Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P10860

- DHE3_RAT

UniProt

P10860 - DHE3_RAT

Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

Glud1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (04 Apr 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle By similarity. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.By similarity1 Publication

    Catalytic activityi

    L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.PROSITE-ProRule annotation

    Enzyme regulationi

    Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei147 – 1471SubstrateBy similarity
    Binding sitei171 – 1711SubstrateBy similarity
    Binding sitei176 – 1761NADBy similarity
    Active sitei183 – 1831
    Binding sitei252 – 2521NADBy similarity
    Binding sitei266 – 2661GTPBy similarity
    Binding sitei270 – 2701GTPBy similarity
    Binding sitei319 – 3191GTPBy similarity
    Binding sitei322 – 3221GTPBy similarity
    Binding sitei438 – 4381SubstrateBy similarity
    Binding sitei444 – 4441NADBy similarity
    Binding sitei450 – 4501ADPBy similarity
    Binding sitei516 – 5161ADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi141 – 1433NADBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. enzyme binding Source: RGD
    3. glutamate dehydrogenase (NAD+) activity Source: RGD
    4. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB
    5. GTP binding Source: UniProtKB-KW

    GO - Biological processi

    1. glutamate catabolic process Source: RGD
    2. glutamine metabolic process Source: UniProtKB
    3. long-term memory Source: RGD
    4. positive regulation of insulin secretion Source: Ensembl
    5. response to aluminum ion Source: RGD
    6. tricarboxylic acid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    ATP-binding, GTP-binding, NADP, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_214662. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP10860.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
    Short name:
    GDH 1
    Alternative name(s):
    Memory-related gene 2 protein
    Short name:
    MRG-2
    Gene namesi
    Name:Glud1
    Synonyms:Glud
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 16

    Organism-specific databases

    RGDi2708. Glud1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353MitochondrionBy similarityAdd
    BLAST
    Chaini54 – 558505Glutamate dehydrogenase 1, mitochondrialPRO_0000007213Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681N6-succinyllysineBy similarity
    Modified residuei79 – 791PhosphoserineBy similarity
    Modified residuei84 – 841N6-acetyllysine; alternateBy similarity
    Modified residuei84 – 841N6-succinyllysine; alternateBy similarity
    Modified residuei90 – 901N6-acetyllysineBy similarity
    Modified residuei110 – 1101N6-acetyllysine; alternateBy similarity
    Modified residuei110 – 1101N6-succinyllysine; alternateBy similarity
    Modified residuei128 – 1281PhosphoserineBy similarity
    Modified residuei135 – 1351PhosphotyrosineBy similarity
    Modified residuei162 – 1621N6-acetyllysine; alternateBy similarity
    Modified residuei162 – 1621N6-succinyllysine; alternateBy similarity
    Modified residuei171 – 1711N6-acetyllysineBy similarity
    Modified residuei172 – 1721ADP-ribosylcysteineBy similarity
    Modified residuei183 – 1831N6-acetyllysine; alternateBy similarity
    Modified residuei183 – 1831N6-succinyllysine; alternateBy similarity
    Modified residuei187 – 1871N6-acetyllysineBy similarity
    Modified residuei191 – 1911N6-acetyllysine; alternateBy similarity
    Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
    Modified residuei200 – 2001N6-succinyllysineBy similarity
    Modified residuei211 – 2111N6-acetyllysineBy similarity
    Modified residuei326 – 3261N6-acetyllysineBy similarity
    Modified residuei346 – 3461N6-acetyllysine; alternateBy similarity
    Modified residuei346 – 3461N6-succinyllysine; alternateBy similarity
    Modified residuei352 – 3521N6-acetyllysine; alternateBy similarity
    Modified residuei352 – 3521N6-succinyllysine; alternateBy similarity
    Modified residuei363 – 3631N6-acetyllysine; alternateBy similarity
    Modified residuei363 – 3631N6-succinyllysine; alternateBy similarity
    Modified residuei365 – 3651N6-acetyllysine; alternateBy similarity
    Modified residuei365 – 3651N6-succinyllysine; alternateBy similarity
    Modified residuei386 – 3861N6-acetyllysineBy similarity
    Modified residuei390 – 3901N6-acetyllysine; alternateBy similarity
    Modified residuei390 – 3901N6-succinyllysine; alternateBy similarity
    Modified residuei399 – 3991N6-acetyllysineBy similarity
    Modified residuei415 – 4151N6-acetyllysine; alternateBy similarity
    Modified residuei415 – 4151N6-succinyllysine; alternateBy similarity
    Modified residuei457 – 4571N6-acetyllysine; alternateBy similarity
    Modified residuei457 – 4571N6-malonyllysine; alternateBy similarity
    Modified residuei457 – 4571N6-succinyllysine; alternateBy similarity
    Modified residuei477 – 4771N6-acetyllysine; alternateBy similarity
    Modified residuei477 – 4771N6-succinyllysine; alternateBy similarity
    Modified residuei480 – 4801N6-acetyllysine; alternateBy similarity
    Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
    Modified residuei503 – 5031N6-acetyllysine; alternateBy similarity
    Modified residuei503 – 5031N6-malonyllysine; alternateBy similarity
    Modified residuei503 – 5031N6-succinyllysine; alternateBy similarity
    Modified residuei527 – 5271N6-acetyllysine; alternateBy similarity
    Modified residuei527 – 5271N6-malonyllysine; alternateBy similarity
    Modified residuei527 – 5271N6-succinyllysine; alternateBy similarity
    Modified residuei545 – 5451N6-acetyllysine; alternateBy similarity
    Modified residuei545 – 5451N6-succinyllysine; alternateBy similarity
    Modified residuei548 – 5481N6-acetyllysineBy similarity

