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Database: UniProt
Entry: O88989
LinkDB: O88989
Original site: O88989 
ID   MDHC_RAT                Reviewed;         334 AA.
AC   O88989; O88585; Q6PCV2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-NOV-2016, entry version 122.
DE   RecName: Full=Malate dehydrogenase, cytoplasmic;
DE            EC=1.1.1.37;
DE   AltName: Full=Cytosolic malate dehydrogenase;
GN   Name=Mdh1; Synonyms=Mdh;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Achenbach P., Steinbrenner H., Reindl G., Seissler J.;
RT   "Cloning of rat cytosolic malate dehydrogenase.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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   [3]
RP   PROTEIN SEQUENCE OF 7-32; 80-92; 126-157; 171-199; 206-230; 239-255;
RP   299-310 AND 319-334, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 251-284.
RA   Earley S.;
RT   "Partial sequence of rat malate dehydrogenase (MDH) mRNA.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-241; SER-332
RP   AND SER-333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: ISGylated. {ECO:0000250}.
CC   -!- PTM: Acetylation at Lys-118 dramatically enhances enzymatic
CC       activity and promotes adipogenic differentiation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000305}.
DR   EMBL; AF093773; AAC64180.1; -; mRNA.
DR   EMBL; BC059124; AAH59124.1; -; mRNA.
DR   EMBL; AF075574; AAC26799.1; -; mRNA.
DR   RefSeq; NP_150238.1; NM_033235.2.
DR   UniGene; Rn.13492; -.
DR   ProteinModelPortal; O88989; -.
DR   BioGrid; 246700; 3.
DR   IntAct; O88989; 1.
DR   MINT; MINT-4580226; -.
DR   STRING; 10116.ENSRNOP00000011429; -.
DR   iPTMnet; O88989; -.
DR   PhosphoSitePlus; O88989; -.
DR   SwissPalm; O88989; -.
DR   World-2DPAGE; 0004:O88989; -.
DR   PaxDb; O88989; -.
DR   PRIDE; O88989; -.
DR   Ensembl; ENSRNOT00000011429; ENSRNOP00000011429; ENSRNOG00000008103.
DR   GeneID; 24551; -.
DR   KEGG; rno:24551; -.
DR   UCSC; RGD:3072; rat.
DR   CTD; 4190; -.
DR   RGD; 3072; Mdh1.
DR   eggNOG; KOG1496; Eukaryota.
DR   eggNOG; COG0039; LUCA.
DR   GeneTree; ENSGT00530000063410; -.
DR   HOGENOM; HOG000220953; -.
DR   HOVERGEN; HBG006340; -.
DR   InParanoid; O88989; -.
DR   KO; K00025; -.
DR   OMA; QYPDAGQ; -.
DR   OrthoDB; EOG091G0BLA; -.
DR   PhylomeDB; O88989; -.
DR   TreeFam; TF105826; -.
DR   Reactome; R-RNO-70263; Gluconeogenesis.
DR   PRO; PR:O88989; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000008103; -.
DR   Genevisible; O88989; RN.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:RGD.
DR   GO; GO:0016615; F:malate dehydrogenase activity; IDA:RGD.
DR   GO; GO:0051287; F:NAD binding; IDA:RGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IDA:RGD.
DR   GO; GO:0098779; P:mitophagy in response to mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:0019674; P:NAD metabolic process; IDA:RGD.
DR   GO; GO:0006734; P:NADH metabolic process; IDA:RGD.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IDA:RGD.
DR   GO; GO:0002230; P:positive regulation of defense response to virus by host; IEA:Ensembl.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   GO; GO:0098792; P:xenophagy; IEA:Ensembl.
DR   CDD; cd01336; MDH_cytoplasmic_cytosolic; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_01517; Malate_dehydrog_2; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DH_AS.
DR   InterPro; IPR011274; Malate_DH_NAD-dep_euk.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   TIGRFAMs; TIGR01758; MDH_euk_cyt; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Methylation; NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Tricarboxylic acid cycle; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P40925}.
FT   CHAIN         2    334       Malate dehydrogenase, cytoplasmic.
FT                                /FTId=PRO_0000226737.
FT   NP_BIND      11     17       NAD. {ECO:0000250}.
FT   NP_BIND     129    131       NAD. {ECO:0000250}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000250}.
FT   BINDING      92     92       Substrate. {ECO:0000250}.
FT   BINDING      98     98       Substrate. {ECO:0000250}.
FT   BINDING     105    105       NAD. {ECO:0000250}.
FT   BINDING     112    112       NAD. {ECO:0000250}.
FT   BINDING     131    131       Substrate. {ECO:0000250}.
FT   BINDING     162    162       Substrate. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000250|UniProtKB:P40925}.
FT   MOD_RES     110    110       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P14152}.
FT   MOD_RES     118    118       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P40925}.
FT   MOD_RES     121    121       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P40925}.
FT   MOD_RES     214    214       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P14152}.
FT   MOD_RES     217    217       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     230    230       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:P14152}.
FT   MOD_RES     241    241       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     298    298       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P40925}.
FT   MOD_RES     298    298       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P14152}.
FT   MOD_RES     309    309       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P14152}.
FT   MOD_RES     318    318       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P14152}.
FT   MOD_RES     332    332       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     333    333       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CONFLICT    251    251       S -> A (in Ref. 4; AAC26799).
FT                                {ECO:0000305}.
FT   CONFLICT    276    276       N -> D (in Ref. 2; AAH59124).
FT                                {ECO:0000305}.
SQ   SEQUENCE   334 AA;  36483 MW;  8F6778722A607B3C CRC64;
     MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC
     ALPLLQDVIA TDKEEVAFKD LDVAVLVGSM PRREGMERKD LLKANVKIFK SQGAALEKYA
     KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKSQIALK LGVTADDVKN
     VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFITTVQQR GAAVIKARKL
     SSAMSAAKAI SDHIRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV
     EGLPINDFSR EKMDLTAKEL TEEKETAFEF LSSA
//
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