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P10860

- DHE3_RAT

UniProt

P10860 - DHE3_RAT

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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

Glud1

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.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
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. mitochondrion Source: RGD
Complete GO annotation...

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

ExpressionAtlasiP10860. baseline and differential.
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

        10         20         30         40         50
MYRRLGEVLL LSRAGPAALG SAAADSAALL GWARGQPSAV PQPGLTPVAR
60 70 80 90 100
RHYSEAATDR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRENEEQKRN
110 120 130 140 150
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGLG
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FKLQHGSILG FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPVVPT AEFQDRISGA
510 520 530 540 550
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY

NEAGVTFT
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

ExpressionAtlasi P10860. baseline and differential.
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: October 29, 2014
This is version 136 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