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P04636

- MDHM_RAT

UniProt

P04636 - MDHM_RAT

Protein

Malate dehydrogenase, mitochondrial

Gene

Mdh2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate + NAD+ = oxaloacetate + NADH.PROSITE-ProRule annotation

    Enzyme regulationi

    Enzyme activity is enhanced by acetylation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571NADBy similarity
    Binding sitei104 – 1041SubstratePROSITE-ProRule annotation
    Binding sitei110 – 1101SubstratePROSITE-ProRule annotation
    Binding sitei117 – 1171NADBy similarity
    Binding sitei142 – 1421SubstratePROSITE-ProRule annotation
    Binding sitei176 – 1761SubstratePROSITE-ProRule annotation
    Active sitei200 – 2001Proton acceptorBy similarity
    Binding sitei251 – 2511NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi31 – 377NADBy similarity
    Nucleotide bindingi140 – 1423NADBy similarity

    GO - Molecular functioni

    1. L-malate dehydrogenase activity Source: RGD
    2. malate dehydrogenase (NADP+) activity Source: RGD
    3. malate dehydrogenase activity Source: RGD
    4. protein binding Source: RGD
    5. protein self-association Source: RGD

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. internal protein amino acid acetylation Source: UniProtKB
    3. malate metabolic process Source: RGD
    4. NADH metabolic process Source: RGD
    5. oxaloacetate metabolic process Source: RGD
    6. tricarboxylic acid cycle Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_216424. Citric acid cycle (TCA cycle).
    REACT_217998. Gluconeogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
    Gene namesi
    Name:Mdh2
    Synonyms:Mor1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 12

    Organism-specific databases

    RGDi619719. Mdh2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. mitochondrial matrix Source: RGD
    3. mitochondrion Source: RGD
    4. nucleus Source: Ensembl
    5. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2424Mitochondrion1 PublicationAdd
    BLAST
    Chaini25 – 338314Malate dehydrogenase, mitochondrialPRO_0000018631Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi33 – 331O-linked (GlcNAc)1 Publication
    Modified residuei78 – 781N6-acetyllysine; alternateBy similarity
    Modified residuei78 – 781N6-succinyllysine; alternateBy similarity
    Modified residuei91 – 911N6-acetyllysine; alternateBy similarity
    Modified residuei91 – 911N6-succinyllysine; alternateBy similarity
    Modified residuei165 – 1651N6-acetyllysineBy similarity
    Modified residuei185 – 1851N6-acetyllysine; alternateBy similarity
    Modified residuei185 – 1851N6-succinyllysine; alternateBy similarity
    Modified residuei203 – 2031N6-succinyllysineBy similarity
    Modified residuei215 – 2151N6-acetyllysine; alternateBy similarity
    Modified residuei215 – 2151N6-succinyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-acetyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-malonyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-succinyllysine; alternateBy similarity
    Modified residuei269 – 2691N6-succinyllysineBy similarity
    Modified residuei296 – 2961N6-acetyllysine; alternateBy similarity
    Modified residuei296 – 2961N6-succinyllysine; alternateBy similarity
    Modified residuei301 – 3011N6-acetyllysine; alternateBy similarity
    Modified residuei301 – 3011N6-succinyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-acetyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-malonyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-succinyllysine; alternateBy similarity
    Modified residuei314 – 3141N6-acetyllysine; alternateBy similarity
    Modified residuei314 – 3141N6-succinyllysine; alternateBy similarity
    Modified residuei324 – 3241N6-acetyllysine; alternateBy similarity
    Modified residuei324 – 3241N6-succinyllysine; alternateBy similarity
    Modified residuei328 – 3281N6-acetyllysine; alternateBy similarity
    Modified residuei328 – 3281N6-succinyllysine; alternateBy similarity
    Modified residuei329 – 3291N6-acetyllysine; alternateBy similarity
    Modified residuei329 – 3291N6-malonyllysine; alternateBy similarity
    Modified residuei335 – 3351N6-acetyllysine; alternateBy similarity
    Modified residuei335 – 3351N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    Acetylation is enhanced by up to 67% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with the appearance of tri-and tetraacetylations. Glucose also increases acetylation by about 60% By similarity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    PaxDbiP04636.
    PRIDEiP04636.

    2D gel databases

    World-2DPAGE0004:P04636.

    PTM databases

    PhosphoSiteiP04636.

