PGP_RAT
ID PGP_RAT Reviewed; 321 AA.
AC D3ZDK7;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Glycerol-3-phosphate phosphatase {ECO:0000305};
DE Short=G3PP {ECO:0000303|PubMed:26755581};
DE EC=3.1.3.21 {ECO:0000269|PubMed:26755581};
DE AltName: Full=Aspartate-based ubiquitous Mg(2+)-dependent phosphatase {ECO:0000303|PubMed:26755581};
DE Short=AUM {ECO:0000303|PubMed:26755581};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q8CHP8};
DE AltName: Full=Phosphoglycolate phosphatase {ECO:0000303|PubMed:26755581};
DE Short=PGP {ECO:0000303|PubMed:26755581};
GN Name=Pgp {ECO:0000312|RGD:1307773};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=26755581; DOI=10.1073/pnas.1514375113;
RA Mugabo Y., Zhao S., Seifried A., Gezzar S., Al-Mass A., Zhang D.,
RA Lamontagne J., Attane C., Poursharifi P., Iglesias J., Joly E., Peyot M.L.,
RA Gohla A., Madiraju S.R., Prentki M.;
RT "Identification of a mammalian glycerol-3-phosphate phosphatase: Role in
RT metabolism and signaling in pancreatic beta-cells and hepatocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E430-439(2016).
CC -!- FUNCTION: Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-
CC phosphate into glycerol (PubMed:26755581). Thereby, regulates the
CC cellular levels of glycerol-3-phosphate a metabolic intermediate of
CC glucose, lipid and energy metabolism. Was also shown to have a 2-
CC phosphoglycolate phosphatase activity and a tyrosine-protein
CC phosphatase activity. However, their physiological relevance is unclear
CC (By similarity). In vitro, has also a phosphatase activity toward ADP,
CC ATP, GDP and GTP (By similarity). {ECO:0000250|UniProtKB:A6NDG6,
CC ECO:0000250|UniProtKB:Q8CHP8, ECO:0000269|PubMed:26755581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000250|UniProtKB:Q8CHP8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57685; EC=3.1.3.21;
CC Evidence={ECO:0000269|PubMed:26755581};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 3-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:66372, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57597; EC=3.1.3.21;
CC Evidence={ECO:0000269|PubMed:26755581};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8CHP8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHP8};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=47 nmol/min/mg enzyme with glycerol-3-phosphate as substrate
CC {ECO:0000269|PubMed:26755581};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8CHP8}.
CC -!- TISSUE SPECIFICITY: Expression was confirmed in liver, adipose tissue,
CC testis and pancreatic islet. {ECO:0000269|PubMed:26755581}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; AC103090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473948; EDM03833.1; -; Genomic_DNA.
DR RefSeq; NP_001162623.1; NM_001169152.1.
DR AlphaFoldDB; D3ZDK7; -.
DR SMR; D3ZDK7; -.
DR STRING; 10116.ENSRNOP00000012720; -.
DR jPOST; D3ZDK7; -.
DR PaxDb; D3ZDK7; -.
DR PeptideAtlas; D3ZDK7; -.
DR PRIDE; D3ZDK7; -.
DR GeneID; 287115; -.
DR KEGG; rno:287115; -.
DR UCSC; RGD:1307773; rat.
DR CTD; 283871; -.
DR RGD; 1307773; Pgp.
DR VEuPathDB; HostDB:ENSRNOG00000009536; -.
DR eggNOG; KOG2882; Eukaryota.
DR HOGENOM; CLU_043473_0_1_1; -.
DR InParanoid; D3ZDK7; -.
DR OMA; PPMHRET; -.
DR OrthoDB; 982374at2759; -.
DR PhylomeDB; D3ZDK7; -.
DR TreeFam; TF314344; -.
DR PRO; PR:D3ZDK7; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000009536; Expressed in testis and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000121; F:glycerol-1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0043136; F:glycerol-3-phosphatase activity; IMP:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; ISO:RGD.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; ISO:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:RGD.
DR GO; GO:0016311; P:dephosphorylation; ISO:RGD.
DR GO; GO:0006114; P:glycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IMP:UniProtKB.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:RGD.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006349; PGP_euk.
DR Pfam; PF13344; Hydrolase_6; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR TIGRFAMs; TIGR01452; PGP_euk; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..321
FT /note="Glycerol-3-phosphate phosphatase"
FT /id="PRO_0000435883"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
FT ACT_SITE 36
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P60487"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P60487"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P60487"
FT SITE 204
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
SQ SEQUENCE 321 AA; 34601 MW; BA4177EA94E10912 CRC64;
MAEAEAGGDE VRCVRLSAER AKLLLAEVDT LLFDCDGVLW RGETAVPGAP ETLRALRARG
KRLGFITNNS SKTRTAYAEK LRRLGFGGPM GPEAGLEVFG TAYCSALYLR QRLAGVPDPK
AYVLGSPALA AELEAVGVTS VGVGPDVLHG DGPSDWLAVP LEPDVRAVVV GFDPHFSYMK
LTKAVRYLQQ PDCLLVGTNM DNRLPLENGR FIAGTGCLVR AVEMAAQRQA DIIGKPSRFI
FDCVSQEYGI NPERTVMVGD RLDTDILLGS TCSLKTILTL TGVSSLEDVK SNQESDCMFK
KKMVPDFYVD SIADLLPALQ G
