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 P14152


[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 MDHC_MOUSE
Primary accession number P14152
Secondary accession numbers Q3TP22 Q80Y13 Q9DB45
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 88)
Name and origin of the protein
Protein name Malate dehydrogenase, cytoplasmic
Synonyms EC 1.1.1.37
Cytosolic malate dehydrogenase
Gene name
Name: Mdh1
Synonyms: Mor2
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].
PubMed=3312200 [NCBI, ExPASy, EBI, Israel, Japan]
Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S., Kuramitsu S., Kagamiyama H., Morino Y.;
"Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase.";
J. Biol. Chem. 262:15127-15131(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C3H/He;
TISSUE=Liver;
DOI=10.1016/0022-2836(88)90270-7; PubMed=3172222 [NCBI, ExPASy, EBI, Israel, Japan]
Setoyama C., Joh T., Tsuzuki T., Shimada K.;
"Structural organization of the mouse cytosolic malate dehydrogenase gene: comparison with that of the mouse mitochondrial malate dehydrogenase gene.";
J. Mol. Biol. 202:355-364(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Cerebellum, Mammary gland, and Stomach;
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 GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6;
TISSUE=Brain;
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).
[6]
PROTEIN SEQUENCE OF 80-92 AND 180-199, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 80-92; 126-142; 171-179; 206-230; 299-310 AND 325-334, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-210, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
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
M29462; AAA39510.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M36084; AAA37423.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK005237; BAB23897.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK164785; BAE37915.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK168545; BAE40421.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL663049; CAI24411.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050940; AAH50940.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S02654; DEMSMC.
RefSeq NP_032644.2; -.
UniGene Mm.212703
3D structure databases
HSSP P11708; 4MDH. [HSSP ENTRY / PDB]
SMR P14152; 2-334.
ModBase P14152.
PTM databases
PhosphoSite P14152; -.
2D gel databases
SWISS-2DPAGE P14152; -.
REPRODUCTION-2DPAGE P14152; -.
Organism-specific databases
MGI MGI:97051; Mdh1.
Gene expression databases
ArrayExpress P14152; -.
CleanEx MM_MDH1; -.
GermOnline ENSMUSG00000020321; Mus musculus.
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.
IPR011274; Malate_DHase_NAD-dep_euk.
IPR010945; Malate_DHase_SF1.
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 PTHR23382; MDH_SF1; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
ProDom PD003052; Mal_dehydrog; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01759; MalateDH-SF1; 1.
TIGR01758; MDH_euk_cyt; 1.
PROSITE PS00068; MDH; 1.
BLOCKS P14152.
Genome annotation databases
Ensembl ENSMUSG00000020321; Mus musculus. [Contig view]
GeneID 17449; -.
KEGG mmu:17449; -.
NMPDR fig|10090.3.peg.23330; -.
Phylogenomic databases
HOGENOM P14152; -.
HOVERGEN P14152; -.
Other
SOURCE Mdh1; Mus musculus.
ProtoNet P14152.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   334  333     Malate dehydrogenase, cytoplasmic. PRO_0000113410
NP_BIND   11    17  7     NAD (By similarity). 
NP_BIND   129   131  3     NAD (By similarity). 
ACT_SITE   187   187        Proton acceptor (By similarity). 
BINDING   92    92        Substrate (By similarity). 
BINDING   98    98        Substrate (By similarity). 
BINDING   105   105        NAD (By similarity). 
BINDING   112   112        NAD (By similarity). 
BINDING   131   131        Substrate (By similarity). 
BINDING   162   162        Substrate (By similarity). 
MOD_RES   2     2        N-acetylserine (By similarity). 
MOD_RES   210   210        Phosphotyrosine. 
CONFLICT   92    92        R -> I (in Ref. 3; BAB23897). 
CONFLICT   177   177        D -> N (in Ref. 3; BAE37915). 
CONFLICT   288   288        F -> L (in Ref. 1 and 2). 
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 36511 Da [This is the MW of the unprocessed precursor] CRC64: 3B9F00372AA939DF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC 

        70         80         90        100        110        120 
ALPLLQDVIA TDKEEIAFKD LDVAVLVGSM PRREGMERKD LLKANVKIFK SQGTALEKYA 

       130        140        150        160        170        180 
KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKSQIALK LGVTADDVKN 

       190        200        210        220        230        240 
VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFITTVQQR GAAVIKARKL 

       250        260        270        280        290        300 
SSAMSAAKAI ADHIRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV 

       310        320        330 
EGLPINDFSR EKMDLTAKEL TEEKETAFEF LSSA 

P14152 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 ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!