ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P08249


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name MDHM_MOUSE
Primary accession number P08249
Secondary accession numbers Q0QF44 Q8CF79 Q8R1P0
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on May 1, 2007 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 96)
Name and origin of the protein
Protein name Malate dehydrogenase, mitochondrial [Precursor]
Synonym EC 1.1.1.37
Gene name
Name: Mdh2
Synonyms: Mor1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00383a017; PubMed=3038184 [NCBI, ExPASy, EBI, Israel, Japan]
Joh T., Takeshima H., Tsuzuki T., Shimada K., Tanase S., Morino Y.;
"Cloning and sequence analysis of cDNAs encoding mammalian mitochondrial malate dehydrogenase.";
Biochemistry 26:2515-2520(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0022-2836(88)90328-2; PubMed=3379635 [NCBI, ExPASy, EBI, Israel, Japan]
Takeshima H., Joh T., Tsuzuki T., Shimada K., Matsukado Y.;
"Structural organization of the mouse mitochondrial malate dehydrogenase gene.";
J. Mol. Biol. 200:1-11(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=BALB/c, and C57BL/6J;
TISSUE=Cerebellum, and Kidney;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary tumor;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-322.
TISSUE=Liver;
DOI=10.1093/molbev/msl027; PubMed=16751257 [NCBI, ExPASy, EBI, Israel, Japan]
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
"Housekeeping genes for phylogenetic analysis of eutherian relationships.";
Mol. Biol. Evol. 23:1493-1503(2006).
[6]
PROTEIN SEQUENCE OF 27-45; 53-74; 79-104; 166-185; 192-239; 242-257; 282-296 AND 308-324, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 53-74 AND 166-176, AND MASS SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157; LYS-239 AND LYS-314, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
Comments
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
M16229; AAA39509.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07295; CAA30274.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07296; CAA30274.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07297; CAA30274.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07298; CAA30274.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07299; CAA30274.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07300; CAA30274.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07301; CAA30274.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002305; BAC24986.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK167809; BAE39836.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK160553; BAE35869.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK135162; BAE22447.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC023482; AAH23482.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ402950; ABD77283.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S01350; DEMSMM.
RefSeq NP_032643.2; -.
UniGene Mm.297096
3D structure databases
HSSP P00346; 1MLD. [HSSP ENTRY / PDB]
SMR P08249; 25-337.
ModBase P08249.
PTM databases
PhosphoSite P08249; -.
2D gel databases
SWISS-2DPAGE P08249; -.
REPRODUCTION-2DPAGE P08249; -.
Organism-specific databases
MGI MGI:97050; Mdh2.
Gene expression databases
ArrayExpress P08249; -.
CleanEx MM_MDH2; -.
GermOnline ENSMUSG00000019179; Mus musculus.
Ontologies
GO
GO:0005743; Cellular component: mitochondrial inner membrane (inferred from direct assay from MGI).
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0030060; Molecular function: L-malate dehydrogenase activity (inferred from direct assay from MGI).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
GO:0006108; Biological process: malate metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001557; L-lactate/malate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR001252; Malate_DHase_AS.
IPR010097; Malate_DHase_NAD-dep_euk_g_bac.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11540:SF1; MDH_euk_g_bac; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
TIGRFAMs TIGR01772; MDH_euk_gproteo; 1.
PROSITE PS00068; MDH; 1.
Proteomics databases
PRIDE P08249; -.
Genome annotation databases
Ensembl ENSMUSG00000019179; Mus musculus. [Contig view]
GeneID 17448; -.
KEGG mmu:17448; -.
NMPDR fig|10090.3.peg.12582; -.
Phylogenomic databases
HOGENOM P08249; -.
HOVERGEN P08249; -.
Other
NextBio 292084; -.
SOURCE Mdh2; Mus musculus.
ProtoNet P08249.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    24  24     Mitochondrion. 
CHAIN   25   338  314     Malate dehydrogenase, mitochondrial. PRO_0000018629
NP_BIND   31    37  7     NAD (By similarity). 
NP_BIND   140   142  3     NAD (By similarity). 
ACT_SITE   200   200        Proton acceptor (By similarity). 
BINDING   57    57        NAD (By similarity). 
BINDING   104   104        Substrate. 
BINDING   110   110        Substrate. 
BINDING   117   117        NAD (By similarity). 
BINDING   142   142        Substrate. 
BINDING   176   176        Substrate. 
BINDING   251   251        NAD (By similarity). 
MOD_RES   56    56        Phosphotyrosine (By similarity). 
MOD_RES   157   157        N6-acetyllysine. 
MOD_RES   239   239        N6-acetyllysine. 
MOD_RES   314   314        N6-acetyllysine. 
CONFLICT   76    76        N -> K (in Ref. 1; AAA39509). 
CONFLICT   269   269        K -> L (in Ref. 1; AAA39509 and 2; CAA30274). 
Sequence information
Length: 338 AA [This is the length of the unprocessed precursor] Molecular weight: 35611 Da [This is the MW of the unprocessed precursor] CRC64: 99D13BB2099C19F1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLSALARPAG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH 

        70         80         90        100        110        120 
TPGVAADLSH IETRANVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI 

       130        140        150        160        170        180 
VATLTAACAQ HCPEAMVCII ANPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANTF 

       190        200        210        220        230        240 
VAELKGLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLATLTGRI QEAGTEVVKA 

       250        260        270        280        290        300 
KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVVECSFVQS KETECTYFST PLLLGKKGLE 

       310        320        330 
KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK 

P08249 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!