ID   MDHM_MOUSE              Reviewed;         338 AA.
AC   P08249; Q0QF44; Q8CF79; Q8R1P0;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 3.
DT   04-NOV-2008, entry version 94.
DE   RecName: Full=Malate dehydrogenase, mitochondrial;
DE            EC=1.1.1.37;
DE   Flags: Precursor;
GN   Name=Mdh2; Synonyms=Mor1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87271646; PubMed=3038184; DOI=10.1021/bi00383a017;
RA   Joh T., Takeshima H., Tsuzuki T., Shimada K., Tanase S., Morino Y.;
RT   "Cloning and sequence analysis of cDNAs encoding mammalian
RT   mitochondrial malate dehydrogenase.";
RL   Biochemistry 26:2515-2520(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88245174; PubMed=3379635; DOI=10.1016/0022-2836(88)90328-2;
RA   Takeshima H., Joh T., Tsuzuki T., Shimada K., Matsukado Y.;
RT   "Structural organization of the mouse mitochondrial malate
RT   dehydrogenase gene.";
RL   J. Mol. Biol. 200:1-11(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J; TISSUE=Cerebellum, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-322.
RC   TISSUE=Liver;
RX   PubMed=16751257; DOI=10.1093/molbev/msl027;
RA   Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT   "Housekeeping genes for phylogenetic analysis of eutherian
RT   relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 27-45; 53-74; 79-104; 166-185; 192-239; 242-257;
RP   282-296 AND 308-324, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   PROTEIN SEQUENCE OF 53-74 AND 166-176, AND MASS SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157; LYS-239 AND LYS-314,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Acetylation of Lys-239 and Lys-314 is observed in liver
CC       mitochondria from fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC24986.1; Type=Frameshift; Positions=39;
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DR   EMBL; M16229; AAA39509.1; -; mRNA.
DR   EMBL; X07295; CAA30274.1; -; Genomic_DNA.
DR   EMBL; X07296; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; X07297; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; X07298; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; X07299; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; X07300; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; X07301; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; AK002305; BAC24986.1; ALT_FRAME; mRNA.
DR   EMBL; AK167809; BAE39836.1; -; mRNA.
DR   EMBL; AK160553; BAE35869.1; -; mRNA.
DR   EMBL; AK135162; BAE22447.1; -; mRNA.
DR   EMBL; BC023482; AAH23482.1; -; mRNA.
DR   EMBL; DQ402950; ABD77283.1; -; mRNA.
DR   PIR; S01350; DEMSMM.
DR   RefSeq; NP_032643.2; -.
DR   UniGene; Mm.297096; -.
DR   HSSP; P00346; 1MLD.
DR   SMR; P08249; 25-337.
DR   PhosphoSite; P08249; -.
DR   SWISS-2DPAGE; P08249; -.
DR   REPRODUCTION-2DPAGE; P08249; -.
DR   Ensembl; ENSMUSG00000019179; Mus musculus.
DR   GeneID; 17448; -.
DR   KEGG; mmu:17448; -.
DR   NMPDR; fig|10090.3.peg.12582; -.
DR   MGI; MGI:97050; Mdh2.
DR   HOGENOM; P08249; -.
DR   HOVERGEN; P08249; -.
DR   NextBio; 292084; -.
DR   ArrayExpress; P08249; -.
DR   CleanEx; MM_MDH2; -.
DR   GermOnline; ENSMUSG00000019179; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:MGI.
DR   InterPro; IPR001557; L-lactate/malate_DHase.
DR   InterPro; IPR001236; Lactate/malate_DHase.
DR   InterPro; IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DHase_AS.
DR   InterPro; IPR010097; Malate_DHase_NAD-dep_euk_g_bac.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11540:SF1; MDH_euk_g_bac; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Mitochondrion; NAD;
KW   Oxidoreductase; Phosphoprotein; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     24       Mitochondrion.
FT   CHAIN        25    338       Malate dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000018629.
FT   NP_BIND      31     37       NAD (By similarity).
FT   NP_BIND     140    142       NAD (By similarity).
FT   ACT_SITE    200    200       Proton acceptor (By similarity).
FT   BINDING      57     57       NAD (By similarity).
FT   BINDING     104    104       Substrate.
FT   BINDING     110    110       Substrate.
FT   BINDING     117    117       NAD (By similarity).
FT   BINDING     142    142       Substrate.
FT   BINDING     176    176       Substrate.
FT   BINDING     251    251       NAD (By similarity).
FT   MOD_RES      56     56       Phosphotyrosine (By similarity).
FT   MOD_RES     157    157       N6-acetyllysine.
FT   MOD_RES     239    239       N6-acetyllysine.
FT   MOD_RES     314    314       N6-acetyllysine.
FT   CONFLICT     76     76       N -> K (in Ref. 1; AAA39509).
FT   CONFLICT    269    269       K -> L (in Ref. 1; AAA39509 and 2;
FT                                CAA30274).
SQ   SEQUENCE   338 AA;  35611 MW;  99D13BB2099C19F1 CRC64;
     MLSALARPAG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH
     TPGVAADLSH IETRANVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI
     VATLTAACAQ HCPEAMVCII ANPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANTF
     VAELKGLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLATLTGRI QEAGTEVVKA
     KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVVECSFVQS KETECTYFST PLLLGKKGLE
     KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK
//