PGP_HUMAN
ID PGP_HUMAN Reviewed; 321 AA.
AC A6NDG6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 120.
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:215071};
DE Short=PGP {ECO:0000303|PubMed:215071};
GN Name=PGP {ECO:0000312|HGNC:HGNC:8909};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=215071; DOI=10.1111/j.1469-1809.1978.tb00644.x;
RA Barker R.F., Hopkinson D.A.;
RT "Genetic polymorphism of human phosphoglycolate phosphatase (PGP).";
RL Ann. Hum. Genet. 42:143-151(1978).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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. Thereby, regulates the cellular levels of
CC glycerol-3-phosphate a metabolic intermediate of glucose, lipid and
CC energy metabolism. Was also shown to have a 2-phosphoglycolate
CC phosphatase activity and a tyrosine-protein phosphatase activity.
CC However, their physiological relevance is unclear (PubMed:26755581). In
CC vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (By
CC similarity). {ECO:0000250|UniProtKB:Q8CHP8,
CC 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 KM=1.4 mM for glycerol-3-phosphate {ECO:0000269|PubMed:26755581};
CC KM=1.5 mM for 2-phosphoglycolate {ECO:0000269|PubMed:26755581};
CC Vmax=100 nmol/min/mg enzyme with glycerol-3-phosphate as substrate
CC {ECO:0000269|PubMed:26755581};
CC Vmax=500 nmol/min/mg enzyme with 2-phosphoglycolate as substrate
CC {ECO:0000269|PubMed:26755581};
CC Note=Given the respective intracellular concentrations of glycerol-3-
CC phosphate and 2-phosphoglycolate, glycerol-3-phosphate with a
CC concentration of 2 to 10 mM is most probably the physiological
CC substrate. {ECO:0000269|PubMed:26755581};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8CHP8}.
CC -!- TISSUE SPECIFICITY: Detected in all tissues including red cells,
CC lymphocytes and cultured fibroblasts (at protein level). The highest
CC activities occur in skeletal muscle and cardiac muscle.
CC {ECO:0000269|PubMed:215071}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85534.1; -; Genomic_DNA.
DR CCDS; CCDS42104.1; -.
DR RefSeq; NP_001035830.1; NM_001042371.2.
DR AlphaFoldDB; A6NDG6; -.
DR SMR; A6NDG6; -.
DR BioGRID; 129694; 18.
DR IntAct; A6NDG6; 5.
DR MINT; A6NDG6; -.
DR STRING; 9606.ENSP00000330918; -.
DR DEPOD; PGP; -.
DR GlyGen; A6NDG6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A6NDG6; -.
DR MetOSite; A6NDG6; -.
DR PhosphoSitePlus; A6NDG6; -.
DR BioMuta; PGP; -.
DR EPD; A6NDG6; -.
DR jPOST; A6NDG6; -.
DR MassIVE; A6NDG6; -.
DR MaxQB; A6NDG6; -.
DR PaxDb; A6NDG6; -.
DR PeptideAtlas; A6NDG6; -.
DR PRIDE; A6NDG6; -.
DR ProteomicsDB; 907; -.
DR Antibodypedia; 54763; 150 antibodies from 25 providers.
DR DNASU; 283871; -.
DR Ensembl; ENST00000333503.8; ENSP00000330918.7; ENSG00000184207.9.
DR GeneID; 283871; -.
DR KEGG; hsa:283871; -.
DR MANE-Select; ENST00000333503.8; ENSP00000330918.7; NM_001042371.3; NP_001035830.1.
DR UCSC; uc002cpk.2; human.
DR CTD; 283871; -.
DR DisGeNET; 283871; -.
DR GeneCards; PGP; -.
DR HGNC; HGNC:8909; PGP.
DR HPA; ENSG00000184207; Tissue enhanced (testis).
DR MIM; 172280; gene.
DR neXtProt; NX_A6NDG6; -.
DR OpenTargets; ENSG00000184207; -.
DR PharmGKB; PA33246; -.
DR VEuPathDB; HostDB:ENSG00000184207; -.
DR eggNOG; KOG2882; Eukaryota.
DR GeneTree; ENSGT00940000160577; -.
DR HOGENOM; CLU_043473_0_1_1; -.
DR InParanoid; A6NDG6; -.
DR OMA; PPMHRET; -.
DR OrthoDB; 982374at2759; -.
DR PhylomeDB; A6NDG6; -.
DR TreeFam; TF314344; -.
DR PathwayCommons; A6NDG6; -.
DR Reactome; R-HSA-70171; Glycolysis.
DR SignaLink; A6NDG6; -.
DR BioGRID-ORCS; 283871; 79 hits in 1092 CRISPR screens.
DR ChiTaRS; PGP; human.
DR GenomeRNAi; 283871; -.
DR Pharos; A6NDG6; Tbio.
DR PRO; PR:A6NDG6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; A6NDG6; protein.
DR Bgee; ENSG00000184207; Expressed in tibialis anterior and 174 other tissues.
DR ExpressionAtlas; A6NDG6; baseline and differential.
DR Genevisible; A6NDG6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000121; F:glycerol-1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0043136; F:glycerol-3-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; ISS:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006114; P:glycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IDA:UniProtKB.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
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_0000316888"
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; 34006 MW; 6277550764EAAF91 CRC64;
MAAAEAGGDD ARCVRLSAER AQALLADVDT LLFDCDGVLW RGETAVPGAP EALRALRARG
KRLGFITNNS SKTRAAYAEK LRRLGFGGPA GPGASLEVFG TAYCTALYLR QRLAGAPAPK
AYVLGSPALA AELEAVGVAS VGVGPEPLQG EGPGDWLHAP LEPDVRAVVV GFDPHFSYMK
LTKALRYLQQ PGCLLVGTNM DNRLPLENGR FIAGTGCLVR AVEMAAQRQA DIIGKPSRFI
FDCVSQEYGI NPERTVMVGD RLDTDILLGA TCGLKTILTL TGVSTLGDVK NNQESDCVSK
KKMVPDFYVD SIADLLPALQ G
