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Glycerol-3-phosphate phosphatase (G3PP) (EC 3.1.3.21) (Aspartate-based ubiquitous Mg(2 )-dependent phosphatase) (AUM) (EC 3.1.3.48) (Phosphoglycolate phosphatase) (PGP)

 PGP_MOUSE               Reviewed;         321 AA.
Q8CHP8;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
05-DEC-2018, entry version 128.
RecName: Full=Glycerol-3-phosphate phosphatase {ECO:0000305};
Short=G3PP {ECO:0000303|PubMed:26755581};
EC=3.1.3.21 {ECO:0000269|PubMed:26755581};
AltName: Full=Aspartate-based ubiquitous Mg(2+)-dependent phosphatase {ECO:0000303|PubMed:24338473};
Short=AUM {ECO:0000303|PubMed:24338473};
EC=3.1.3.48 {ECO:0000269|PubMed:24338473};
AltName: Full=Phosphoglycolate phosphatase {ECO:0000303|PubMed:24338473};
Short=PGP {ECO:0000303|PubMed:24338473};
Name=Pgp {ECO:0000312|MGI:MGI:1914328};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=26755581; DOI=10.1073/pnas.1514375113;
Mugabo Y., Zhao S., Seifried A., Gezzar S., Al-Mass A., Zhang D.,
Lamontagne J., Attane C., Poursharifi P., Iglesias J., Joly E.,
Peyot M.L., Gohla A., Madiraju S.R., Prentki M.;
"Identification of a mammalian glycerol-3-phosphate phosphatase: Role
in metabolism and signaling in pancreatic beta-cells and
hepatocytes.";
Proc. Natl. Acad. Sci. U.S.A. 113:E430-439(2016).
[4]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 44-233 IN COMPLEX WITH
MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY,
MUTAGENESIS OF ASP-34; ARG-41; THR-44; ALA-45; THR-67; SER-71; LYS-72;
THR-73 AND LEU-204, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES,
ACTIVITY REGULATION, AND SUBUNIT.
PubMed=24338473; DOI=10.1074/jbc.M113.503359;
Seifried A., Knobloch G., Duraphe P.S., Segerer G., Manhard J.,
Schindelin H., Schultz J., Gohla A.;
"Evolutionary and structural analyses of the mammalian haloacid
dehalogenase-type phosphatases AUM and chronophin provide insight into
the basis of their different substrate specificities.";
J. Biol. Chem. 289:3416-3431(2014).
-!- FUNCTION: 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). {ECO:0000269|PubMed:24338473,
ECO:0000269|PubMed:26755581}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein]
+ phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48;
Evidence={ECO:0000269|PubMed:24338473};
-!- CATALYTIC ACTIVITY:
Reaction=glycerol 1-phosphate + H2O = glycerol + phosphate;
Xref=Rhea:RHEA:11476, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
ChEBI:CHEBI:43474, ChEBI:CHEBI:231935; EC=3.1.3.21;
Evidence={ECO:0000269|PubMed:26755581};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:24338473};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000269|PubMed:24338473};
-!- ACTIVITY REGULATION: Inhibited by orthovanadate, beryllium
trifluoride, Ca(2+) and EDTA. {ECO:0000269|PubMed:24338473}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.42 mM for ADP {ECO:0000269|PubMed:24338473};
KM=1.23 mM for ATP {ECO:0000269|PubMed:24338473};
KM=1.48 mM for GDP {ECO:0000269|PubMed:24338473};
KM=1.47 mM for GTP {ECO:0000269|PubMed:24338473};
KM=1.29 mM for glycerol-3-phosphate
{ECO:0000269|PubMed:26755581};
Vmax=100 nmol/min/mg enzyme with glycerol-3-phosphate as
substrate {ECO:0000269|PubMed:26755581};
Note=Kcat is 0.1 sec(-1) with glycerol-3-phosphate.
{ECO:0000269|PubMed:26755581};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24338473}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression
in testis, heart, skeletal muscle and islet tissue (at protein
level). {ECO:0000269|PubMed:24338473,
ECO:0000269|PubMed:26755581}.
-!- INDUCTION: Up-regulated in white adipose tissue and down-regulated
in brown adipose tissue upon fasting.
{ECO:0000269|PubMed:26755581}.
-!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC040100; AAH40100.1; -; mRNA.
CCDS; CCDS28482.1; -.
RefSeq; NP_080230.2; NM_025954.3.
UniGene; Mm.28541; -.
UniGene; Mm.486259; -.
PDB; 4BKM; X-ray; 2.65 A; A/B/C/D=114-233.
PDBsum; 4BKM; -.
ProteinModelPortal; Q8CHP8; -.
SMR; Q8CHP8; -.
STRING; 10090.ENSMUSP00000052866; -.
iPTMnet; Q8CHP8; -.
PhosphoSitePlus; Q8CHP8; -.
REPRODUCTION-2DPAGE; IPI00380195; -.
REPRODUCTION-2DPAGE; Q8CHP8; -.
EPD; Q8CHP8; -.
MaxQB; Q8CHP8; -.
PaxDb; Q8CHP8; -.
PeptideAtlas; Q8CHP8; -.
PRIDE; Q8CHP8; -.
DNASU; 67078; -.
