GenomeNet

Database: RefSeq
Entry: NP_150238
LinkDB: NP_150238
Original site: NP_150238 
LOCUS       NP_150238                334 aa            linear   ROD 22-DEC-2017
DEFINITION  malate dehydrogenase, cytoplasmic isoform Mdh1 [Rattus norvegicus].
ACCESSION   NP_150238
VERSION     NP_150238.1
DBSOURCE    REFSEQ: accession NM_033235.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Stiebler AC, Freitag J, Schink KO, Stehlik T, Tillmann BA, Ast J
            and Bolker M.
  TITLE     Ribosomal readthrough at a short UGA stop codon context triggers
            dual localization of metabolic enzymes in Fungi and animals
  JOURNAL   PLoS Genet. 10 (10), e1004685 (2014)
   PUBMED   25340584
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Bohm D, Keller K, Pieter J, Boehm N, Wolters D, Siggelkow W,
            Lebrecht A, Schmidt M, Kolbl H, Pfeiffer N and Grus FH.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol. Rep. 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Gonzales PA, Pisitkun T, Hoffert JD, Tchapyjnikov D, Star RA, Kleta
            R, Wang NS and Knepper MA.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J. Am. Soc. Nephrol. 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Ying W.
  TITLE     NAD+/NADH and NADP+/NADPH in cellular functions and cell death:
            regulation and biological consequences
  JOURNAL   Antioxid. Redox Signal. 10 (2), 179-206 (2008)
   PUBMED   18020963
  REMARK    Review article
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Werner HB, Kuhlmann K, Shen S, Uecker M, Schardt A, Dimova K,
            Orfaniotou F, Dhaunchak A, Brinkmann BG, Mobius W, Guarente L,
            Casaccia-Bonnefil P, Jahn O and Nave KA.
  TITLE     Proteolipid protein is required for transport of sirtuin 2 into CNS
            myelin
  JOURNAL   J. Neurosci. 27 (29), 7717-7730 (2007)
   PUBMED   17634366
REFERENCE   6  (residues 1 to 334)
  AUTHORS   McKenna MC, Waagepetersen HS, Schousboe A and Sonnewald U.
  TITLE     Neuronal and astrocytic shuttle mechanisms for
            cytosolic-mitochondrial transfer of reducing equivalents: current
            evidence and pharmacological tools
  JOURNAL   Biochem. Pharmacol. 71 (4), 399-407 (2006)
   PUBMED   16368075
  REMARK    Review article
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Navarro-Lerida I, Martinez Moreno M, Roncal F, Gavilanes F, Albar
            JP and Rodriguez-Crespo I.
  TITLE     Proteomic identification of brain proteins that interact with
            dynein light chain LC8
  JOURNAL   Proteomics 4 (2), 339-346 (2004)
   PUBMED   14760703
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Tan C, Tuch BE, Tu J and Brown SA.
  TITLE     Role of NADH shuttles in glucose-induced insulin secretion from
            fetal beta-cells
  JOURNAL   Diabetes 51 (10), 2989-2996 (2002)
   PUBMED   12351438
  REMARK    Erratum:[Diabetes 2003 Jan;52(1):224]
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Beier H and Grimm M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res. 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Smit MJ, Duursma AM, Bouma JM and Gruber M.
  TITLE     Receptor-mediated endocytosis of lactate dehydrogenase M4 by liver
            macrophages: a mechanism for elimination of enzymes from plasma.
            Evidence for competition by creatine kinase MM, adenylate kinase,
            malate, and alcohol dehydrogenase
  JOURNAL   J. Biol. Chem. 262 (27), 13020-13026 (1987)
   PUBMED   2820961
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FM081843.1, FN799180.1,
            FM055335.1, FM085125.1, FM108375.1 and FM086546.1.
            
            Summary: This gene encodes an enzyme that catalyzes the
            NAD/NADH-dependent, reversible oxidation of malate to oxaloacetate
            in many metabolic pathways, including the citric acid cycle. Two
            main isozymes are known to exist in eukaryotic cells: one is found
            in the mitochondrial matrix and the other in the cytoplasm. This
            gene encodes the cytosolic isozyme, which plays a key role in the
            malate-aspartate shuttle that allows malate to pass through the
            mitochondrial membrane to be transformed into oxaloacetate for
            further cellular processes. A recent study showed that a
            C-terminally extended isoform is produced by use of an alternative
            in-frame translation termination codon via a stop codon readthrough
            mechanism, and that this isoform is localized in the peroxisomes.
