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Protein

Probable D-lactate dehydrogenase, mitochondrial

Gene

Ldhd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+.

Cofactori

FADBy similarity

GO - Molecular functioni

GO - Biological processi

  • ATP biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-2845-MONOMER.
RETL1328306-WGS:GSTH-4547-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable D-lactate dehydrogenase, mitochondrial (EC:1.1.2.4)
Short name:
DLD
Short name:
Lactate dehydrogenase D
Gene namesi
Name:LdhdImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:106428. Ldhd.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: Ensembl
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 484Probable D-lactate dehydrogenase, mitochondrialPRO_0000262953
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6-acetyllysineCombined sources
Modified residuei292 – 2921N6-acetyllysineCombined sources
Modified residuei335 – 3351N6-acetyllysine; alternateCombined sources
Modified residuei335 – 3351N6-succinyllysine; alternateCombined sources
Modified residuei422 – 4221N6-acetyllysineCombined sources
Modified residuei449 – 4491N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ7TNG8.
MaxQBiQ7TNG8.
PaxDbiQ7TNG8.
PRIDEiQ7TNG8.

PTM databases

iPTMnetiQ7TNG8.
PhosphoSiteiQ7TNG8.

Expressioni

Tissue specificityi

Readily detected in liver and kidney, with a weaker signal observed in heart, skeletal muscle, stomach, brain, and lung.1 Publication

Gene expression databases

BgeeiQ7TNG8.
CleanExiMM_LDHD.
GenevisibleiQ7TNG8. MM.

Interactioni

Subunit structurei

Interacts with CSRP3.1 Publication

Protein-protein interaction databases

IntActiQ7TNG8. 2 interactions.
MINTiMINT-4116468.
STRINGi10090.ENSMUSP00000068086.

Structurei

3D structure databases

ProteinModelPortaliQ7TNG8.
SMRiQ7TNG8. Positions 27-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 242181FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1231. Eukaryota.
COG0277. LUCA.
GeneTreeiENSGT00530000063515.
HOGENOMiHOG000230995.
HOVERGENiHBG066407.
InParanoidiQ7TNG8.
KOiK00102.
OMAiICYGYDA.
OrthoDBiEOG7QNVKV.
PhylomeDBiQ7TNG8.
TreeFamiTF314122.

Family and domain databases

Gene3Di1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q7TNG8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMLLRVATQ RLSPWRSFCS RGSQGGLSQD FVEALKAVVG SPHVSTASAV
60 70 80 90 100
REQHGHDESM HRCQPPDAVV WPQNVDQVSR VASLCYNQGV PIIPFGTGTG
110 120 130 140 150
VEGGVCAVQG GVCINLTHMD QITELNTEDF SVVVEPGVTR KALNTHLRDS
160 170 180 190 200
GLWFPVDPGA DASLCGMAAT GASGTNAVRY GTMRDNVINL EVVLPDGRLL
210 220 230 240 250
HTAGRGRHYR KSAAGYNLTG LFVGSEGTLG IITSTTLRLH PAPEATVAAT
260 270 280 290 300
CAFPSVQAAV DSTVQILQAA VPVARIEFLD DVMMDACNRH SKLNCPVAPT
310 320 330 340 350
LFLEFHGSQQ TLAEQLQRTE AITQDNGGSH FSWAKEAEKR NELWAARHNA
360 370 380 390 400
WYAALALSPG SKAYSTDVCV PISRLPEILV ETKEEIKASK LTGAIVGHVG
410 420 430 440 450
DGNFHCILLV DPDDAEEQRR VKAFAENLGR RALALGGTCT GEHGIGLGKR
460 470 480
QLLQEEVGPV GVETMRQLKN TLDPRGLMNP GKVL
Length:484
Mass (Da):51,848
Last modified:October 1, 2003 - v1
Checksum:i78BDF31A861B9A82
GO

Sequence cautioni

The sequence AAM50323.1 differs from that shown. Reason: Frameshift at positions 459 and 474. Curated
The sequence BAC29917.1 differs from that shown. Reason: Frameshift at positions 141, 229 and 315. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti413 – 4131D → H in BAC29917 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY092768 mRNA. Translation: AAM50323.1. Frameshift.
BC039155 mRNA. Translation: AAH39155.1.
BC055443 mRNA. Translation: AAH55443.1.
AK037996 mRNA. Translation: BAC29917.1. Frameshift.
CCDSiCCDS22677.1.
RefSeqiNP_081846.3. NM_027570.3.
UniGeneiMm.271578.
Mm.27589.

Genome annotation databases

EnsembliENSMUST00000070004; ENSMUSP00000068086; ENSMUSG00000031958.
GeneIDi52815.
KEGGimmu:52815.
UCSCiuc009nmn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY092768 mRNA. Translation: AAM50323.1. Frameshift.
BC039155 mRNA. Translation: AAH39155.1.
BC055443 mRNA. Translation: AAH55443.1.
AK037996 mRNA. Translation: BAC29917.1. Frameshift.
CCDSiCCDS22677.1.
RefSeqiNP_081846.3. NM_027570.3.
UniGeneiMm.271578.
Mm.27589.

3D structure databases

ProteinModelPortaliQ7TNG8.
SMRiQ7TNG8. Positions 27-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7TNG8. 2 interactions.
MINTiMINT-4116468.
STRINGi10090.ENSMUSP00000068086.

PTM databases

iPTMnetiQ7TNG8.
PhosphoSiteiQ7TNG8.

Proteomic databases

EPDiQ7TNG8.
MaxQBiQ7TNG8.
PaxDbiQ7TNG8.
PRIDEiQ7TNG8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070004; ENSMUSP00000068086; ENSMUSG00000031958.
GeneIDi52815.
KEGGimmu:52815.
UCSCiuc009nmn.1. mouse.

Organism-specific databases

CTDi197257.
MGIiMGI:106428. Ldhd.

Phylogenomic databases

eggNOGiKOG1231. Eukaryota.
COG0277. LUCA.
GeneTreeiENSGT00530000063515.
HOGENOMiHOG000230995.
HOVERGENiHBG066407.
InParanoidiQ7TNG8.
KOiK00102.
OMAiICYGYDA.
OrthoDBiEOG7QNVKV.
PhylomeDBiQ7TNG8.
TreeFamiTF314122.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-2845-MONOMER.
RETL1328306-WGS:GSTH-4547-MONOMER.

Miscellaneous databases

NextBioi309579.
PROiQ7TNG8.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TNG8.
CleanExiMM_LDHD.
GenevisibleiQ7TNG8. MM.

Family and domain databases

Gene3Di1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of putative mammalian D-lactate dehydrogenase enzymes."
    Flick M.J., Konieczny S.F.
    Biochem. Biophys. Res. Commun. 295:910-916(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CSRP3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: 129/SvImported.
  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].
    Strain: FVB/NImported.
    Tissue: KidneyImported.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-430.
    Strain: C57BL/6JImported.
    Tissue: ThymusImported.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney and Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-292; LYS-335; LYS-422 AND LYS-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiLDHD_MOUSE
AccessioniPrimary (citable) accession number: Q7TNG8
Secondary accession number(s): Q8BYU7, Q8CIV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 1, 2003
Last modified: March 16, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.