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Q7TNG8 (LDHD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable D-lactate dehydrogenase, mitochondrial
Short name=DLD
Short name=Lactate dehydrogenase D
EC=1.1.2.4
Gene names
Name:Ldhd
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

FAD By similarity. UniProtKB P39976

Subunit structure

Interacts with CSRP3. Ref.1

Subcellular location

Mitochondrion Ref.1.

Tissue specificity

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 484Probable D-lactate dehydrogenase, mitochondrialPRO_0000262953

Regions

Domain62 – 242181FAD-binding PCMH-type

Experimental info

Sequence conflict4131D → H in BAC29917. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q7TNG8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 78BDF31A861B9A82

FASTA48451,848
        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

« Hide

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. expand/collapse author list , 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: 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

EMBL
GenBank
DDBJ		AY092768 mRNA. Translation: AAM50323.1. Frameshift.
BC039155 mRNA. Translation: AAH39155.1.
BC055443 mRNA. Translation: AAH55443.1.
AK037996 mRNA. Translation: BAC29917.1. Frameshift.
IPIIPI00380320.
RefSeqNP_081846.3. NM_027570.3.
UniGeneMm.271578.
Mm.27589.

3D structure databases

ProteinModelPortalQ7TNG8.
SMRQ7TNG8. Positions 26-484.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7TNG8.

Proteomic databases

PRIDEQ7TNG8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070004; ENSMUSP00000068086; ENSMUSG00000031958.
GeneID52815.
KEGGmmu:52815.
UCSCuc009nmn.1. mouse.

Organism-specific databases

CTD197257.
MGIMGI:106428. Ldhd.

Phylogenomic databases

eggNOGroNOG06984.
GeneTreeENSGT00530000063515.
HOGENOMHBG553036.
HOVERGENHBG066407.
InParanoidQ7TNG8.
OMALLRCELM.
PhylomeDBQ7TNG8.

Gene expression databases

ArrayExpressQ7TNG8.
BgeeQ7TNG8.
CleanExMM_LDHD.
GenevestigatorQ7TNG8.
GermOnlineENSMUSG00000031958. Mus musculus.

Family and domain databases

InterProIPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR016168. FAD-linked_Oxase_FAD-bd_sub2.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
Gene3DG3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit.
G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit.
G3DSA:1.10.45.10. Vanillyl_alc_oxidase_C-sub2. 1 hit.
KOK00102.
PfamPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMSSF55103. FAD-binding_2. 1 hit.
SSF56176. FAD-binding_2. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio309579.
SOURCESearch...

Entry information

Entry nameLDHD_MOUSE
AccessionPrimary (citable) accession number: Q7TNG8
Secondary accession number(s): Q8BYU7, Q8CIV4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 1, 2003
Last modified: November 16, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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