GRHPR_MOUSE
ID GRHPR_MOUSE Reviewed; 328 AA.
AC Q91Z53;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Glyoxylate reductase/hydroxypyruvate reductase;
DE EC=1.1.1.79;
DE EC=1.1.1.81;
GN Name=Grhpr; Synonyms=Glxr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvEv; TISSUE=Liver;
RA Cramer S.D.;
RT "Identification of the mouse GRHPR cDNA from liver.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 44-58 AND 303-318, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase
CC and D-glycerate dehydrogenase enzymatic activities. Reduces
CC hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-
CC glycerate to hydroxypyruvate (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycolate + NADP(+) = glyoxylate + H(+) + NADPH;
CC Xref=Rhea:RHEA:10992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.79;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH;
CC Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.81;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH;
CC Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.81;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AY113690; AAM52985.1; -; mRNA.
DR EMBL; BC010194; AAH10194.1; -; mRNA.
DR CCDS; CCDS18128.1; -.
DR RefSeq; NP_525028.1; NM_080289.2.
DR AlphaFoldDB; Q91Z53; -.
DR SMR; Q91Z53; -.
DR BioGRID; 218043; 3.
DR STRING; 10090.ENSMUSP00000047218; -.
DR iPTMnet; Q91Z53; -.
DR PhosphoSitePlus; Q91Z53; -.
DR SwissPalm; Q91Z53; -.
DR REPRODUCTION-2DPAGE; Q91Z53; -.
DR EPD; Q91Z53; -.
DR jPOST; Q91Z53; -.
DR MaxQB; Q91Z53; -.
DR PaxDb; Q91Z53; -.
DR PRIDE; Q91Z53; -.
DR ProteomicsDB; 271298; -.
DR Antibodypedia; 11982; 319 antibodies from 27 providers.
DR DNASU; 76238; -.
DR Ensembl; ENSMUST00000045078; ENSMUSP00000047218; ENSMUSG00000035637.
DR GeneID; 76238; -.
DR KEGG; mmu:76238; -.
DR UCSC; uc008ssb.1; mouse.
DR CTD; 9380; -.
DR MGI; MGI:1923488; Grhpr.
DR VEuPathDB; HostDB:ENSMUSG00000035637; -.
DR eggNOG; KOG0069; Eukaryota.
DR GeneTree; ENSGT00940000158578; -.
DR InParanoid; Q91Z53; -.
DR OMA; KMKPNCI; -.
DR OrthoDB; 1378766at2759; -.
DR PhylomeDB; Q91Z53; -.
DR TreeFam; TF324791; -.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR BioGRID-ORCS; 76238; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Grhpr; mouse.
DR PRO; PR:Q91Z53; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91Z53; protein.
DR Bgee; ENSMUSG00000035637; Expressed in left lobe of liver and 253 other tissues.
DR ExpressionAtlas; Q91Z53; baseline and differential.
DR Genevisible; Q91Z53; MM.
DR GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031406; F:carboxylic acid binding; ISO:MGI.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; ISO:MGI.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; ISO:MGI.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; ISO:MGI.
DR GO; GO:0051287; F:NAD binding; ISO:MGI.
DR GO; GO:0050661; F:NADP binding; ISO:MGI.
DR GO; GO:0070402; F:NADPH binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0043648; P:dicarboxylic acid metabolic process; ISO:MGI.
DR GO; GO:0046487; P:glyoxylate metabolic process; ISO:MGI.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..328
FT /note="Glyoxylate reductase/hydroxypyruvate reductase"
FT /id="PRO_0000075945"
FT ACT_SITE 293
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT BINDING 83..84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT BINDING 162..164
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT BINDING 185..188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT BINDING 217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT BINDING 243
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT BINDING 293..296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT BINDING 295
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT SITE 274
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ7"
SQ SEQUENCE 328 AA; 35329 MW; BDEC1ADEC1E18153 CRC64;
MKPARLMKVF VTGPLPAEGR AALAQAADCE VEQWNSDDPI PRKDLEQGVV GAHGLLCRLS
DRVDKKLLDA AGANLRVIST LSVGVDHLAL DEIKKRGIRV GYTPGVLTDA TAELAVSLLL
TTCRRLPEAI EEVKNGGWSS WSPLWMCGYG LSQSTVGIVG LGRIGQAIAR RLKPFGVQRF
LYTGRQPRPQ EAAEFQAEFV PIAQLAAESD FIVVSCSLTP DTMGLCSKDF FQKMKNTAIF
INISRGDVVN QEDLYQALAS GQIAAAGLDV TTPEPLPPSH PLLTLKNCVI LPHIGSATYK
TRNTMSLLAA NNLLAGLRGE AMPSELKL
