GRE1_YEAST
ID GRE1_YEAST Reviewed; 168 AA.
AC Q08969; D6W3E7;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein GRE1;
DE AltName: Full=Genes de respuesta a estres protein 1;
DE AltName: Full=Hydrophilin;
GN Name=GRE1; OrderedLocusNames=YPL223C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP GENE NAME, AND INDUCTION.
RX PubMed=10407268;
RX DOI=10.1002/(sici)1097-0061(199907)15:10a<879::aid-yea428>3.0.co;2-q;
RA Garay-Arroyo A., Covarrubias A.A.;
RT "Three genes whose expression is induced by stress in Saccharomyces
RT cerevisiae.";
RL Yeast 15:879-892(1999).
RN [5]
RP INDUCTION.
RX PubMed=10681550; DOI=10.1074/jbc.275.8.5668;
RA Garay-Arroyo A., Colmenero-Flores J.M., Garciarrubio A., Covarrubias A.A.;
RT "Highly hydrophilic proteins in prokaryotes and eukaryotes are common
RT during conditions of water deficit.";
RL J. Biol. Chem. 275:5668-5674(2000).
RN [6]
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By osmotic, ionic and heat stress, and by water-deficiency.
CC {ECO:0000269|PubMed:10407268, ECO:0000269|PubMed:10681550}.
CC -!- MISCELLANEOUS: 'De respuesta a estres' means stress response in
CC Spanish.
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DR EMBL; Z73579; CAA97938.1; -; Genomic_DNA.
DR EMBL; AY692932; AAT92951.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11213.1; -; Genomic_DNA.
DR PIR; S65242; S65242.
DR RefSeq; NP_015101.1; NM_001184037.1.
DR AlphaFoldDB; Q08969; -.
DR SMR; Q08969; -.
DR BioGRID; 35962; 40.
DR STRING; 4932.YPL223C; -.
DR PaxDb; Q08969; -.
DR PRIDE; Q08969; -.
DR EnsemblFungi; YPL223C_mRNA; YPL223C; YPL223C.
DR GeneID; 855878; -.
DR KEGG; sce:YPL223C; -.
DR SGD; S000006144; GRE1.
DR VEuPathDB; FungiDB:YPL223C; -.
DR HOGENOM; CLU_1603680_0_0_1; -.
DR OMA; MDEYDQS; -.
DR BioCyc; YEAST:G3O-34112-MON; -.
DR PRO; PR:Q08969; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08969; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..168
FT /note="Protein GRE1"
FT /id="PRO_0000083846"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 168 AA; 19026 MW; FD3FE734898F6811 CRC64;
MSNLLNKFAD KLHGNDHDER YEDDNDDQTR QQRHEKHQQR EFRNQGSKAD PYGEENQGNF
PQRQQPQSNL GGNTQFGGND FQQQTTDYTA GTGGGTYTQT YRETNTQGQL DDDEDDDFLT
SGQQQKQGRT RGAQSNRYQS SNIGSGRRDL SGSGNDEYDD DSGNQGVW