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Protein

Malate dehydrogenase, mitochondrial

Gene

Mdh2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.PROSITE-ProRule annotation

Enzyme regulationi

Enzyme activity is enhanced by acetylation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571NADBy similarity
Binding sitei104 – 1041SubstratePROSITE-ProRule annotation
Binding sitei110 – 1101SubstratePROSITE-ProRule annotation
Binding sitei117 – 1171NADBy similarity
Binding sitei142 – 1421SubstratePROSITE-ProRule annotation
Binding sitei176 – 1761SubstratePROSITE-ProRule annotation
Active sitei200 – 2001Proton acceptorBy similarity
Binding sitei251 – 2511NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 377NADBy similarity
Nucleotide bindingi140 – 1423NADBy similarity

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: RGD
  2. malate dehydrogenase (NADP+) activity Source: RGD
  3. malate dehydrogenase activity Source: RGD
  4. poly(A) RNA binding Source: Ensembl
  5. protein self-association Source: RGD

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. internal protein amino acid acetylation Source: UniProtKB
  3. malate metabolic process Source: RGD
  4. NADH metabolic process Source: RGD
  5. oxaloacetate metabolic process Source: RGD
  6. tricarboxylic acid cycle Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_331968. Gluconeogenesis.
REACT_338796. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
Gene namesi
Name:Mdh2
Synonyms:Mor1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi619719. Mdh2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial matrix Source: RGD
  4. mitochondrion Source: RGD
  5. nucleus Source: Ensembl
  6. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424Mitochondrion1 PublicationAdd
BLAST
Chaini25 – 338314Malate dehydrogenase, mitochondrialPRO_0000018631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331O-linked (GlcNAc)1 Publication
Modified residuei78 – 781N6-acetyllysine; alternateBy similarity
Modified residuei78 – 781N6-succinyllysine; alternateBy similarity
Modified residuei91 – 911N6-acetyllysine; alternateBy similarity
Modified residuei91 – 911N6-succinyllysine; alternateBy similarity
Modified residuei165 – 1651N6-acetyllysineBy similarity
Modified residuei185 – 1851N6-acetyllysine; alternateBy similarity
Modified residuei185 – 1851N6-succinyllysine; alternateBy similarity
Modified residuei203 – 2031N6-succinyllysineBy similarity
Modified residuei215 – 2151N6-acetyllysine; alternateBy similarity
Modified residuei215 – 2151N6-succinyllysine; alternateBy similarity
Modified residuei239 – 2391N6-acetyllysine; alternateBy similarity
Modified residuei239 – 2391N6-malonyllysine; alternateBy similarity
Modified residuei239 – 2391N6-succinyllysine; alternateBy similarity
Modified residuei269 – 2691N6-succinyllysineBy similarity
Modified residuei296 – 2961N6-acetyllysine; alternateBy similarity
Modified residuei296 – 2961N6-succinyllysine; alternateBy similarity
Modified residuei301 – 3011N6-acetyllysine; alternateBy similarity
Modified residuei301 – 3011N6-succinyllysine; alternateBy similarity
Modified residuei307 – 3071N6-acetyllysine; alternateBy similarity
Modified residuei307 – 3071N6-malonyllysine; alternateBy similarity
Modified residuei307 – 3071N6-succinyllysine; alternateBy similarity
Modified residuei314 – 3141N6-acetyllysine; alternateBy similarity
Modified residuei314 – 3141N6-succinyllysine; alternateBy similarity
Modified residuei324 – 3241N6-acetyllysine; alternateBy similarity
Modified residuei324 – 3241N6-succinyllysine; alternateBy similarity
Modified residuei328 – 3281N6-acetyllysine; alternateBy similarity
Modified residuei328 – 3281N6-succinyllysine; alternateBy similarity
Modified residuei329 – 3291N6-acetyllysine; alternateBy similarity
Modified residuei329 – 3291N6-malonyllysine; alternateBy similarity
Modified residuei335 – 3351N6-acetyllysine; alternateBy similarity
Modified residuei335 – 3351N6-succinyllysine; alternateBy similarity

Post-translational modificationi

Acetylation is enhanced by up to 67% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with the appearance of tri-and tetraacetylations. Glucose also increases acetylation by about 60% (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

PaxDbiP04636.
PRIDEiP04636.

2D gel databases

World-2DPAGE0004:P04636.

