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EOS1_YEAST
ID   EOS1_YEAST              Reviewed;         366 AA.
AC   P53938; D6W199; Q45TY2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=N-glycosylation protein EOS1;
DE   AltName: Full=ER-localized and oxidants sensitive protein 1;
GN   Name=EOS1; OrderedLocusNames=YNL080C; ORFNames=N2327;
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].
RC   STRAIN=SK1;
RX   PubMed=16273108; DOI=10.1038/ng1674;
RA   Deutschbauer A.M., Davis R.W.;
RT   "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL   Nat. Genet. 37:1333-1340(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8701611;
RX   DOI=10.1002/(sici)1097-0061(19960330)12:4<391::aid-yea921>3.0.co;2-n;
RA   Poehlmann R., Philippsen P.;
RT   "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
RT   reveals 12 new open reading frames (ORFs) and an ancient duplication of six
RT   ORFs.";
RL   Yeast 12:391-402(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
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   SUBCELLULAR LOCATION.
RX   PubMed=10649453;
RX   DOI=10.1002/(sici)1097-0061(200002)16:3<241::aid-yea517>3.0.co;2-t;
RA   Brachat A., Liebundguth N., Rebischung C., Lemire S., Schaerer F.,
RA   Hoepfner D., Demchyshyn V., Howald I., Duesterhoeft A., Moestl D.,
RA   Poehlmann R., Koetter P., Hall M.N., Wach A., Philippsen P.;
RT   "Analysis of deletion phenotypes and GFP fusions of 21 novel Saccharomyces
RT   cerevisiae open reading frames.";
RL   Yeast 16:241-253(2000).
RN   [6]
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   [7]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17187761; DOI=10.1016/j.bbrc.2006.12.012;
RA   Nakamura T., Ando A., Takagi H., Shima J.;
RT   "EOS1, whose deletion confers sensitivity to oxidative stress, is involved
RT   in N-glycosylation in Saccharomyces cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 353:293-298(2007).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX   PubMed=19756047; DOI=10.1038/msb.2009.64;
RA   Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT   "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT   new roles for protein glycosylation in eukaryotes.";
RL   Mol. Syst. Biol. 5:308-308(2009).
CC   -!- FUNCTION: Involved in oxidative stress resistance and N-glycosylation.
CC       {ECO:0000269|PubMed:17187761}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:10649453, ECO:0000269|PubMed:17187761}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:10649453,
CC       ECO:0000269|PubMed:17187761}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC   -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the EOS1 family. {ECO:0000305}.
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DR   EMBL; DQ115393; AAZ22528.1; -; Genomic_DNA.
DR   EMBL; X86470; CAA60178.1; -; Genomic_DNA.
DR   EMBL; Z71356; CAA95954.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10465.1; -; Genomic_DNA.
DR   PIR; S53898; S53898.
DR   RefSeq; NP_014319.1; NM_001182918.1.
DR   AlphaFoldDB; P53938; -.
DR   BioGRID; 35743; 745.
DR   IntAct; P53938; 1.
DR   STRING; 4932.YNL080C; -.
DR   iPTMnet; P53938; -.
DR   MaxQB; P53938; -.
DR   PaxDb; P53938; -.
DR   PRIDE; P53938; -.
DR   EnsemblFungi; YNL080C_mRNA; YNL080C; YNL080C.
DR   GeneID; 855644; -.
DR   KEGG; sce:YNL080C; -.
DR   SGD; S000005024; EOS1.
DR   VEuPathDB; FungiDB:YNL080C; -.
DR   eggNOG; ENOG502QTWB; Eukaryota.
DR   HOGENOM; CLU_043059_2_0_1; -.
DR   InParanoid; P53938; -.
DR   OMA; SLMIRWI; -.
DR   BioCyc; YEAST:G3O-33109-MON; -.
DR   PRO; PR:P53938; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53938; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IMP:SGD.
DR   InterPro; IPR021100; N-glycosylation_EOS1.
DR   PANTHER; PTHR28147; PTHR28147; 1.
DR   Pfam; PF12326; EOS1; 1.
DR   PRINTS; PR02070; NGLYCOSEOS1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..366
FT                   /note="N-glycosylation protein EOS1"
FT                   /id="PRO_0000203446"
FT   TOPO_DOM        1..136
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..167
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..195
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        217..321
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        343..366
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          233..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..259
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   366 AA;  41674 MW;  CFE1BA51A638DF5A CRC64;
     MTWILSTGMG PHEDKYAKHE RATFKKTYSS MKTLSLNHLT AKQHMLMALC RDISLLPPLT
     YIFTSLRKAW RVSMRTSITL YEPQSLRDAF TYFWQKLNSA YDNNSSFEGA SQKAVNGDGK
     DSLLLSALTT ARASEYLLCS LWCLVSLYLS YAILDSLMVR WIVKYSTVAA ILRMFSMSLI
     IVTLELLLLS SLSPELDYFL HTWILISCVL TAVYIWQSYL TSDLRYIRNQ EGEVQEDTNV
     PEETEDYEDG EDDADEDSHV VVADESTVDV PSNDSLSDNS DGGLFPVNRP SVSHSQSPKR
     PKKYPKKAFN FTTKRTIDLY KITVLCVVPV GLASFITMLG LLRNLFIQRL DVEQLERILH
     EMHPPA
 
 
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