            [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This transcript (1) encodes two isoforms, which
            result from the use of alternative in-frame translation termination
            codons. The shorter isoform (Mdh1) results from translation
            termination at the upstream UGA stop codon, while the longer
            isoform (Mdh1x) results from UGA stop codon readthrough to the
            downstream UGA termination codon. This RefSeq represents the
            shorter isoform (Mdh1), which is localized in the cytosol.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ215603.1, FQ217819.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00052296, SAMD00052297
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q22"
     Protein         1..334
                     /product="malate dehydrogenase, cytoplasmic isoform Mdh1"
                     /EC_number="1.1.1.37"
                     /note="malate dehydrogenase, soluble; malate
                     dehydrogenase, cytoplasmic; cytosolic malate
                     dehydrogenase; Malate dehydrogenase-like enzyme; malate
                     dehydrogenase 1, NAD (soluble); malate dehydrogenase,
                     peroxisomal"
                     /calculated_mol_wt=36352
     Region          2..327
                     /region_name="MalateDH-SF1"
                     /note="malate dehydrogenase; TIGR01759"
                     /db_xref="CDD:130820"
     Site            2
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N-acetylserine. {ECO:0000250|UniProtKB:P40925};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     Region          3..328
                     /region_name="MDH_cytoplasmic_cytosolic"
                     /note="Cytoplasmic and cytosolic Malate dehydrogenases;
                     cd01336"
                     /db_xref="CDD:133421"
     Site            order(11,13..16,42,87..90,108,129,131,155,187,241)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133421"
     Site            order(18,55..56,58..60,161..162,165,230,233,237..238,
                     242..245,248)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133421"
     Site            order(92,98,131,158,162,187,235,242)
                     /site_type="other"
                     /note="malate binding site [chemical binding]"
                     /db_xref="CDD:133421"
     Site            110
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine. {ECO:0000250|UniProtKB:P14152};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     Site            118
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine. {ECO:0000250|UniProtKB:P40925};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     Site            121
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine. {ECO:0000250|UniProtKB:P40925};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     Site            214
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine. {ECO:0000250|UniProtKB:P14152};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     Site            217
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:22673903};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     Site            230
                     /site_type="methylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Omega-N-methylarginine.
                     {ECO:0000250|UniProtKB:P14152}; propagated from
                     UniProtKB/Swiss-Prot (O88989.3)"
     Site            241
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:22673903};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     Site            298
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine, alternate.
                     {ECO:0000250|UniProtKB:P40925}; propagated from
                     UniProtKB/Swiss-Prot (O88989.3)"
     Site            298
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine, alternate.
                     {ECO:0000250|UniProtKB:P14152}; propagated from
                     UniProtKB/Swiss-Prot (O88989.3)"
     Site            309
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000250|UniProtKB:P14152};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     Site            318
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine. {ECO:0000250|UniProtKB:P14152};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     Site            332
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:22673903};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     Site            333
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:22673903};
                     propagated from UniProtKB/Swiss-Prot (O88989.3)"
     CDS             1..334
                     /gene="Mdh1"
                     /gene_synonym="Mdhl; MDL1; Mor2"
                     /coded_by="NM_033235.2:78..1082"
                     /note="isoform Mdh1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24551"
                     /db_xref="RGD:3072"
ORIGIN      
        1 msepirvlvt gaagqiaysl lysigngsvf gkdqpiilvl lditpmmgvl dgvlmelqdc
       61 alpllqdvia tdkeevafkd ldvavlvgsm prregmerkd llkanvkifk sqgaalekya
      121 kksvkvivvg npantnclta sksapsipke nfscltrldh nraksqialk lgvtaddvkn
      181 viiwgnhsst qypdvnhakv klqgkevgvy ealkddswlk gefittvqqr gaavikarkl
      241 ssamsaakai sdhirdiwfg tpegefvsmg visdgnsygv pddllysfpv viknktwkfv
      301 eglpindfsr ekmdltakel teeketafef lssa
//
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