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P10860 (DHE3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate dehydrogenase 1, mitochondrial

Short name=GDH 1
EC=1.4.1.3
Alternative name(s):
Memory-related gene 2 protein
Short name=MRG-2
Gene names
Name:Glud1
Synonyms:Glud
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Catalytic activity

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

Enzyme regulation

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.

Subunit structure

Homohexamer.

Subcellular location

Mitochondrion matrix.

Tissue specificity

Widely expressed throughout the hippocampus. After induction by training, highly expressed in the dentate gyrus, pyrimidal layer and lacunosum molecolare. Ref.7

Induction

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. Ref.7

Post-translational modification

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.

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
GTP-binding
NADP
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMAcetylation
ADP-ribosylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglutamate catabolic process

Traceable author statement PubMed 12684230. Source: RGD

glutamine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

long-term memory

Inferred from expression pattern Ref.7. Source: RGD

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

response to aluminum ion

Inferred from direct assay PubMed 10806405. Source: RGD

tricarboxylic acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 15273247. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme binding

Inferred from physical interaction Ref.6. Source: RGD

glutamate dehydrogenase (NAD+) activity

Inferred from direct assay PubMed 15273247. Source: RGD

glutamate dehydrogenase [NAD(P)+] activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Mitochondrion By similarity
Chain54 – 558505Glutamate dehydrogenase 1, mitochondrial
PRO_0000007213

Regions

Nucleotide binding141 – 1433NAD By similarity

Sites

Active site1831
Binding site1471Substrate By similarity
Binding site1711Substrate By similarity
Binding site1761NAD By similarity
Binding site2521NAD By similarity
Binding site2661GTP By similarity
Binding site2701GTP By similarity
Binding site3191GTP By similarity
Binding site3221GTP By similarity
Binding site4381Substrate By similarity
Binding site4441NAD By similarity
Binding site4501ADP By similarity
Binding site5161ADP By similarity

Amino acid modifications

Modified residue681N6-succinyllysine By similarity
Modified residue791Phosphoserine By similarity
Modified residue841N6-acetyllysine; alternate By similarity
Modified residue841N6-succinyllysine; alternate By similarity
Modified residue901N6-acetyllysine By similarity
Modified residue1101N6-acetyllysine; alternate By similarity
Modified residue1101N6-succinyllysine; alternate By similarity
Modified residue1281Phosphoserine By similarity
Modified residue1351Phosphotyrosine By similarity
Modified residue1621N6-acetyllysine; alternate By similarity
Modified residue1621N6-succinyllysine; alternate By similarity
Modified residue1711N6-acetyllysine By similarity
Modified residue1721ADP-ribosylcysteine By similarity
Modified residue1831N6-acetyllysine; alternate By similarity
Modified residue1831N6-succinyllysine; alternate By similarity
Modified residue1871N6-acetyllysine By similarity
Modified residue1911N6-acetyllysine; alternate By similarity
Modified residue1911N6-succinyllysine; alternate By similarity
Modified residue2001N6-succinyllysine By similarity
Modified residue2111N6-acetyllysine By similarity
Modified residue3261N6-acetyllysine By similarity
Modified residue3461N6-acetyllysine; alternate By similarity
Modified residue3461N6-succinyllysine; alternate By similarity
Modified residue3521N6-acetyllysine; alternate By similarity
Modified residue3521N6-succinyllysine; alternate By similarity
Modified residue3631N6-acetyllysine; alternate By similarity
Modified residue3631N6-succinyllysine; alternate By similarity
Modified residue3651N6-acetyllysine; alternate By similarity
Modified residue3651N6-succinyllysine; alternate By similarity
Modified residue3861N6-acetyllysine By similarity
Modified residue3901N6-acetyllysine; alternate By similarity
Modified residue3901N6-succinyllysine; alternate By similarity
Modified residue3991N6-acetyllysine By similarity
Modified residue4151N6-acetyllysine; alternate By similarity
Modified residue4151N6-succinyllysine; alternate By similarity
Modified residue4571N6-acetyllysine; alternate By similarity
Modified residue4571N6-malonyllysine; alternate By similarity
Modified residue4571N6-succinyllysine; alternate By similarity
Modified residue4771N6-acetyllysine; alternate By similarity
Modified residue4771N6-succinyllysine; alternate By similarity
Modified residue4801N6-acetyllysine; alternate By similarity
Modified residue4801N6-succinyllysine; alternate By similarity
Modified residue5031N6-acetyllysine; alternate By similarity
Modified residue5031N6-malonyllysine; alternate By similarity
Modified residue5031N6-succinyllysine; alternate By similarity
Modified residue5271N6-acetyllysine; alternate By similarity
Modified residue5271N6-malonyllysine; alternate By similarity
Modified residue5271N6-succinyllysine; alternate By similarity
Modified residue5451N6-acetyllysine; alternate By similarity
Modified residue5451N6-succinyllysine; alternate By similarity
Modified residue5481N6-acetyllysine By similarity

Experimental info

Sequence conflict56 – 572AA → GP in CAA32441. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P10860 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: 388B8B5490C10F31

FASTA55861,416
        10         20         30         40         50         60 
MYRRLGEVLL LSRAGPAALG SAAADSAALL GWARGQPSAV PQPGLTPVAR RHYSEAATDR 

        70         80         90        100        110        120 
EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRENEEQKRN RVRGILRIIK PCNHVLSLSF 

       130        140        150        160        170        180 
PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG 

       190        200        210        220        230        240 
GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY 

       250        260        270        280        290        300 
ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGLG 

       310        320        330        340        350        360 
DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED FKLQHGSILG 

       370        380        390        400        410        420 
FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER 

       430        440        450        460        470        480 
NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK 

       490        500        510        520        530        540 
HGGTIPVVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV 

       550 
NAIEKVFKVY NEAGVTFT 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS03707.
RefSeqNP_036702.1. NM_012570.2.
UniGeneRn.55106.

3D structure databases

ProteinModelPortalP10860.
SMRP10860. Positions 63-558.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246566. 1 interaction.
IntActP10860. 4 interactions.
MINTMINT-2793533.

Chemistry

ChEMBLCHEMBL2176833.

PTM databases

PhosphoSiteP10860.

2D gel databases

World-2DPAGE0004:P10860.

Proteomic databases

PaxDbP10860.
PRIDEP10860.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000013788; ENSRNOP00000013789; ENSRNOG00000010222.
GeneID24399.
KEGGrno:24399.
UCSCRGD:2708. rat.

Organism-specific databases

CTD2746.
RGD2708. Glud1.

Phylogenomic databases

eggNOGCOG0334.
GeneTreeENSGT00390000000854.
HOGENOMHOG000243801.
HOVERGENHBG005479.
InParanoidP10860.
KOK00261.
OMASGLEYTM.
OrthoDBEOG73NG50.
PhylomeDBP10860.
TreeFamTF313945.

Enzyme and pathway databases

SABIO-RKP10860.

Gene expression databases

GenevestigatorP10860.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR006095. 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]
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSPR00082. GLFDHDRGNASE.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603195.
PROP10860.

Entry information

Entry nameDHE3_RAT
AccessionPrimary (citable) accession number: P10860
Secondary accession number(s): Q66HI8, Q6LC16
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 4, 2006
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families