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P08249

- MDHM_MOUSE

UniProt

P08249 - MDHM_MOUSE

Protein

Malate dehydrogenase, mitochondrial

Gene

Mdh2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (01 May 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 – 1041Substrate
    Binding sitei110 – 1101Substrate
    Binding sitei117 – 1171NADBy similarity
    Binding sitei142 – 1421Substrate
    Binding sitei176 – 1761Substrate
    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: MGI
    2. malate dehydrogenase (NADP+) activity Source: Ensembl
    3. malate dehydrogenase activity Source: MGI

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
    Gene namesi
    Name:Mdh2
    Synonyms:Mor1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:97050. Mdh2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. mitochondrion Source: MGI
    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 – 2424MitochondrionAdd
    BLAST
    Chaini25 – 338314Malate dehydrogenase, mitochondrialPRO_0000018629Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi33 – 331O-linked (GlcNAc)By similarity
    Modified residuei78 – 781N6-acetyllysine; alternate1 Publication
    Modified residuei78 – 781N6-succinyllysine; alternate1 Publication
    Modified residuei91 – 911N6-acetyllysine; alternate1 Publication
    Modified residuei91 – 911N6-succinyllysine; alternate1 Publication
    Modified residuei165 – 1651N6-acetyllysine1 Publication
    Modified residuei185 – 1851N6-acetyllysine; alternate1 Publication
    Modified residuei185 – 1851N6-succinyllysine; alternate1 Publication
    Modified residuei203 – 2031N6-succinyllysine1 Publication
    Modified residuei215 – 2151N6-acetyllysine; alternate1 Publication
    Modified residuei215 – 2151N6-succinyllysine; alternate1 Publication
    Modified residuei239 – 2391N6-acetyllysine; alternate2 Publications
    Modified residuei239 – 2391N6-malonyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-succinyllysine; alternate1 Publication
    Modified residuei269 – 2691N6-succinyllysine1 Publication
    Modified residuei296 – 2961N6-acetyllysine; alternate1 Publication
    Modified residuei296 – 2961N6-succinyllysine; alternate1 Publication
    Modified residuei301 – 3011N6-acetyllysine; alternate1 Publication
    Modified residuei301 – 3011N6-succinyllysine; alternate1 Publication
    Modified residuei307 – 3071N6-acetyllysine; alternate1 Publication
    Modified residuei307 – 3071N6-malonyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-succinyllysine; alternate1 Publication
    Modified residuei314 – 3141N6-acetyllysine; alternate1 Publication
    Modified residuei314 – 3141N6-succinyllysine; alternate1 Publication
    Modified residuei324 – 3241N6-acetyllysine; alternate1 Publication
    Modified residuei324 – 3241N6-succinyllysine; alternate1 Publication
    Modified residuei328 – 3281N6-acetyllysine; alternateBy similarity
    Modified residuei328 – 3281N6-succinyllysine; alternateBy similarity
    Modified residuei329 – 3291N6-acetyllysine; alternate1 Publication
    Modified residuei329 – 3291N6-malonyllysine; alternateBy similarity
    Modified residuei335 – 3351N6-acetyllysine; alternate1 Publication
    Modified residuei335 – 3351N6-succinyllysine; alternate1 Publication

    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. Acetylation of Lys-239 and Lys-314 is observed in liver mitochondria from fasted mice but not from fed mice.By similarity2 Publications

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    MaxQBiP08249.
    PaxDbiP08249.
    PRIDEiP08249.

    2D gel databases

    REPRODUCTION-2DPAGEP08249.
    SWISS-2DPAGEP08249.
    UCD-2DPAGEP08249.

    PTM databases

    PhosphoSiteiP08249.

    Expressioni

    Gene expression databases

    ArrayExpressiP08249.
    BgeeiP08249.
    CleanExiMM_MDH2.
    GenevestigatoriP08249.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi201467. 3 interactions.
    IntActiP08249. 7 interactions.
    MINTiMINT-4101644.

    Structurei

    3D structure databases

    ProteinModelPortaliP08249.
    SMRiP08249. 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.
    InParanoidiP08249.
    KOiK00026.
    OMAiVEVKGFA.
    OrthoDBiEOG74R1R7.
    PhylomeDBiP08249.
    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.

