Reviewed, UniProtKB/Swiss-Prot P14152 (MDHC_MOUSE)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase, cytoplasmic
    EC=1.1.1.37
Alternative name(s):
    Cytosolic malate dehydrogenase

Gene names

Name:	Mdh1
Synonyms:	Mor2

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	334 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)

Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro malate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 334	333	Malate dehydrogenase, cytoplasmic		PRO_0000113410
Regions
	Nucleotide binding	11 – 17	7	NAD By similarity
	Nucleotide binding	129 – 131	3	NAD By similarity
Sites
	Active site	187	1	Proton acceptor By similarity
	Binding site	92	1	Substrate By similarity
	Binding site	98	1	Substrate By similarity
	Binding site	105	1	NAD By similarity
	Binding site	112	1	NAD By similarity
	Binding site	131	1	Substrate By similarity
	Binding site	162	1	Substrate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	210	1	Phosphotyrosine Ref.7
Experimental info
	Sequence conflict	92	1	R → I in BAB23897. Ref.3
	Sequence conflict	177	1	D → N in BAE37915. Ref.3
	Sequence conflict	288	1	F → L Ref.1
	Sequence conflict	288	1	F → L Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P14152-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3B9F00372AA939DF	FASTA	334	36,511
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase." Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S., Kuramitsu S., Kagamiyama H., Morino Y. J. Biol. Chem. 262:15127-15131(1987) [PubMed: 3312200] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural organization of the mouse cytosolic malate dehydrogenase gene: comparison with that of the mouse mitochondrial malate dehydrogenase gene." Setoyama C., Joh T., Tsuzuki T., Shimada K. J. Mol. Biol. 202:355-364(1988) [PubMed: 3172222] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C3H/He. Tissue: Liver.
[3]	"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: Cerebellum, Mammary gland and Stomach.
[4]	The mouse genome sequencing consortium Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	"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.
[6]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 80-92; 126-142; 171-199; 206-230; 299-310 AND 325-334, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[7]	"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-210, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M29462 mRNA. Translation: AAA39510.1. M36084 Genomic DNA. Translation: AAA37423.1. AK005237 mRNA. Translation: BAB23897.1. AK164785 mRNA. Translation: BAE37915.1. AK168545 mRNA. Translation: BAE40421.1. AL663049 Genomic DNA. Translation: CAI24411.1. BC050940 mRNA. Translation: AAH50940.2.
IPI	IPI00336324.
PIR	DEMSMC. S02654.
RefSeq	NP_032644.2.
UniGene	Mm.212703
3D structure databases
HSSP	HSSP built from PDB template 4MDH based on UniProtKB P11708.
SMR	P14152. Positions 2-334.
ModBase	Search...
PTM databases
PhosphoSite	P14152.
2-D gel databases
SWISS-2DPAGE	P14152.
REPRODUCTION-2DPAGE	P14152.
Proteomic databases
PRIDE	P14152.
Genome annotation databases
Ensembl	ENSMUSG00000020321. Mus musculus. [Contig view]
GeneID	17449.
KEGG	mmu:17449.
NMPDR	fig|10090.3.peg.23330.
Organism-specific databases
MGI	MGI:97051. Mdh1.
Phylogenomic databases
HOGENOM	P14152.
HOVERGEN	P14152.
OMA	P14152. DQPIILV.
Enzyme and pathway databases
BRENDA	1.1.1.37. 244.
Gene expression databases
ArrayExpress	P14152.
Bgee	P14152.
CleanEx	MM_MDH1.
GermOnline	ENSMUSG00000020321. Mus musculus.
Family and domain databases
InterPro	IPR001557. L-lactate/malate_DH. IPR001236. Lactate/malate_DH. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR001252. Malate_DH_AS. IPR011274. Malate_DH_NAD-dep_euk. IPR010945. Malate_DH_SF1. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR23382. MDH_SF1. 1 hit.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
ProDom	PD003052. Mal_dehydrog. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01759. MalateDH-SF1. 1 hit. TIGR01758. MDH_euk_cyt. 1 hit.
PROSITE	PS00068. MDH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	292088.
SOURCE	Search...

Entry information

Entry name

MDHC_MOUSE

Accession

Primary (citable) accession number: P14152
Secondary accession number(s): Q3TP22, Q80Y13, Q9DB45

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)