Ensembl; ENSMUST00000053024; ENSMUSP00000052866; ENSMUSG00000043445.
GeneID; 67078; -.
KEGG; mmu:67078; -.
UCSC; uc008awe.1; mouse.
CTD; 283871; -.
MGI; MGI:1914328; Pgp.
eggNOG; KOG2882; Eukaryota.
eggNOG; COG0647; LUCA.
GeneTree; ENSGT00940000160577; -.
HOGENOM; HOG000068104; -.
HOVERGEN; HBG049429; -.
InParanoid; Q8CHP8; -.
KO; K19269; -.
OMA; VFGTAYC; -.
OrthoDB; EOG091G0I92; -.
PhylomeDB; Q8CHP8; -.
TreeFam; TF314344; -.
BRENDA; 3.1.3.74; 3474.
ChiTaRS; Pgp; mouse.
PRO; PR:Q8CHP8; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000043445; Expressed in 267 organ(s), highest expression level in testis.
Genevisible; Q8CHP8; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0000121; F:glycerol-1-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0043136; F:glycerol-3-phosphatase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IDA:UniProtKB.
GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
GO; GO:0008967; F:phosphoglycolate phosphatase activity; ISO:MGI.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
GO; GO:0006114; P:glycerol biosynthetic process; IDA:UniProtKB.
GO; GO:0006650; P:glycerophospholipid metabolic process; IDA:UniProtKB.
GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
Gene3D; 3.40.50.1000; -; 2.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006357; HAD-SF_hydro_IIA.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006349; PGP_euk.
Pfam; PF13344; Hydrolase_6; 1.
PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
TIGRFAMs; TIGR01452; PGP_euk; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Complete proteome; Hydrolase;
Magnesium; Metal-binding; Protein phosphatase; Reference proteome.
CHAIN 1 321 Glycerol-3-phosphate phosphatase.
/FTId=PRO_0000316889.
ACT_SITE 34 34 Nucleophile.
{ECO:0000269|PubMed:24338473}.
ACT_SITE 36 36 Proton donor. {ECO:0000305}.
METAL 34 34 Magnesium.
{ECO:0000250|UniProtKB:P60487}.
METAL 36 36 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P60487}.
METAL 260 260 Magnesium.
{ECO:0000250|UniProtKB:P60487}.
SITE 204 204 Important for substrate specificity.
{ECO:0000305|PubMed:24338473}.
MUTAGEN 34 34 D->N: Abolishes phosphatase activity.
{ECO:0000269|PubMed:24338473}.
MUTAGEN 41 41 R->N: Slightly increases phosphatase
activity with p-nitrophenylphosphate;
when associated with R-44 and I-45.
{ECO:0000269|PubMed:24338473}.
MUTAGEN 44 44 T->R: Slightly increases phosphatase
activity with p-nitrophenylphosphate;
when associated with N-41 and I-45.
{ECO:0000269|PubMed:24338473}.
MUTAGEN 45 45 A->I: Slightly increases phosphatase
activity with p-nitrophenylphosphate;
when associated with N-41 and R-44.
{ECO:0000269|PubMed:24338473}.
MUTAGEN 67 67 T->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.
{ECO:0000269|PubMed:24338473}.
MUTAGEN 71 71 S->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. {ECO:0000269|PubMed:24338473}.
MUTAGEN 72 72 K->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.
{ECO:0000269|PubMed:24338473}.
MUTAGEN 73 73 T->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.
{ECO:0000269|PubMed:24338473}.
MUTAGEN 204 204 L->H: Strongly increases activity with
pyridoxal phosphate.
{ECO:0000269|PubMed:24338473}.
STRAND 120 125 {ECO:0000244|PDB:4BKM}.
HELIX 127 135 {ECO:0000244|PDB:4BKM}.
STRAND 139 141 {ECO:0000244|PDB:4BKM}.
STRAND 150 152 {ECO:0000244|PDB:4BKM}.
HELIX 153 156 {ECO:0000244|PDB:4BKM}.
STRAND 165 170 {ECO:0000244|PDB:4BKM}.
HELIX 178 187 {ECO:0000244|PDB:4BKM}.
STRAND 193 198 {ECO:0000244|PDB:4BKM}.
STRAND 202 205 {ECO:0000244|PDB:4BKM}.
STRAND 211 213 {ECO:0000244|PDB:4BKM}.
HELIX 215 226 {ECO:0000244|PDB:4BKM}.
SEQUENCE 321 AA; 34541 MW; F083ED0432327A83 CRC64;
MAEAEAGGDE ARCVRLSAER AKLLLAEVDT LLFDCDGVLW RGETAVPGAP ETLRALRARG
KRLGFITNNS SKTRTAYAEK LRRLGFGGPV GPEAGLEVFG TAYCSALYLR QRLAGVPDPK
AYVLGSPALA AELEAVGVTS VGVGPDVLHG DGPSDWLAVP LEPDVRAVVV GFDPHFSYMK
LTKAVRYLQQ PDCLLVGTNM DNRLPLENGR FIAGTGCLVR AVEMAAQRQA DIIGKPSRFI
FDCVSQEYGI NPERTVMVGD RLDTDILLGS TCSLKTILTL TGVSSLEDVK SNQESDCMFK
KKMVPDFYVD SIADLLPALQ G


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