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Protein

Glycerol-3-phosphate phosphatase

Gene

Pgp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism (PubMed:26755581). Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear (PubMed:26755581, PubMed:24338473). In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (PubMed:24338473).2 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication
Glycerol 1-phosphate + H2O = glycerol + phosphate.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Enzyme regulationi

Inhibited by orthovanadate, beryllium trifluoride, Ca2+ and EDTA.1 Publication

Kineticsi

Kcat is 0.1 sec(-1) with glycerol-3-phosphate.1 Publication

Manual assertion based on experiment ini

  1. KM=0.42 mM for ADP1 Publication
  2. KM=1.23 mM for ATP1 Publication
  3. KM=1.48 mM for GDP1 Publication
  4. KM=1.47 mM for GTP1 Publication
  5. KM=1.29 mM for glycerol-3-phosphate1 Publication
  1. Vmax=100 nmol/min/mg enzyme with glycerol-3-phosphate as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei34Nucleophile1 Publication1
Metal bindingi34MagnesiumBy similarity1
Active sitei36Proton donorCurated1
Metal bindingi36Magnesium; via carbonyl oxygenBy similarity1
Sitei204Important for substrate specificity1 Publication1
Metal bindingi260MagnesiumBy similarity1

GO - Molecular functioni

  • glycerol-1-phosphatase activity Source: UniProtKB-EC
  • glycerol-3-phosphatase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • nucleotide phosphatase activity, acting on free nucleotides Source: UniProtKB
  • phosphoglycolate phosphatase activity Source: MGI
  • protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  • dephosphorylation Source: UniProtKB
  • glycerol biosynthetic process Source: UniProtKB
  • glycerophospholipid metabolic process Source: UniProtKB
  • negative regulation of gluconeogenesis Source: UniProtKB
  • peptidyl-tyrosine dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.74. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate phosphataseCurated (EC:3.1.3.211 Publication)
Short name:
G3PP1 Publication
Alternative name(s):
Aspartate-based ubiquitous Mg(2+)-dependent phosphatase1 Publication (EC:3.1.3.481 Publication)
Short name:
AUM1 Publication
Phosphoglycolate phosphatase1 Publication
Short name:
PGP1 Publication
Gene namesi
Name:PgpImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1914328. Pgp.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi34D → N: Abolishes phosphatase activity. 1 Publication1
Mutagenesisi41R → N: Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with R-44 and I-45. 1 Publication1
Mutagenesisi44T → R: Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with N-41 and I-45. 1 Publication1
Mutagenesisi45A → I: Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with N-41 and R-44. 1 Publication1
Mutagenesisi67T → S: Strongly reduces phosphatase activity; when associated with R-71; R-72 and A-73. Abolishes phosphatase activity; when associated with R-72 and A-73. 1 Publication1
Mutagenesisi71S → R: Mildly reduces phosphatase activity; when associated with R-72 and A-73. Strongly reduces phosphatase activity; when associated with S-67; R-72 and A-73. 1 Publication1
Mutagenesisi72K → R: Mildly reduces phosphatase activity; when associated with R-71 and A-73. Strongly reduces phosphatase activity; when associated with S-67; R-71 and A-73. Abolishes phosphatase activity; when associated with S-67 and A-73. 1 Publication1
Mutagenesisi73T → A: Abolishes phosphatase activity. Abolishes phosphatase activity; when associated with S-67 and R-72. Strongly reduces phosphatase activity; when associated with S-67; R-71 and R-72. Mildly reduces phosphatase activity; when associated with R-71 and R-72. 1 Publication1
Mutagenesisi204L → H: Strongly increases activity with pyridoxal phosphate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003168891 – 321Glycerol-3-phosphate phosphataseAdd BLAST321

Proteomic databases

EPDiQ8CHP8.
MaxQBiQ8CHP8.
PaxDbiQ8CHP8.
PeptideAtlasiQ8CHP8.
PRIDEiQ8CHP8.

2D gel databases

REPRODUCTION-2DPAGEIPI00380195.
Q8CHP8.

PTM databases

iPTMnetiQ8CHP8.
PhosphoSitePlusiQ8CHP8.

Expressioni

Tissue specificityi

Ubiquitously expressed with higher expression in testis, heart, skeletal muscle and islet tissue (at protein level).2 Publications

Inductioni

Up-regulated in white adipose tissue and down-regulated in brown adipose tissue upon fasting.1 Publication

Gene expression databases

BgeeiENSMUSG00000043445.
GenevisibleiQ8CHP8. MM.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000052866.

