LOCUS NP_525028 328 aa linear ROD 25-FEB-2019
DEFINITION glyoxylate reductase/hydroxypyruvate reductase isoform 1 [Mus
musculus].
ACCESSION NP_525028
VERSION NP_525028.1
DBSOURCE REFSEQ: accession NM_080289.2
KEYWORDS RefSeq.
SOURCE Mus musculus (house mouse)
ORGANISM Mus musculus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE 1 (residues 1 to 328)
AUTHORS Zong C, Nie X, Zhang D, Ji Q, Qin Y, Wang L, Jiang D, Gong C, Liu Y
and Zhou G.
TITLE Up regulation of glyoxylate reductase/hydroxypyruvate reductase
(GRHPR) is associated with intestinal epithelial cells apoptosis in
TNBS-induced experimental colitis
JOURNAL Pathol. Res. Pract. 212 (5), 365-371 (2016)
PUBMED 26997491
REMARK GeneRIF: These data suggested that GRHPR might exert its
pro-apoptosis function in intestinal epithelial cells. Thus, GRHPR
might play an important role in regulating IECs apoptosis, and
might be a potential therapeutic target for Crohn's disease.
REFERENCE 2 (residues 1 to 328)
AUTHORS Knight J, Holmes RP, Cramer SD, Takayama T and Salido E.
TITLE Hydroxyproline metabolism in mouse models of primary hyperoxaluria
JOURNAL Am. J. Physiol. Renal Physiol. 302 (6), F688-F693 (2012)
PUBMED 22189945
REFERENCE 3 (residues 1 to 328)
AUTHORS Genolet R, Kersten S, Braissant O, Mandard S, Tan NS, Bucher P,
Desvergne B, Michalik L and Wahli W.
TITLE Promoter rearrangements cause species-specific hepatic regulation
of the glyoxylate reductase/hydroxypyruvate reductase gene by the
peroxisome proliferator-activated receptor alpha
JOURNAL J. Biol. Chem. 280 (25), 24143-24152 (2005)
PUBMED 15840574
REMARK GeneRIF: data indicate a species-specific regulation by PPARalpha
of GRHPR, a key gene of the glyoxylate cycle
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AK004307.1, BB869843.1,
CF738475.1 and AL824706.8.
Summary: This gene encodes a member of the D-isomer specific
2-hydroxyacid dehydrogenase family of proteins. The encoded protein
catalyzes three enzymatic reactions: the conversion of
hydroxypyruvate to D-glycerate as well as the reverse reaction, and
the conversion of glyoxylate to glycolate. Homozygous knockout mice
exhibit elevated synthesis of oxalate and glycerate. [provided by
RefSeq, Aug 2015].
Transcript Variant: This variant (1) represents the longer
transcript and encodes the longer isoform (1).
##Evidence-Data-START##
Transcript exon combination :: SRR1660817.421369.1, BC010194.1
[ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMN00849374, SAMN00849375
[ECO:0000348]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..328
/organism="Mus musculus"
/strain="C57BL/6"
/db_xref="taxon:10090"
/chromosome="4"
/map="4"
Protein 1..328
/product="glyoxylate reductase/hydroxypyruvate reductase
isoform 1"
/EC_number="1.1.1.79"
/EC_number="1.1.1.81"
/calculated_mol_wt=35198
Region 1..327
/region_name="LdhA"
/note="Lactate dehydrogenase or related 2-hydroxyacid
dehydrogenase [Energy production and conversion, Coenzyme
transport and metabolism, General function prediction
only]; COG1052"
/db_xref="CDD:223980"
Region 7..319
/region_name="GDH"
/note="D-glycerate dehydrogenase/hydroxypyruvate reductase
(GDH); cd05301"
/db_xref="CDD:240626"
Site order(13..14,16,58..60,81,109..110,113..114,116..117,120,
124,126,134,136,138,140..146,148..152,170..171,174..175,
274..275,283,289..295,297..300,302)
/site_type="other"
/note="dimerization interface [polypeptide binding]"
/db_xref="CDD:240626"
Site 36
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/note="Phosphoserine. {ECO:0000250|UniProtKB:Q9UBQ7};
propagated from UniProtKB/Swiss-Prot (Q91Z53.1)"
Site order(59,82..84,107,245,293,296)
/site_type="other"
/note="ligand binding site [chemical binding]"
/db_xref="CDD:240626"
Site order(83..84,111,160..164,183..185,188,215..217,221..222,
243..245,269..270,293,295..296)
/site_type="other"
/note="NADP binding site [chemical binding]"
/db_xref="CDD:240626"
Region 83..84
/region_name="Substrate binding.
{ECO:0000250|UniProtKB:Q9UBQ7}"
/experiment="experimental evidence, no additional details
recorded"
/note="propagated from UniProtKB/Swiss-Prot (Q91Z53.1)"
Site order(245,274,293)
/site_type="active"
/note="catalytic site [active]"
/db_xref="CDD:240626"
Site 274
/site_type="other"
/experiment="experimental evidence, no additional details
recorded"
/note="Raises pKa of active site His.
{ECO:0000250|UniProtKB:Q9UBQ7}; propagated from
UniProtKB/Swiss-Prot (Q91Z53.1)"
Region 293..296
/region_name="Substrate binding.
{ECO:0000250|UniProtKB:Q9UBQ7}"
/experiment="experimental evidence, no additional details
recorded"
/note="propagated from UniProtKB/Swiss-Prot (Q91Z53.1)"
Site 298
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/note="Phosphothreonine. {ECO:0000250|UniProtKB:Q9UBQ7};
propagated from UniProtKB/Swiss-Prot (Q91Z53.1)"
CDS 1..328
/gene="Grhpr"
/gene_synonym="1110059D05Rik; 6430629L09Rik; Glxr"
/coded_by="NM_080289.2:59..1045"
/note="isoform 1 is encoded by transcript variant 1"
/db_xref="CCDS:CCDS18128.1"
/db_xref="GeneID:76238"
/db_xref="MGI:MGI:1923488"
ORIGIN
1 mkparlmkvf vtgplpaegr aalaqaadce veqwnsddpi prkdleqgvv gahgllcrls
61 drvdkkllda aganlrvist lsvgvdhlal deikkrgirv gytpgvltda taelavslll
121 ttcrrlpeai eevknggwss wsplwmcgyg lsqstvgivg lgrigqaiar rlkpfgvqrf
181 lytgrqprpq eaaefqaefv piaqlaaesd fivvscsltp dtmglcskdf fqkmkntaif
241 inisrgdvvn qedlyqalas gqiaaagldv ttpeplppsh plltlkncvi lphigsatyk
301 trntmsllaa nnllaglrge ampselkl
//
