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UniProtKB/Swiss-Prot entry Q7TNG8


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LDHD_MOUSE
Primary accession number Q7TNG8
Secondary accession numbers Q8BYU7 Q8CIV4
Integrated into Swiss-Prot on November 28, 2006
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 39)
Name and origin of the protein
Protein name Probable D-lactate dehydrogenase, mitochondrial [Precursor]
Synonyms Lactate dehydrogenase D
DLD
EC 1.1.2.4
Gene name
Name: Ldhd
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CSRP3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=129/Sv;
DOI=10.1016/S0006-291X(02)00768-4; PubMed=12127981 [NCBI, ExPASy, EBI, Israel, Japan]
Flick M.J., Konieczny S.F.;
"Identification of putative mammalian D-lactate dehydrogenase enzymes.";
Biochem. Biophys. Res. Commun. 295:910-916(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-430.
STRAIN=C57BL/6J;
TISSUE=Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY092768; AAM50323.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039155; AAH39155.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC055443; AAH55443.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK037996; BAC29917.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_081846.3; -.
UniGene Mm.271578
3D structure databases
ModBase Q7TNG8.
Organism-specific databases
MGI MGI:106428; Ldhd.
Gene expression databases
ArrayExpress Q7TNG8; -.
CleanEx MM_LDHD; -.
GermOnline ENSMUSG00000031958; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0008720; Molecular function: D-lactate dehydrogenase activity (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006754; Biological process: ATP biosynthetic process (non-traceable author statement from UniProtKB).
QuickGo view.
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 of domain structure.
Gene3D G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.
Pfam PF02913; FAD-oxidase_C; 1.
PF01565; FAD_binding_4; 1.
Pfam graphical view of domain structure.
PROSITE PS51387; FAD_PCMH; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q7TNG8.
ProtoNet Q7TNG8.
Genome annotation databases
Ensembl ENSMUSG00000031958; Mus musculus. [Contig view]
GeneID 52815; -.
KEGG mmu:52815; -.
Phylogenomic databases
HOVERGEN Q7TNG8; -.
Other
NextBio 309579; -.
SOURCE Ldhd; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   484        Probable D-lactate dehydrogenase, mitochondrial. PRO_0000262953
DOMAIN   62   242  181     FAD-binding PCMH-type. 
CONFLICT   413   413        D -> H (in Ref. 2; BAC29917). 
Sequence information
Length: 484 AA [This is the length of the unprocessed precursor] Molecular weight: 51848 Da [This is the MW of the unprocessed precursor] CRC64: 78BDF31A861B9A82 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAMLLRVATQ RLSPWRSFCS RGSQGGLSQD FVEALKAVVG SPHVSTASAV REQHGHDESM 

        70         80         90        100        110        120 
HRCQPPDAVV WPQNVDQVSR VASLCYNQGV PIIPFGTGTG VEGGVCAVQG GVCINLTHMD 

       130        140        150        160        170        180 
QITELNTEDF SVVVEPGVTR KALNTHLRDS GLWFPVDPGA DASLCGMAAT GASGTNAVRY 

       190        200        210        220        230        240 
GTMRDNVINL EVVLPDGRLL HTAGRGRHYR KSAAGYNLTG LFVGSEGTLG IITSTTLRLH 

       250        260        270        280        290        300 
PAPEATVAAT CAFPSVQAAV DSTVQILQAA VPVARIEFLD DVMMDACNRH SKLNCPVAPT 

       310        320        330        340        350        360 
LFLEFHGSQQ TLAEQLQRTE AITQDNGGSH FSWAKEAEKR NELWAARHNA WYAALALSPG 

       370        380        390        400        410        420 
SKAYSTDVCV PISRLPEILV ETKEEIKASK LTGAIVGHVG DGNFHCILLV DPDDAEEQRR 

       430        440        450        460        470        480 
VKAFAENLGR RALALGGTCT GEHGIGLGKR QLLQEEVGPV GVETMRQLKN TLDPRGLMNP 


GKVL 

Q7TNG8 in FASTA format

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