    Post-translational modificationi

    ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer By similarity.By similarity

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Phosphoprotein

    Proteomic databases

    PaxDbiP10860.
    PRIDEiP10860.

    2D gel databases

    World-2DPAGE0004:P10860.

    PTM databases

    PhosphoSiteiP10860.

    Expressioni

    Tissue specificityi

    Widely expressed throughout the hippocampus. After induction by training, highly expressed in the dentate gyrus, pyrimidal layer and lacunosum molecolare.1 Publication

    Inductioni

    By water maze training in the hippocampus and in other regions of the brain including the laterodorsal nucleus of the thalamus and the cingulate cortex.1 Publication

    Gene expression databases

    GenevestigatoriP10860.

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    BioGridi246566. 1 interaction.
    IntActiP10860. 4 interactions.
    MINTiMINT-2793533.

    Structurei

    3D structure databases

    ProteinModelPortaliP10860.
    SMRiP10860. Positions 63-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0334.
    GeneTreeiENSGT00390000000854.
    HOGENOMiHOG000243801.
    HOVERGENiHBG005479.
    InParanoidiP10860.
    KOiK00261.
    OMAiTCIGVIE.
    OrthoDBiEOG73NG50.
    PhylomeDBiP10860.
    TreeFamiTF313945.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR006095. Glu/Leu/Phe/Val_DH.
    IPR006096. Glu/Leu/Phe/Val_DH_C.
    IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view]
    PRINTSiPR00082. GLFDHDRGNASE.
    SMARTiSM00839. ELFV_dehydrog. 1 hit.
    [Graphical view]
    PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10860-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYRRLGEVLL LSRAGPAALG SAAADSAALL GWARGQPSAV PQPGLTPVAR    50
    RHYSEAATDR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRENEEQKRN 100
    RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI 150
    RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK 200
    ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN 250
    AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGLG 300
    DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED 350
    FKLQHGSILG FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI 400
    IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS 450
    YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPVVPT AEFQDRISGA 500
    SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY 550
    NEAGVTFT 558
    Length:558
    Mass (Da):61,416
    Last modified:April 4, 2006 - v2
    Checksum:i388B8B5490C10F31
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 572AA → GP in CAA32441. (PubMed:2704625)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14223 mRNA. Translation: CAA32441.1.
    X14044 mRNA. Translation: CAA32202.1.
    BC081841 mRNA. Translation: AAH81841.1.
    X64365 Genomic DNA. Translation: CAA45717.1.
    U95148 mRNA. Translation: AAB70012.1.
    PIRiS03707.
    RefSeqiNP_036702.1. NM_012570.2.
    UniGeneiRn.55106.