Structurei

Secondary structure

1321
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi120 – 125Combined sources6
Helixi127 – 135Combined sources9
Beta strandi139 – 141Combined sources3
Beta strandi150 – 152Combined sources3
Helixi153 – 156Combined sources4
Beta strandi165 – 170Combined sources6
Helixi178 – 187Combined sources10
Beta strandi193 – 198Combined sources6
Beta strandi202 – 205Combined sources4
Beta strandi211 – 213Combined sources3
Helixi215 – 226Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BKMX-ray2.65A/B/C/D114-233[»]
ProteinModelPortaliQ8CHP8.
SMRiQ8CHP8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2882. Eukaryota.
COG0647. LUCA.
GeneTreeiENSGT00510000047020.
HOGENOMiHOG000068104.
HOVERGENiHBG049429.
InParanoidiQ8CHP8.
KOiK19269.
OMAiFIFDCVA.
OrthoDBiEOG091G0I92.
PhylomeDBiQ8CHP8.
TreeFamiTF314344.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR023215. NPhePase-like_dom.
IPR006349. PGP_euk.
[Graphical view]
PfamiPF13344. Hydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF000915. PGP-type_phosphatase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8CHP8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEAEAGGDE ARCVRLSAER AKLLLAEVDT LLFDCDGVLW RGETAVPGAP
60 70 80 90 100
ETLRALRARG KRLGFITNNS SKTRTAYAEK LRRLGFGGPV GPEAGLEVFG
110 120 130 140 150
TAYCSALYLR QRLAGVPDPK AYVLGSPALA AELEAVGVTS VGVGPDVLHG
160 170 180 190 200
DGPSDWLAVP LEPDVRAVVV GFDPHFSYMK LTKAVRYLQQ PDCLLVGTNM
210 220 230 240 250
DNRLPLENGR FIAGTGCLVR AVEMAAQRQA DIIGKPSRFI FDCVSQEYGI
260 270 280 290 300
NPERTVMVGD RLDTDILLGS TCSLKTILTL TGVSSLEDVK SNQESDCMFK
310 320
KKMVPDFYVD SIADLLPALQ G
Length:321
Mass (Da):34,541
Last modified:March 1, 2003 - v1
Checksum:iF083ED0432327A83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC040100 mRNA. Translation: AAH40100.1.
CCDSiCCDS28482.1.
RefSeqiNP_080230.2. NM_025954.3.
UniGeneiMm.28541.
Mm.486259.

Genome annotation databases

EnsembliENSMUST00000053024; ENSMUSP00000052866; ENSMUSG00000043445.
GeneIDi67078.
KEGGimmu:67078.
UCSCiuc008awe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC040100 mRNA. Translation: AAH40100.1.
CCDSiCCDS28482.1.
RefSeqiNP_080230.2. NM_025954.3.
UniGeneiMm.28541.
Mm.486259.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BKMX-ray2.65A/B/C/D114-233[»]
ProteinModelPortaliQ8CHP8.
SMRiQ8CHP8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000052866.

PTM databases

iPTMnetiQ8CHP8.
PhosphoSitePlusiQ8CHP8.

2D gel databases

REPRODUCTION-2DPAGEIPI00380195.
Q8CHP8.

Proteomic databases

EPDiQ8CHP8.
MaxQBiQ8CHP8.
PaxDbiQ8CHP8.
PeptideAtlasiQ8CHP8.
PRIDEiQ8CHP8.

Protocols and materials databases

DNASUi67078.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053024; ENSMUSP00000052866; ENSMUSG00000043445.
GeneIDi67078.
KEGGimmu:67078.
UCSCiuc008awe.1. mouse.

Organism-specific databases

CTDi283871.
MGIiMGI:1914328. Pgp.

Phylogenomic databases

eggNOGiKOG2882. Eukaryota.
COG0647. LUCA.
GeneTreeiENSGT00510000047020.
HOGENOMiHOG000068104.
HOVERGENiHBG049429.
InParanoidiQ8CHP8.
KOiK19269.
OMAiFIFDCVA.
OrthoDBiEOG091G0I92.
PhylomeDBiQ8CHP8.
TreeFamiTF314344.

Enzyme and pathway databases

BRENDAi3.1.3.74. 3474.

Miscellaneous databases

ChiTaRSiPgp. mouse.
PROiQ8CHP8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000043445.
GenevisibleiQ8CHP8. MM.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR023215. NPhePase-like_dom.
IPR006349. PGP_euk.
[Graphical view]
PfamiPF13344. Hydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF000915. PGP-type_phosphatase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPGP_MOUSE
AccessioniPrimary (citable) accession number: Q8CHP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.