SOL2_YEAST
ID SOL2_YEAST Reviewed; 315 AA.
AC P37262; D6VR76;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=6-phosphogluconolactonase-like protein 2;
DE AltName: Full=Suppressor of LOS1;
GN Name=SOL2; OrderedLocusNames=YCR073W-A; ORFNames=YCRX13W;
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=8725220; DOI=10.1093/genetics/143.2.699;
RA Shen W.-C., Stanford D.R., Hopper A.K.;
RT "Los1p, involved in yeast pre-tRNA splicing, positively regulates members
RT of the SOL gene family.";
RL Genetics 143:699-712(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
RP SEQUENCE REVISION TO 171.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION, AND SIMILARITY.
RX PubMed=8313894; DOI=10.1002/j.1460-2075.1994.tb06287.x;
RA Koonin E.V., Bork P., Sander C.;
RT "Yeast chromosome III: new gene functions.";
RL EMBO J. 13:493-503(1994).
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).
RN [7]
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 [8]
RP FUNCTION, LACK OF ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=15454531; DOI=10.1534/genetics.104.030452;
RA Stanford D.R., Whitney M.L., Hurto R.L., Eisaman D.M., Shen W.-C.,
RA Hopper A.K.;
RT "Division of labor among the yeast Sol proteins implicated in tRNA nuclear
RT export and carbohydrate metabolism.";
RL Genetics 168:117-127(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: May be involved in regulation of tRNA subcellular
CC distribution. {ECO:0000269|PubMed:15454531}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15454531}.
CC -!- MISCELLANEOUS: Present with 1160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. 6-phosphogluconolactonase subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks 6-phosphogluconolactonase activity. {ECO:0000305}.
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DR EMBL; U46559; AAB49322.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42272.2; -; Genomic_DNA.
DR EMBL; BK006937; DAA07545.1; -; Genomic_DNA.
DR PIR; S53589; S53589.
DR RefSeq; NP_009999.2; NM_001178815.1.
DR AlphaFoldDB; P37262; -.
DR SMR; P37262; -.
DR BioGRID; 31049; 85.
DR DIP; DIP-8183N; -.
DR IntAct; P37262; 6.
DR MINT; P37262; -.
DR STRING; 4932.YCR073W-A; -.
DR iPTMnet; P37262; -.
DR MaxQB; P37262; -.
DR PaxDb; P37262; -.
DR PRIDE; P37262; -.
DR EnsemblFungi; YCR073W-A_mRNA; YCR073W-A; YCR073W-A.
DR GeneID; 850437; -.
DR KEGG; sce:YCR073W-A; -.
DR SGD; S000000718; SOL2.
DR VEuPathDB; FungiDB:YCR073W-A; -.
DR eggNOG; KOG3147; Eukaryota.
DR GeneTree; ENSGT00550000075110; -.
DR HOGENOM; CLU_053947_0_1_1; -.
DR InParanoid; P37262; -.
DR OMA; IAMSQST; -.
DR BioCyc; YEAST:G3O-29399-MON; -.
DR PRO; PR:P37262; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P37262; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR CDD; cd01400; 6PGL; 1.
DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR039104; PGLS.
DR PANTHER; PTHR11054; PTHR11054; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR01198; pgl; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..315
FT /note="6-phosphogluconolactonase-like protein 2"
FT /id="PRO_0000090083"
FT REGION 59..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50278"
SQ SEQUENCE 315 AA; 34501 MW; 7F0AAD76574AB276 CRC64;
MTTTVPKIFA FHEFSDVAEA VADHVVHAQD GALAPKNERK HSVPNISMNA LDMTREASCK
STASAAEGKS GSSGSGSGSS KPKKEKRFKI ALSGGSLIEV LHEGLLKRDD VRWGDWDIYF
ADERLVPFSS NESNYGCAKR KILDLIDTAK YGTPKVYHID ESLIDDPQEC ADNYEKVLIR
GFAGRDSVKL PMFDLFLLGC APDGHIASLF PNFQDNLREK LAWVVPVENA PSGPSTRISL
TIPVICHSHR VTFVVEGATK APIIKTIMER PEKGLPSSIV NEGAAGRVSW FVDDDALTDV
LVTKKKYKFH QGLSI
