MaxQB; P36168; -.
DR PaxDb; P36168; -.
DR PRIDE; P36168; -.
DR EnsemblFungi; YKR096W_mRNA; YKR096W; YKR096W.
DR GeneID; 853971; -.
DR KEGG; sce:YKR096W; -.
DR SGD; S000001804; ESL2.
DR VEuPathDB; FungiDB:YKR096W; -.
DR eggNOG; ENOG502QQKF; Eukaryota.
DR GeneTree; ENSGT00940000176784; -.
DR HOGENOM; CLU_006407_0_0_1; -.
DR InParanoid; P36168; -.
DR OMA; PEVWKCW; -.
DR BioCyc; YEAST:G3O-32059-MON; -.
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P36168; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36168; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005777; C:peroxisome; 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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR InterPro; IPR045153; Est1/Ebs1-like.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR15696; PTHR15696; 1.
DR Pfam; PF13638; PIN_4; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Peroxisome; Reference proteome.
FT CHAIN 1..1195
FT /note="EST/SMG-like protein 2"
FT /id="PRO_0000203229"
FT DOMAIN 1025..1164
FT /note="PINc"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1195 AA; 137491 MW; D7251DED6B523622 CRC64;
MPETSVQNPL RLSENENTRS MFLSASQQQR PSATPSFPRL VRNTTANLSL SDFQVLNPSS
KRQNSNSVYD DINSSKRRIS RPRFSDIEGK NNDHTYPERT TVKESEKNPS PRYVSSSKRA
LKRENSVGIT QSSALISKSF SENGGSIAHE KWSPENMIKP LNVSQNSLAF VDAGSDEQSK
SEIVGGFQRK SNNSQEINDK DNSARDQDFN NSGNNNNNNN HSSNNNDNNN NNNDDNNNNN
NSNSRDNNNN SDDSNEREEN DSCKPASNKR SGIALIQKLQ ELYKVIVKQE IELQERCSQL
TNSQTTELKS LWTIYKINTD LVNNYVTFIT TALLPSQPPH DLVIGQEIVE IYRIERRLWV
YGTITFLDVL KNFSNFMDPE VCCQFITHVF VSLSTMISDI PSKYSITWLQ RLGDLSRMAI
ALYPSSFIDW KLSAEHWYTE AMKYIYNHGK LYYHMSTVQQ NTLEAFVNLG KSVFCQETFT
PSPQYMQLVI DNIYQRAFVE RNNGNLRNSL LIEYLKHSEA MLLPSFLESP DLQNVVLSYF
IEKFGIDANG CNIFNAEDMF VQNPDFFKYF FRHGPSFAQS HILQIVGFGE PKNPFAILFE
LPKYLKERKD KKERKKSSNN DSSVTESSTG NSRNDNEDDD EIMSSTTSIS DHDLLAEFFN
DIDTLRRPIL PSMLTNEAWL ETLKFLNMTS LKCGIIVLRK FLHGPLGIAL PHILPWIYFI
ISICLKSSQL SDPVSKEFWM IIVKRAFPWD TMVTFMNVLI VYLLDNQTSN SIIGDLCDDY
DKLSLSELLE LFNEGEELPE ILGCWGTLWF DTICEKNTHS ISSEDNFQEI GIKDYMALDS
PTDGIIFDEK DENGEKFWKR ACRTIFLFRE LSRSFPIGVI IRNDPLIYRS SFQNTNILGS
LVFKLEPLCN IHNNIPVLGA LESIIDISEA RSENNTDLHA VPELSVNEGD NIFHYVGYKK
LRADYTCFDK NGEFLSASLY TTWYVPNSNN TNIEDNINYN SEKENEGLFL ECIKSDYPEI
DFKTTYFVFD ATSWLRHSAR IFKLAQNRLL RFAICLTTFQ ELRFLRKSKD ENVMEAATRG
IITIRQLYYE NKVLPLRFTG NVATHIEENL EFEEQITWRT HVDEFVIESV MKAQEKLESA
SEPRLSPRRF NYVVLISDDD AMKKKAEEKE IKTLSTRFVF SLCTKLGEQR HLCTD