    Expressioni

    Tissue specificityi

    Expressed in flagella of epididymal sperm.1 Publication

    Gene expression databases

    GenevestigatoriP04636.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi249687. 1 interaction.
    IntActiP04636. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP04636.
    SMRiP04636. Positions 25-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 1 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0039.
    GeneTreeiENSGT00390000016686.
    HOGENOMiHOG000213792.
    HOVERGENiHBG001662.
    InParanoidiP04636.
    KOiK00026.
    OMAiMVAEAMS.
    OrthoDBiEOG74R1R7.
    PhylomeDBiP04636.
    TreeFamiTF300834.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProiIPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR001252. Malate_DH_AS.
    IPR010097. Malate_DH_type1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11540. PTHR11540. 1 hit.
    PfamiPF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
    PROSITEiPS00068. MDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P04636-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSALARPVG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV    50
    SRLTLYDIAH TPGVAADLSH IETRANVKGY LGPEQLPDCL KGCDVVVIPA 100
    GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPEAMICII SNPVNSTIPI 150
    TAEVFKKHGV YNPNKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH 200
    AGKTIIPLIS QCTPKVDFPQ DQLATLTGRI QEAGTEVVKA KAGAGSATLS 250
    MAYAGARFVF SLVDAMNGKE GVIECSFVQS KETECTYFST PLLLGKKGLE 300
    KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK 338
    Length:338
    Mass (Da):35,684
    Last modified:January 9, 2007 - v2
    Checksum:i13849CCFB78C87E7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti229 – 2291R → K in CAA27812. (PubMed:3755817)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04240 mRNA. Translation: CAA27812.1.
    BC063165 mRNA. Translation: AAH63165.1.
    PIRiA25509. DERTMM.
    RefSeqiNP_112413.2. NM_031151.2.
    UniGeneiRn.1011.

    Genome annotation databases

    EnsembliENSRNOT00000001958; ENSRNOP00000001958; ENSRNOG00000001440.
    GeneIDi81829.
    KEGGirno:81829.
    UCSCiRGD:619719. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04240 mRNA. Translation: CAA27812.1 .
    BC063165 mRNA. Translation: AAH63165.1 .
    PIRi A25509. DERTMM.
    RefSeqi NP_112413.2. NM_031151.2.
    UniGenei Rn.1011.

    3D structure databases

    ProteinModelPortali P04636.
    SMRi P04636. Positions 25-337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249687. 1 interaction.
    IntActi P04636. 2 interactions.

    Chemistry

    ChEMBLi CHEMBL2176835.

    PTM databases

    PhosphoSitei P04636.

    2D gel databases

    World-2DPAGE 0004:P04636.

    Proteomic databases

    PaxDbi P04636.
    PRIDEi P04636.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000001958 ; ENSRNOP00000001958 ; ENSRNOG00000001440 .
    GeneIDi 81829.
    KEGGi rno:81829.
    UCSCi RGD:619719. rat.

    Organism-specific databases

    CTDi 4191.
    RGDi 619719. Mdh2.

    Phylogenomic databases

    eggNOGi COG0039.
    GeneTreei ENSGT00390000016686.
    HOGENOMi HOG000213792.
    HOVERGENi HBG001662.
    InParanoidi P04636.
    KOi K00026.
    OMAi MVAEAMS.
    OrthoDBi EOG74R1R7.
    PhylomeDBi P04636.
    TreeFami TF300834.

    Enzyme and pathway databases

    Reactomei REACT_216424. Citric acid cycle (TCA cycle).
    REACT_217998. Gluconeogenesis.

    Miscellaneous databases

    NextBioi 615775.
    PROi P04636.

    Gene expression databases

    Genevestigatori P04636.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProi IPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR001252. Malate_DH_AS.
    IPR010097. Malate_DH_type1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11540. PTHR11540. 1 hit.
    Pfami PF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    TIGRFAMsi TIGR01772. MDH_euk_gproteo. 1 hit.
    PROSITEi PS00068. MDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and nucleotide sequence of a cDNA clone encoding rat mitochondrial malate dehydrogenase."
      Grant P.M., Tellam J., May V.L., Strauss A.W.
      Nucleic Acids Res. 14:6053-6066(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pituitary anterior lobe.
    3. "Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenase."
      Grant P.M., Roderick S.L., Grant G.A., Banaszak L.J., Strauss A.W.
      Biochemistry 26:128-134(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-338.
    4. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 27-52; 53-74; 166-185; 192-203; 216-239; 242-296 AND 308-324, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain, Hippocampus and Spinal cord.
    5. "Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
      Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
      Reproduction 138:81-93(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
    6. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
      Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
      PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-33.

    Entry informationi

    Entry nameiMDHM_RAT
    AccessioniPrimary (citable) accession number: P04636
    Secondary accession number(s): Q6GSM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3