    P08249-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSALARPAG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV    50
    SRLTLYDIAH TPGVAADLSH IETRANVKGY LGPEQLPDCL KGCDVVVIPA 100
    GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPEAMVCII ANPVNSTIPI 150
    TAEVFKKHGV YNPNKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH 200
    AGKTIIPLIS QCTPKVDFPQ DQLATLTGRI QEAGTEVVKA KAGAGSATLS 250
    MAYAGARFVF SLVDAMNGKE GVVECSFVQS KETECTYFST PLLLGKKGLE 300
    KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK 338
    Length:338
    Mass (Da):35,611
    Last modified:May 1, 2007 - v3
    Checksum:i99D13BB2099C19F1
    GO

    Sequence cautioni

    The sequence BAC24986.1 differs from that shown. Reason: Frameshift at position 39.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761N → K in AAA39509. (PubMed:3038184)Curated
    Sequence conflicti269 – 2691K → L in AAA39509. (PubMed:3038184)Curated
    Sequence conflicti269 – 2691K → L in CAA30274. (PubMed:3379635)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16229 mRNA. Translation: AAA39509.1.
    X07295
    , X07296, X07297, X07298, X07299, X07300, X07301 Genomic DNA. Translation: CAA30274.1.
    AK002305 mRNA. Translation: BAC24986.1. Frameshift.
    AK167809 mRNA. Translation: BAE39836.1.
    AK160553 mRNA. Translation: BAE35869.1.
    AK135162 mRNA. Translation: BAE22447.1.
    BC023482 mRNA. Translation: AAH23482.1.
    DQ402950 mRNA. Translation: ABD77283.1.
    CCDSiCCDS19746.1.
    PIRiS01350. DEMSMM.
    RefSeqiNP_032643.2. NM_008617.2.
    UniGeneiMm.297096.

    Genome annotation databases

    EnsembliENSMUST00000019323; ENSMUSP00000019323; ENSMUSG00000019179.
    GeneIDi17448.
    KEGGimmu:17448.
    UCSCiuc008zyz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16229 mRNA. Translation: AAA39509.1 .
    X07295
    , X07296 , X07297 , X07298 , X07299 , X07300 , X07301 Genomic DNA. Translation: CAA30274.1 .
    AK002305 mRNA. Translation: BAC24986.1 . Frameshift.
    AK167809 mRNA. Translation: BAE39836.1 .
    AK160553 mRNA. Translation: BAE35869.1 .
    AK135162 mRNA. Translation: BAE22447.1 .
    BC023482 mRNA. Translation: AAH23482.1 .
    DQ402950 mRNA. Translation: ABD77283.1 .
    CCDSi CCDS19746.1.
    PIRi S01350. DEMSMM.
    RefSeqi NP_032643.2. NM_008617.2.
    UniGenei Mm.297096.

    3D structure databases

    ProteinModelPortali P08249.
    SMRi P08249. Positions 25-337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201467. 3 interactions.
    IntActi P08249. 7 interactions.
    MINTi MINT-4101644.

    PTM databases

    PhosphoSitei P08249.

    2D gel databases

    REPRODUCTION-2DPAGE P08249.
    SWISS-2DPAGE P08249.
    UCD-2DPAGE P08249.

    Proteomic databases

    MaxQBi P08249.
    PaxDbi P08249.
    PRIDEi P08249.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000019323 ; ENSMUSP00000019323 ; ENSMUSG00000019179 .
    GeneIDi 17448.
    KEGGi mmu:17448.
    UCSCi uc008zyz.1. mouse.

    Organism-specific databases

    CTDi 4191.
    MGIi MGI:97050. Mdh2.

    Phylogenomic databases

    eggNOGi COG0039.
    GeneTreei ENSGT00390000016686.
    HOGENOMi HOG000213792.
    HOVERGENi HBG001662.
    InParanoidi P08249.
    KOi K00026.
    OMAi VEVKGFA.
    OrthoDBi EOG74R1R7.
    PhylomeDBi P08249.
    TreeFami TF300834.

    Miscellaneous databases

    ChiTaRSi Mdh2. mouse.
    NextBioi 292084.
    PROi P08249.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08249.
    Bgeei P08249.
    CleanExi MM_MDH2.
    Genevestigatori P08249.

    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. "Cloning and sequence analysis of cDNAs encoding mammalian mitochondrial malate dehydrogenase."
      Joh T., Takeshima H., Tsuzuki T., Shimada K., Tanase S., Morino Y.
      Biochemistry 26:2515-2520(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural organization of the mouse mitochondrial malate dehydrogenase gene."
      Takeshima H., Joh T., Tsuzuki T., Shimada K., Matsukado Y.
      J. Mol. Biol. 200:1-11(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c and C57BL/6J.
      Tissue: Cerebellum and Kidney.
    4. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    5. "Housekeeping genes for phylogenetic analysis of eutherian relationships."
      Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
      Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-322.
      Tissue: Liver.
    6. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 27-45; 53-74; 79-104; 166-185; 192-239; 242-257; 282-296 AND 308-324, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-91; LYS-185; LYS-203; LYS-215; LYS-239; LYS-269; LYS-296; LYS-301; LYS-307; LYS-314; LYS-324 AND LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    8. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-91; LYS-165; LYS-185; LYS-215; LYS-239; LYS-296; LYS-301; LYS-307; LYS-314; LYS-324; LYS-329 AND LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiMDHM_MOUSE
    AccessioniPrimary (citable) accession number: P08249
    Secondary accession number(s): Q0QF44, Q8CF79, Q8R1P0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 3 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3