    Genome annotation databases

    EnsembliENSRNOT00000013788; ENSRNOP00000013789; ENSRNOG00000010222.
    GeneIDi24399.
    KEGGirno:24399.
    UCSCiRGD:2708. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14223 mRNA. Translation: CAA32441.1 .
    X14044 mRNA. Translation: CAA32202.1 .
    BC081841 mRNA. Translation: AAH81841.1 .
    X64365 Genomic DNA. Translation: CAA45717.1 .
    U95148 mRNA. Translation: AAB70012.1 .
    PIRi S03707.
    RefSeqi NP_036702.1. NM_012570.2.
    UniGenei Rn.55106.

    3D structure databases

    ProteinModelPortali P10860.
    SMRi P10860. Positions 63-558.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246566. 1 interaction.
    IntActi P10860. 4 interactions.
    MINTi MINT-2793533.

    Chemistry

    ChEMBLi CHEMBL2176833.

    PTM databases

    PhosphoSitei P10860.

    2D gel databases

    World-2DPAGE 0004:P10860.

    Proteomic databases

    PaxDbi P10860.
    PRIDEi P10860.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000013788 ; ENSRNOP00000013789 ; ENSRNOG00000010222 .
    GeneIDi 24399.
    KEGGi rno:24399.
    UCSCi RGD:2708. rat.

    Organism-specific databases

    CTDi 2746.
    RGDi 2708. Glud1.

    Phylogenomic databases

    eggNOGi COG0334.
    GeneTreei ENSGT00390000000854.
    HOGENOMi HOG000243801.
    HOVERGENi HBG005479.
    InParanoidi P10860.
    KOi K00261.
    OMAi TCIGVIE.
    OrthoDBi EOG73NG50.
    PhylomeDBi P10860.
    TreeFami TF313945.

    Enzyme and pathway databases

    Reactomei REACT_214662. Amino acid synthesis and interconversion (transamination).
    SABIO-RK P10860.

    Miscellaneous databases

    NextBioi 603195.
    PROi P10860.

    Gene expression databases

    Genevestigatori P10860.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR006095. Glu/Leu/Phe/Val_DH.
    IPR006096. Glu/Leu/Phe/Val_DH_C.
    IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00082. GLFDHDRGNASE.
    SMARTi SM00839. ELFV_dehydrog. 1 hit.
    [Graphical view ]
    PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of rat liver glutamate dehydrogenase cDNA."
      Amuro N., Ooki K., Ito A., Goto Y., Okazaki T.
      Nucleic Acids Res. 17:2356-2357(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Liver.
    2. "Nucleotide sequence of rat liver glutamate dehydrogenase cDNA."
      Das A.T., Moerer P., Lamers W.H.
      Nucleic Acids Res. 17:2355-2355(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Liver.
    3. "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: Kidney.
    4. "Isolation and characterization of the rat gene encoding glutamate dehydrogenase."
      Das A.T., Arnberg A.C., Malingre H., Moerer P., Charles R., Moorman A.F.M., Lamers W.H.
      Eur. J. Biochem. 211:795-803(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
      Strain: Wistar.
      Tissue: Liver.
    5. Lubec G., Afjehi-Sadat L., Chen W.-Q.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 108-123; 303-318; 347-363; 400-420; 481-496 AND 504-516, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus and Spinal cord.
    6. "Identification of the CoA-modified forms of mitochondrial acetyl-CoA acetyltransferase and of glutamate dehydrogenase as nearest-neighbour proteins."
      Schwerdt G., Moller U., Huth W.
      Biochem. J. 280:353-357(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 161-190.
    7. "Late memory-related genes in the hippocampus revealed by RNA fingerprinting."
      Cavallaro S., Meiri N., Yi C.-L., Musco S., Ma W., Goldberg J., Alkon D.L.
      Proc. Natl. Acad. Sci. U.S.A. 94:9669-9673(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 431-558, FUNCTION, TISSUE SPECIFICITY, INDUCTION.
      Strain: Wistar.
      Tissue: Hippocampus.

    Entry informationi

    Entry nameiDHE3_RAT
    AccessioniPrimary (citable) accession number: P10860
    Secondary accession number(s): Q66HI8, Q6LC16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 135 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