(data stored in ACNUC8465 zone)

SWISSPROT: GPP2_YEAST

ID   GPP2_YEAST              Reviewed;         250 AA.
AC   P40106; D3DLW7;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-MAY-2019, entry version 161.
DE   RecName: Full=Glycerol-1-phosphate phosphohydrolase 2 {ECO:0000305};
DE            EC=3.1.3.21 {ECO:0000269|PubMed:8662716};
DE   AltName: Full=(DL)-glycerol-3-phosphatase 2 {ECO:0000303|PubMed:8662716};
DE   AltName: Full=Hyperosmolarity-responsive protein 2 {ECO:0000303|PubMed:7500933};
GN   Name=GPP2 {ECO:0000303|PubMed:8662716};
GN   Synonyms=HOR2 {ECO:0000303|PubMed:7500933}; OrderedLocusNames=YER062C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=RS16;
RX   PubMed=7500933; DOI=10.1007/BF00290358;
RA   Hirayama T., Maeda T., Saito H., Shinozaki K.;
RT   "Cloning and characterization of seven cDNAs for hyperosmolarity-
RT   responsive (HOR) genes of Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 249:127-138(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
RA   Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
RA   Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
RA   Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
RA   Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RX   PubMed=8662716; DOI=10.1074/jbc.271.23.13875;
RA   Norbeck J., Paehlman A.-K., Akhtar N., Blomberg A., Adler L.;
RT   "Purification and characterization of two isoenzymes of DL-glycerol-3-
RT   phosphatase from Saccharomyces cerevisiae. Identification of the
RT   corresponding GPP1 and GPP2 genes and evidence for osmotic regulation
RT   of Gpp2p expression by the osmosensing mitogen-activated protein
RT   kinase signal transduction pathway.";
RL   J. Biol. Chem. 271:13875-13881(1996).
RN   [5]
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   [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.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Glycerol-1-phosphate phosphohydrolase involved in
CC       glycerol biosynthesis. Plays a role in osmoadaptation.
CC       {ECO:0000269|PubMed:8662716}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycerol 1-phosphate + H2O = glycerol + phosphate;
CC         Xref=Rhea:RHEA:11476, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:231935; EC=3.1.3.21;
CC         Evidence={ECO:0000269|PubMed:8662716};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:8662716};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.9 mM for (DL)-glycerol 3-phosphate
CC         {ECO:0000269|PubMed:8662716};
CC         Vmax=46 umol/min/mg enzyme {ECO:0000269|PubMed:8662716};
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:8662716};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8662716}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: By osmotic stress (at protein level).
CC       {ECO:0000269|PubMed:8662716}.
CC   -!- MISCELLANEOUS: Present with 5000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. DOG/GPP
CC       family. {ECO:0000305}.
DR   EMBL; D50469; BAA09058.1; -; mRNA.
DR   EMBL; U18813; AAB64598.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07721.1; -; Genomic_DNA.
DR   PIR; S50565; S50565.
DR   RefSeq; NP_010984.3; NM_001178953.3.
DR   SMR; P40106; -.
DR   BioGrid; 36804; 90.
DR   DIP; DIP-1366N; -.
DR   IntAct; P40106; 8.
DR   MINT; P40106; -.
DR   STRING; 4932.YER062C; -.
DR   iPTMnet; P40106; -.
DR   MaxQB; P40106; -.
DR   PaxDb; P40106; -.
DR   PRIDE; P40106; -.
DR   EnsemblFungi; YER062C_mRNA; YER062C_mRNA; YER062C.
DR   GeneID; 856791; -.
DR   KEGG; sce:YER062C; -.
DR   EuPathDB; FungiDB:YER062C; -.
DR   SGD; S000000864; GPP2.
DR   GeneTree; ENSGT00940000176698; -.
DR   HOGENOM; HOG000248341; -.
DR   InParanoid; P40106; -.
DR   KO; K06116; -.
DR   OMA; FLKTIHG; -.
DR   BioCyc; MetaCyc:YER062C-MONOMER; -.
DR   BioCyc; YEAST:YER062C-MONOMER; -.
DR   BRENDA; 3.1.3.21; 984.
DR   PRO; PR:P40106; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0000121; F:glycerol-1-phosphatase activity; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044262; P:cellular carbohydrate metabolic process; IDA:SGD.
DR   GO; GO:0006114; P:glycerol biosynthetic process; IMP:SGD.
DR   GO; GO:0006071; P:glycerol metabolic process; IBA:GO_Central.
DR   GO; GO:0006970; P:response to osmotic stress; IDA:SGD.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   Pfam; PF13419; HAD_2; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P40106.
DR   SWISS-2DPAGE; P40106.
KW   Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Isopeptide bond; Magnesium; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Stress response; Ubl conjugation.
FT   CHAIN         1    250       Glycerol-1-phosphate phosphohydrolase 2.
FT                                /FTId=PRO_0000087561.
FT   ACT_SITE     18     18       Nucleophile. {ECO:0000250}.
FT   ACT_SITE     20     20       Proton donor. {ECO:0000250}.
FT   METAL        18     18       Magnesium. {ECO:0000250}.
FT   METAL        20     20       Magnesium. {ECO:0000250}.
FT   METAL       179    179       Magnesium. {ECO:0000250}.
FT   MOD_RES      90     90       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P41277}.
FT   CROSSLNK     64     64       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P41277}.
FT   CROSSLNK    144    144       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P41277}.
SQ   SEQUENCE   250 AA;  27814 MW;  D69F343B10417313 CRC64;
     MGLTTKPLSL KVNAALFDVD GTIIISQPAI AAFWRDFGKD KPYFDAEHVI QVSHGWRTFD
     AIAKFAPDFA NEEYVNKLEA EIPVKYGEKS IEVPGAVKLC NALNALPKEK WAVATSGTRD
     MAQKWFEHLG IRRPKYFITA NDVKQGKPHP EPYLKGRNGL GYPINEQDPS KSKVVVFEDA
     PAGIAAGKAA GCKIIGIATT FDLDFLKEKG CDIIVKNHES IRVGGYNAET DEVEFIFDDY
     LYAKDDLLKW
//

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