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Probable D-lactate dehydrogenase, mitochondrial (DLD) (Lactate dehydrogenase D) (EC 1.1.2.4)

 LDHD_MOUSE              Reviewed;         484 AA.
Q7TNG8; Q8BYU7; Q8CIV4;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
25-OCT-2017, entry version 109.
RecName: Full=Probable D-lactate dehydrogenase, mitochondrial;
Short=DLD;
Short=Lactate dehydrogenase D;
EC=1.1.2.4;
Flags: Precursor;
Name=Ldhd {ECO:0000312|MGI:MGI:106428};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAM50323.1}
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CSRP3, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
STRAIN=129/Sv {ECO:0000312|EMBL:AAM50323.1};
PubMed=12127981; DOI=10.1016/S0006-291X(02)00768-4;
Flick M.J., Konieczny S.F.;
"Identification of putative mammalian D-lactate dehydrogenase
enzymes.";
Biochem. Biophys. Res. Commun. 295:910-916(2002).
[2] {ECO:0000305, ECO:0000312|EMBL:AAH39155.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N {ECO:0000312|EMBL:AAH39155.1};
TISSUE=Kidney {ECO:0000312|EMBL:AAH39155.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
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] {ECO:0000305, ECO:0000312|EMBL:BAC29917.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-430.
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29917.1};
TISSUE=Thymus {ECO:0000312|EMBL:BAC29917.1};
PubMed=16141072; DOI=10.1126/science.1112014;
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).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-335, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
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.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-292; LYS-335;
LYS-422 AND LYS-449, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
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.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- CATALYTIC ACTIVITY: (R)-lactate + 2 ferricytochrome c = pyruvate +
2 ferrocytochrome c + 2 H(+).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:P39976};
-!- SUBUNIT: Interacts with CSRP3. {ECO:0000269|PubMed:12127981}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12127981}.
-!- TISSUE SPECIFICITY: Readily detected in liver and kidney, with a
weaker signal observed in heart, skeletal muscle, stomach, brain,
and lung. {ECO:0000269|PubMed:12127981}.
-!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase
type 4 family. {ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=AAM50323.1; Type=Frameshift; Positions=459, 474; Evidence={ECO:0000305};
Sequence=BAC29917.1; Type=Frameshift; Positions=141, 229, 315; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY092768; AAM50323.1; ALT_FRAME; mRNA.
EMBL; BC039155; AAH39155.1; -; mRNA.
EMBL; BC055443; AAH55443.1; -; mRNA.
EMBL; AK037996; BAC29917.1; ALT_FRAME; mRNA.
CCDS; CCDS22677.1; -.
RefSeq; NP_081846.3; NM_027570.3.
UniGene; Mm.271578; -.
UniGene; Mm.27589; -.
ProteinModelPortal; Q7TNG8; -.
SMR; Q7TNG8; -.
IntAct; Q7TNG8; 2.
MINT; MINT-4116468; -.
STRING; 10090.ENSMUSP00000068086; -.
iPTMnet; Q7TNG8; -.
PhosphoSitePlus; Q7TNG8; -.
MaxQB; Q7TNG8; -.
PaxDb; Q7TNG8; -.
PeptideAtlas; Q7TNG8; -.
PRIDE; Q7TNG8; -.
Ensembl; ENSMUST00000070004; ENSMUSP00000068086; ENSMUSG00000031958.
GeneID; 52815; -.
KEGG; mmu:52815; -.
UCSC; uc009nmn.1; mouse.
CTD; 197257; -.
MGI; MGI:106428; Ldhd.
eggNOG; KOG1231; Eukaryota.
eggNOG; COG0277; LUCA.
GeneTree; ENSGT00530000063515; -.
HOGENOM; HOG000230995; -.
HOVERGEN; HBG066407; -.
InParanoid; Q7TNG8; -.
KO; K00102; -.
OMA; TPRTCGE; -.
OrthoDB; EOG091G0BAW; -.
PhylomeDB; Q7TNG8; -.
TreeFam; TF314122; -.
PRO; PR:Q7TNG8; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031958; -.
CleanEx; MM_LDHD; -.
Genevisible; Q7TNG8; MM.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
GO; GO:0008720; F:D-lactate dehydrogenase activity; NAS:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0006754; P:ATP biosynthetic process; NAS:UniProtKB.
Gene3D; 1.10.45.10; -; 1.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.465.10; -; 1.
InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_sub1.
InterPro; IPR016164; FAD-linked_Oxase-like_C.
InterPro; IPR004113; FAD-linked_oxidase_C.
InterPro; IPR006094; Oxid_FAD_bind_N.
InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
Pfam; PF02913; FAD-oxidase_C; 1.
Pfam; PF01565; FAD_binding_4; 1.
SUPFAM; SSF55103; SSF55103; 1.
SUPFAM; SSF56176; SSF56176; 1.
PROSITE; PS51387; FAD_PCMH; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion;
Oxidoreductase; Reference proteome; Transit peptide.
TRANSIT 1 ? Mitochondrion. {ECO:0000255}.
CHAIN ? 484 Probable D-lactate dehydrogenase,
mitochondrial.
/FTId=PRO_0000262953.
DOMAIN 62 242 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
MOD_RES 36 36 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 292 292 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 335 335 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 335 335 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 422 422 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 449 449 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
CONFLICT 413 413 D -> H (in Ref. 2; BAC29917).
{ECO:0000305}.
SEQUENCE 484 AA; 51848 MW; 78BDF31A861B9A82 CRC64;
MAMLLRVATQ RLSPWRSFCS RGSQGGLSQD FVEALKAVVG SPHVSTASAV REQHGHDESM
HRCQPPDAVV WPQNVDQVSR VASLCYNQGV PIIPFGTGTG VEGGVCAVQG GVCINLTHMD
QITELNTEDF SVVVEPGVTR KALNTHLRDS GLWFPVDPGA DASLCGMAAT GASGTNAVRY
GTMRDNVINL EVVLPDGRLL HTAGRGRHYR KSAAGYNLTG LFVGSEGTLG IITSTTLRLH
PAPEATVAAT CAFPSVQAAV DSTVQILQAA VPVARIEFLD DVMMDACNRH SKLNCPVAPT
LFLEFHGSQQ TLAEQLQRTE AITQDNGGSH FSWAKEAEKR NELWAARHNA WYAALALSPG
SKAYSTDVCV PISRLPEILV ETKEEIKASK LTGAIVGHVG DGNFHCILLV DPDDAEEQRR
VKAFAENLGR RALALGGTCT GEHGIGLGKR QLLQEEVGPV GVETMRQLKN TLDPRGLMNP
GKVL


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