Reviewed, UniProtKB/Swiss-Prot P26443 (DHE3_MOUSE)

Names and origin

Protein names

Recommended name:
    Glutamate dehydrogenase 1, mitochondrial
      Short name=GDH
    EC=1.4.1.3

Gene names

Name:	Glud1
Synonyms:	Glud

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate By similarity.
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.
Post-translational modification	Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding GTP-binding NADP Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	amino acid metabolic process Inferred from electronic annotation. Source: InterPro negative regulation of insulin secretion Inferred from genetic interaction. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW transmembrane receptor protein tyrosine kinase signaling pathway Non-traceable author statement. Source: UniProtKB
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate dehydrogenase [NAD(P)+] activity Inferred from direct assay. Source: MGI protein binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 53	53	Mitochondrion
	Chain	54 – 558	505	Glutamate dehydrogenase 1, mitochondrial		PRO_0000007212
Regions
	Nucleotide binding	141 – 143	3	NAD By similarity
Sites
	Active site	183	1	By similarity
	Binding site	147	1	Substrate By similarity
	Binding site	171	1	Substrate By similarity
	Binding site	176	1	NAD By similarity
	Binding site	252	1	NAD By similarity
	Binding site	266	1	GTP By similarity
	Binding site	270	1	GTP By similarity
	Binding site	319	1	GTP By similarity
	Binding site	322	1	GTP By similarity
	Binding site	438	1	Substrate By similarity
	Binding site	444	1	NAD By similarity
	Binding site	450	1	ADP By similarity
	Binding site	516	1	ADP By similarity
Amino acid modifications
	Modified residue	84	1	N6-acetyllysine Ref.5
	Modified residue	135	1	Phosphotyrosine Ref.6
	Modified residue	227	1	Phosphoserine Ref.7
	Modified residue	503	1	N6-acetyllysine Ref.5
	Modified residue	512	1	Phosphotyrosine Ref.6
	Modified residue	527	1	N6-acetyllysine Ref.5
Experimental info
	Sequence conflict	495	1	D → G in BAC40767. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P26443-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 92738AA5A133838A	FASTA	558	61,337
	10 20 30 40 50 60 MYRRLGEALL LSRAGPAALG SAAADSAALL GWARGQPSAA PQPGLTPVAR RHYSEAAADR 70 80 90 100 110 120 EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRESEEQKRN 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 SILGMTPGFG 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, structure and expression analysis of a full-length mouse brain glutamate dehydrogenase cDNA." Tzimagiorgis G., Moschonas N.K. Biochim. Biophys. Acta 1089:250-253(1991) [PubMed: 1711373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Olfactory bulb.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[4]	Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 61-76; 108-123; 125-136; 152-183; 192-200; 212-231; 275-318; 327-346; 353-363; 366-386; 400-420; 461-476; 481-496; 504-516; 528-545 AND 549-558. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[5]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-503 AND LYS-527, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135 AND TYR-512, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X57024 mRNA. Translation: CAA40341.1. AK089152 mRNA. Translation: BAC40767.1. BC052724 mRNA. Translation: AAH52724.1. BC057347 mRNA. Translation: AAH57347.1.
IPI	IPI00114209.
PIR	S16239.
RefSeq	NP_032159.1.
UniGene	Mm.10600
3D structure databases
HSSP	HSSP built from PDB template 1L1F based on UniProtKB P00367.
SMR	P26443. Positions 58-558.
ModBase	Search...
PTM databases
PhosphoSite	P26443.
2-D gel databases
SWISS-2DPAGE	P26443.
REPRODUCTION-2DPAGE	P26443.
Proteomic databases
PRIDE	P26443.
Genome annotation databases
Ensembl	ENSMUSG00000021794. Mus musculus. [Contig view]
GeneID	14661.
KEGG	mmu:14661.
NMPDR	fig|10090.3.peg.28839.
Organism-specific databases
MGI	MGI:95753. Glud1.
Phylogenomic databases
HOGENOM	P26443.
HOVERGEN	P26443.
OMA	P26443. RIQAKII.
Enzyme and pathway databases
BRENDA	1.4.1.3. 244.
Gene expression databases
ArrayExpress	P26443.
Bgee	P26443.
GermOnline	ENSMUSG00000021794. Mus musculus.
Family and domain databases
InterPro	IPR006095. Glu/Leu/Phe/Val_DH. IPR006096. Glu/Leu/Phe/Val_DH_C. IPR006097. Glu/Leu/Phe/Val_DH_dimer. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11606:SF2. GLFV_DH. 1 hit.
Pfam	PF00208. ELFV_dehydrog. 1 hit. PF02812. ELFV_dehydrog_N. 1 hit. [Graphical view]
PRINTS	PR00082. GLFDHDRGNASE.
PROSITE	PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	286534.
SOURCE	Search...

Entry information

Entry name

DHE3_MOUSE

Accession

Primary (citable) accession number: P26443
Secondary accession number(s): Q8C273

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)