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P10860

- DHE3_RAT

UniProt

P10860 - DHE3_RAT

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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene
Glud1, Glud
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

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

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.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi141 – 1433NAD By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 572AA → GP in CAA32441. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 134 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

Similar proteinsi