PTM databases

PhosphoSiteiP04636.

Expressioni

Tissue specificityi

Expressed in flagella of epididymal sperm.1 Publication

Gene expression databases

GenevestigatoriP04636.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi249687. 1 interaction.
IntActiP04636. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP04636.
SMRiP04636. Positions 25-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 1 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0039.
GeneTreeiENSGT00390000016686.
HOGENOMiHOG000213792.
HOVERGENiHBG001662.
InParanoidiP04636.
KOiK00026.
OMAiTECTYFS.
OrthoDBiEOG74R1R7.
PhylomeDBiP04636.
TreeFamiTF300834.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010097. Malate_DH_type1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04636-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSALARPVG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV
60 70 80 90 100
SRLTLYDIAH TPGVAADLSH IETRANVKGY LGPEQLPDCL KGCDVVVIPA
110 120 130 140 150
GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPEAMICII SNPVNSTIPI
160 170 180 190 200
TAEVFKKHGV YNPNKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH
210 220 230 240 250
AGKTIIPLIS QCTPKVDFPQ DQLATLTGRI QEAGTEVVKA KAGAGSATLS
260 270 280 290 300
MAYAGARFVF SLVDAMNGKE GVIECSFVQS KETECTYFST PLLLGKKGLE
310 320 330
KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK
Length:338
Mass (Da):35,684
Last modified:January 9, 2007 - v2
Checksum:i13849CCFB78C87E7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291R → K in CAA27812 (PubMed:3755817).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04240 mRNA. Translation: CAA27812.1.
BC063165 mRNA. Translation: AAH63165.1.
PIRiA25509. DERTMM.
RefSeqiNP_112413.2. NM_031151.2.
UniGeneiRn.1011.

Genome annotation databases

EnsembliENSRNOT00000001958; ENSRNOP00000001958; ENSRNOG00000001440.
GeneIDi81829.
KEGGirno:81829.
UCSCiRGD:619719. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04240 mRNA. Translation: CAA27812.1.
BC063165 mRNA. Translation: AAH63165.1.
PIRiA25509. DERTMM.
RefSeqiNP_112413.2. NM_031151.2.
UniGeneiRn.1011.

3D structure databases

ProteinModelPortaliP04636.
SMRiP04636. Positions 25-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249687. 1 interaction.
IntActiP04636. 2 interactions.

Chemistry

ChEMBLiCHEMBL2176835.

PTM databases

PhosphoSiteiP04636.

2D gel databases

World-2DPAGE0004:P04636.

Proteomic databases

PaxDbiP04636.
PRIDEiP04636.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001958; ENSRNOP00000001958; ENSRNOG00000001440.
GeneIDi81829.
KEGGirno:81829.
UCSCiRGD:619719. rat.

Organism-specific databases

CTDi4191.
RGDi619719. Mdh2.

Phylogenomic databases

eggNOGiCOG0039.
GeneTreeiENSGT00390000016686.
HOGENOMiHOG000213792.
HOVERGENiHBG001662.
InParanoidiP04636.
KOiK00026.
OMAiTECTYFS.
OrthoDBiEOG74R1R7.
PhylomeDBiP04636.
TreeFamiTF300834.

Enzyme and pathway databases

ReactomeiREACT_331968. Gluconeogenesis.
REACT_338796. Citric acid cycle (TCA cycle).

Miscellaneous databases

NextBioi615775.
PROiP04636.

Gene expression databases

GenevestigatoriP04636.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010097. Malate_DH_type1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and nucleotide sequence of a cDNA clone encoding rat mitochondrial malate dehydrogenase."
    Grant P.M., Tellam J., May V.L., Strauss A.W.
    Nucleic Acids Res. 14:6053-6066(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary anterior lobe.
  3. "Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenase."
    Grant P.M., Roderick S.L., Grant G.A., Banaszak L.J., Strauss A.W.
    Biochemistry 26:128-134(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-338.
  4. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 27-52; 53-74; 166-185; 192-203; 216-239; 242-296 AND 308-324, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  5. "Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
    Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
    Reproduction 138:81-93(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  6. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
    Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
    PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-33.

Entry informationi

Entry nameiMDHM_RAT
AccessioniPrimary (citable) accession number: P04636
Secondary accession number(s): Q6GSM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 9, 2007
Last modified: April 1, 2015
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.