Reviewed,
UniProtKB/Swiss-Prot Q7TNG8 (LDHD_MOUSE)
Last modified
November 25, 2008.
Version 40.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable D-lactate dehydrogenase, mitochondrial Short name=Lactate dehydrogenase D Short name=DLD EC=1.1.2.4 | ||
| Gene names |
| ||
| 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 | 484 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 | (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c. |
| Cofactor | FAD By similarity. |
| Subunit structure | Interacts with CSRP3. |
| Subcellular location | |
| Tissue specificity | Readily detected in liver and kidney, with a weaker signal observed in heart, skeletal muscle, stomach, brain, and lung. |
| Sequence similarities | Belongs to the FAD-binding oxidoreductase/transferase type 4 family. Contains 1 FAD-binding PCMH-type domain. |
| Sequence caution | The sequence AAM50323.1 differs from that shown. Reason: Frameshift at positions 459 and 474. The sequence BAC29917.1 differs from that shown. Reason: Frameshift at positions 141, 229 and 315. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
Gene Ontology (GO) | |
| Biological process | ATP biosynthetic process Ref.1 Non-traceable author statement. Source: UniProtKB oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from direct assay. Source: UniProtKB |
| Molecular function | D-lactate dehydrogenase (cytochrome) activity Inferred from electronic annotation. Source: EC D-lactate dehydrogenase activity Ref.1Non-traceable author statement. Source: UniProtKB FAD bindingInferred from electronic annotation. Source: InterPro protein binding Ref.1Inferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 484 | Probable D-lactate dehydrogenase, mitochondrial | PRO_0000262953 | ||||||
Regions | |||||||||
| Domain | 62 – 242 | 181 | FAD-binding PCMH-type | ||||||
Experimental info | |||||||||
| Sequence conflict | 413 | 1 | D → H in BAC29917. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of putative mammalian D-lactate dehydrogenase enzymes." Flick M.J., Konieczny S.F. Biochem. Biophys. Res. Commun. 295:910-916(2002) [PubMed: 12127981] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CSRP3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: 129/Sv. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney. |
| [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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-430. Strain: C57BL/6J. Tissue: Thymus. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AY092768 mRNA. Translation: AAM50323.1. Frameshift. BC039155 mRNA. Translation: AAH39155.1. BC055443 mRNA. Translation: AAH55443.1. AK037996 mRNA. Translation: BAC29917.1. Frameshift. | |
| RefSeq | NP_081846.3. |
| UniGene | Mm.271578 Mm.27589 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUSG00000031958. Mus musculus. [Contig view] |
| GeneID | 52815. |
| KEGG | mmu:52815. |
Organism-specific databases | |
| MGI | MGI:106428. Ldhd. |
Phylogenomic databases | |
| HOVERGEN | Q7TNG8. |
Gene expression databases | |
| ArrayExpress | Q7TNG8. |
| CleanEx | MM_LDHD. |
| GermOnline | ENSMUSG00000031958. Mus musculus. |
Family and domain databases | |
| InterPro | IPR016167. FAD-bd_2_sub1. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR004113. FAD-linked_oxidase_C. IPR006094. Oxid_FAD_bind_N. [Graphical view] |
| Gene3D | G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit. |
| Pfam | PF02913. FAD-oxidase_C. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view] |
| PROSITE | PS51387. FAD_PCMH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 309579. |
| SOURCE | Search... |
Entry information
| Entry name | LDHD_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q7TNG8 Secondary accession number(s): Q8BYU7, Q8CIV4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

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