PGP_BOVIN
ID PGP_BOVIN Reviewed; 321 AA.
AC Q2T9S4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Glycerol-3-phosphate phosphatase {ECO:0000305};
DE Short=G3PP {ECO:0000250|UniProtKB:Q8CHP8};
DE EC=3.1.3.21 {ECO:0000250|UniProtKB:Q8CHP8};
DE AltName: Full=Aspartate-based ubiquitous Mg(2+)-dependent phosphatase {ECO:0000250|UniProtKB:Q8CHP8};
DE Short=AUM {ECO:0000250|UniProtKB:Q8CHP8};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q8CHP8};
DE AltName: Full=Phosphoglycolate phosphatase {ECO:0000250|UniProtKB:Q8CHP8};
DE Short=PGP {ECO:0000250|UniProtKB:Q8CHP8};
GN Name=PGP {ECO:0000250|UniProtKB:A6NDG6};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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. In vitro, has also a
CC phosphatase activity toward ADP, ATP, GDP and GTP.
CC {ECO:0000250|UniProtKB:A6NDG6, ECO:0000250|UniProtKB:Q8CHP8}.
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:0000250|UniProtKB:Q8CHP8};
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:0000250|UniProtKB:Q8CHP8};
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8CHP8}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; BC111291; AAI11292.1; -; mRNA.
DR RefSeq; NP_001033261.1; NM_001038172.2.
DR AlphaFoldDB; Q2T9S4; -.
DR SMR; Q2T9S4; -.
DR STRING; 9913.ENSBTAP00000013127; -.
DR PaxDb; Q2T9S4; -.
DR PRIDE; Q2T9S4; -.
DR Ensembl; ENSBTAT00000013127; ENSBTAP00000013127; ENSBTAG00000009951.
DR GeneID; 538173; -.
DR KEGG; bta:538173; -.
DR CTD; 283871; -.
DR VEuPathDB; HostDB:ENSBTAG00000009951; -.
DR VGNC; VGNC:32798; PGP.
DR eggNOG; KOG2882; Eukaryota.
DR GeneTree; ENSGT00940000160577; -.
DR HOGENOM; CLU_043473_0_1_1; -.
DR InParanoid; Q2T9S4; -.
DR OMA; PPMHRET; -.
DR OrthoDB; 982374at2759; -.
DR TreeFam; TF314344; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000009951; Expressed in infraspinatus muscle and 106 other tissues.
DR ExpressionAtlas; Q2T9S4; baseline and differential.
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; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; ISS:UniProtKB.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS: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 2: Evidence at transcript 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_0000316887"
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; 34320 MW; 209E64F8BF5B9E1F CRC64;
MAEAEAGGDD GRCVRLNAER AQALLADVDT LLFDCDGVLW RGETAVPGAP ETLTALRARG
KRLAFITNNS SKTREAYAEK LRCLGFGAPA GPDAGREVFG TAYCTALYLR QRLTGPPAPK
AYVLGSVALA AELEAVGVSC VGVGPEPLLG DGPGAWLDAP LEPDVRAVVV GFDPHFSYMK
LTKAVRYLQQ PDCLLVGTNM DNRLPLENGR FIAGTGCLVR AVEMAAQRQA DIIGKPSRFI
FDCVSQEYGI HPERTVMVGD RLDTDILLGV TCGLKTILTL TGVSSLRDVK SNQESDCMAK
KKMVPDFYVD SIADLLPALQ G
