GenomeNet

Database: RefSeq
Entry: NP_525028
LinkDB: NP_525028
Original site: NP_525028 
LOCUS       NP_525028                328 aa            linear   ROD 27-APR-2025
DEFINITION  glyoxylate reductase/hydroxypyruvate reductase isoform 1 [Mus
            musculus].
ACCESSION   NP_525028
VERSION     NP_525028.1
DBSOURCE    REFSEQ: accession NM_080289.2
KEYWORDS    RefSeq; RefSeq Select.
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   Buchalski,B., Wood,K.D., Challa,A., Fargue,S., Holmes,R.P.,
            Lowther,W.T. and Knight,J.
  TITLE     The effects of the inactivation of Hydroxyproline dehydrogenase on
            urinary oxalate and glycolate excretion in mouse models of primary
            hyperoxaluria
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1866 (3), 165633 (2020)
   PUBMED   31821850
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Wood,K.D., Holmes,R.P., Erbe,D., Liebow,A., Fargue,S. and Knight,J.
  TITLE     Reduction in urinary oxalate excretion in mouse models of Primary
            Hyperoxaluria by RNA interference inhibition of liver lactate
            dehydrogenase activity
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1865 (9), 2203-2209 (2019)
   PUBMED   31055082
REFERENCE   3  (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   4  (residues 1 to 328)
  AUTHORS   Li,X., Knight,J., Fargue,S., Buchalski,B., Guan,Z., Inscho,E.W.,
            Liebow,A., Fitzgerald,K., Querbes,W., Todd Lowther,W. and
            Holmes,R.P.
  TITLE     Metabolism of (13)C5-hydroxyproline in mouse models of Primary
            Hyperoxaluria and its inhibition by RNAi therapeutics targeting
            liver glycolate oxidase and hydroxyproline dehydrogenase
  JOURNAL   Biochim Biophys Acta 1862 (2), 233-239 (2016)
   PUBMED   26655602
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Knight,J., Holmes,R.P., Cramer,S.D., 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   6  (residues 1 to 328)
  AUTHORS   Genolet,R., Kersten,S., Braissant,O., Mandard,S., Tan,N.S.,
            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 :: BC010194.1, AY113690.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 23.65 cM"
     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          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"
                     /note="Phosphoserine.
                     /evidence=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"
     Site            274
                     /site_type="other"
                     /note="Raises pKa of active site His.
                     /evidence=ECO:0000250|UniProtKB:Q9UBQ7; propagated from
                     UniProtKB/Swiss-Prot (Q91Z53.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=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
//
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