[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Liver; DOI=10.1093/nar/17.6.2356; PubMed=2704625 [NCBI, ExPASy, EBI, Israel, Japan] Amuro N., Ooki K., Ito A., Goto Y., Okazaki T.; "Nucleotide sequence of rat liver glutamate dehydrogenase cDNA."; Nucleic Acids Res. 17:2356-2357(1989).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Wistar; TISSUE=Liver; DOI=10.1093/nar/17.6.2355; PubMed=2704624 [NCBI, ExPASy, EBI, Israel, Japan] Das A.T., Moerer P., Lamers W.H.; "Nucleotide sequence of rat liver glutamate dehydrogenase cDNA."; Nucleic Acids Res. 17:2355-2355(1989).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30. STRAIN=Wistar; TISSUE=Liver; PubMed=8094669 [NCBI, ExPASy, EBI, Israel, Japan] Das A.T., Arnberg A.C., Malingre H., Moerer P., Charles R., Moorman A.F.M., Lamers W.H.; "Isolation and characterization of the rat gene encoding glutamate dehydrogenase."; Eur. J. Biochem. 211:795-803(1993).
[5]	PROTEIN SEQUENCE OF 108-123; 303-318; 347-363; 400-420; 481-496 AND 504-516, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; Lubec G., Afjehi-Sadat L., Chen W.-Q.; Submitted (APR-2007) to UniProtKB.
[6]	PROTEIN SEQUENCE OF 161-190. PubMed=1684101 [NCBI, ExPASy, EBI, Israel, Japan] Schwerdt G., Moller U., Huth W.; "Identification of the CoA-modified forms of mitochondrial acetyl-CoA acetyltransferase and of glutamate dehydrogenase as nearest-neighbour proteins."; Biochem. J. 280:353-357(1991).
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 431-558, FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. STRAIN=Wistar; TISSUE=Hippocampus; DOI=10.1073/pnas.94.18.9669; PubMed=9275181 [NCBI, ExPASy, EBI, Israel, Japan] Cavallaro S., Meiri N., Yi C.-L., Musco S., Ma W., Goldberg J., Alkon D.L.; "Late memory-related genes in the hippocampus revealed by RNA fingerprinting."; Proc. Natl. Acad. Sci. U.S.A. 94:9669-9673(1997).

Comments

FUNCTION: May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.
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: 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.
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.
SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X14223; CAA32441.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X14044; CAA32202.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC081841; AAH81841.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X64365; CAA45717.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U95148; AAB70012.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S03707; S03707.

NP_036702.1; -.

3D structure databases

HSSP

P00367; 1L1F. [HSSP ENTRY / PDB]

P10860; 59-558.

PTM databases

P10860; -.

Organism-specific databases

RGD

2708; Glud1.

Gene expression databases

ArrayExpress

P10860; -.

GermOnline

ENSRNOG00000010222; Rattus norvegicus.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004353;	Molecular function: glutamate dehydrogenase [NAD(P)+] activity (inferred from electronic annotation from EC).
GO:0005525;	Molecular function: GTP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006520;	Biological process: amino acid metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006095; Glu/Leu/Phe/Val_DHase.
IPR006096; Glu/Leu/Phe/Val_DHase_C.
IPR006097; Glu/Leu/Phe/Val_DHase_dimer.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR11606:SF2; GLFV_DH; 1.

Pfam

PF00208; ELFV_dehydrog; 1.
PF02812; ELFV_dehydrog_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00082; GLFDHDRGNASE.

PROSITE

PS00074; GLFV_DEHYDROGENASE; 1.

Genome annotation databases

Ensembl

ENSRNOG00000010222; Rattus norvegicus. [Contig view]

GeneID

24399; -.

KEGG

rno:24399; -.

NMPDR

fig|10116.3.peg.12078; -.

Phylogenomic databases

HOVERGEN

P10860; -.

Other

603195; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; ATP-binding; Direct protein sequencing; GTP-binding; Mitochondrion; NADP; Nucleotide-binding; Oxidoreductase; Phosphoprotein; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 53`	`53`	`Mitochondrion (By similarity).`
`CHAIN`	`54 558`	`505`	`Glutamate dehydrogenase 1, mitochondrial.`	`PRO_0000007213`
`NP_BIND`	`141 143`	`3`	`NAD (By similarity).`
`ACT_SITE`	`183 183`
`BINDING`	`147 147`		`Substrate (By similarity).`
`BINDING`	`171 171`		`Substrate (By similarity).`
`BINDING`	`176 176`		`NAD (By similarity).`
`BINDING`	`252 252`		`NAD (By similarity).`
`BINDING`	`266 266`		`GTP (By similarity).`
`BINDING`	`270 270`		`GTP (By similarity).`
`BINDING`	`319 319`		`GTP (By similarity).`
`BINDING`	`322 322`		`GTP (By similarity).`
`BINDING`	`438 438`		`Substrate (By similarity).`
`BINDING`	`444 444`		`NAD (By similarity).`
`BINDING`	`450 450`		`ADP (By similarity).`
`BINDING`	`516 516`		`ADP (By similarity).`
`MOD_RES`	`84 84`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`135 135`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`227 227`		`Phosphoserine (By similarity).`
`MOD_RES`	`503 503`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`512 512`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`527 527`		`N6-acetyllysine (By similarity).`
`CONFLICT`	`56 57`		`AA -> GP (in Ref. 1; CAA32441).`

Sequence information

Length: 558 AA [This is the length of the unprocessed precursor]

Molecular weight: 61416 Da [This is the MW of the unprocessed precursor]

CRC64: 388B8B5490C10F31 [This is a checksum on the sequence]

        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

P10860 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools