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Database: UniProt
Entry: Q564E2_MOUSE
LinkDB: Q564E2_MOUSE
Original site: Q564E2_MOUSE 
ID   Q564E2_MOUSE            Unreviewed;       332 AA.
AC   Q564E2; G5E8N5;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|RuleBase:RU000496};
DE            EC=1.1.1.27 {ECO:0000256|RuleBase:RU000496};
GN   Name=Ldha {ECO:0000313|EMBL:AAH94019.1, ECO:0000313|MGI:MGI:96759};
GN   Synonyms=Ldh1 {ECO:0000313|MGI:MGI:96759};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAC41000.1};
RN   [1] {ECO:0000313|EMBL:BAC41000.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29347.1}, DBA/2
RC   {ECO:0000313|EMBL:BAE39819.1}, and NOD {ECO:0000313|EMBL:BAE41760.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE29347.1}, Heart
RC   {ECO:0000313|EMBL:BAE40733.1}, and Kidney
RC   {ECO:0000313|EMBL:BAC41000.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAC41000.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29347.1}, DBA/2
RC   {ECO:0000313|EMBL:BAE39819.1}, and NOD {ECO:0000313|EMBL:BAE41760.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE29347.1}, Heart
RC   {ECO:0000313|EMBL:BAE40733.1}, and Kidney
RC   {ECO:0000313|EMBL:BAC41000.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAC41000.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29347.1}, DBA/2
RC   {ECO:0000313|EMBL:BAE39819.1}, and NOD {ECO:0000313|EMBL:BAE41760.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE29347.1}, Heart
RC   {ECO:0000313|EMBL:BAE40733.1}, and Kidney
RC   {ECO:0000313|EMBL:BAC41000.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAC41000.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29347.1}, DBA/2
RC   {ECO:0000313|EMBL:BAE39819.1}, and NOD {ECO:0000313|EMBL:BAE41760.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE29347.1}, Heart
RC   {ECO:0000313|EMBL:BAE40733.1}, and Kidney
RC   {ECO:0000313|EMBL:BAC41000.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAC41000.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29347.1}, DBA/2
RC   {ECO:0000313|EMBL:BAE39819.1}, and NOD {ECO:0000313|EMBL:BAE41760.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE29347.1}, Heart
RC   {ECO:0000313|EMBL:BAE40733.1}, and Kidney
RC   {ECO:0000313|EMBL:BAC41000.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:BAC41000.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Kidney {ECO:0000313|EMBL:BAC41000.1};
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K.,
RA   Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y.,
RA   Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T.,
RA   Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R.,
RA   Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K.,
RA   Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S.,
RA   Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M.,
RA   Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:AAH94019.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH94428.1}, and FVB/N
RC   {ECO:0000313|EMBL:AAH94019.1};
RC   TISSUE=Brain {ECO:0000313|EMBL:AAH94428.1}, and Liver
RC   {ECO:0000313|EMBL:AAH94019.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8] {ECO:0000313|EMBL:BAE39819.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29347.1}, DBA/2
RC   {ECO:0000313|EMBL:BAE39819.1}, and NOD {ECO:0000313|EMBL:BAE41760.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE29347.1}, and Heart
RC   {ECO:0000313|EMBL:BAE40733.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:BAC41000.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29347.1}, DBA/2
RC   {ECO:0000313|EMBL:BAE39819.1}, and NOD {ECO:0000313|EMBL:BAE41760.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE29347.1}, Heart
RC   {ECO:0000313|EMBL:BAE40733.1}, and Kidney
RC   {ECO:0000313|EMBL:BAC41000.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [10] {ECO:0000313|EMBL:BAC41000.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29347.1}, DBA/2
RC   {ECO:0000313|EMBL:BAE39819.1}, and NOD {ECO:0000313|EMBL:BAE41760.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE29347.1}, Heart
RC   {ECO:0000313|EMBL:BAE40733.1}, and Kidney
RC   {ECO:0000313|EMBL:BAC41000.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [11] {ECO:0007829|PubMed:17947660}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [12] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [13] {ECO:0007829|PubMed:23806337}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC         Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC         Evidence={ECO:0000256|RuleBase:RU000496};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843,
CC       ECO:0000256|RuleBase:RU000496}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054}.
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DR   EMBL; BC094019; AAH94019.1; -; mRNA.
DR   EMBL; BC094428; AAH94428.1; -; mRNA.
DR   EMBL; AK089929; BAC41000.1; -; mRNA.
DR   EMBL; AK150156; BAE29347.1; -; mRNA.
DR   EMBL; AK167789; BAE39819.1; -; mRNA.
DR   EMBL; AK168920; BAE40733.1; -; mRNA.
DR   EMBL; AK170386; BAE41760.1; -; mRNA.
DR   RefSeq; NP_001129541.2; NM_001136069.2.
DR   RefSeq; NP_034829.1; NM_010699.2.
DR   AlphaFoldDB; Q564E2; -.
DR   SMR; Q564E2; -.
DR   IntAct; Q564E2; 1.
DR   MINT; Q564E2; -.
DR   MaxQB; Q564E2; -.
DR   ProteomicsDB; 343100; -.
DR   Antibodypedia; 4200; 1029 antibodies from 40 providers.
DR   DNASU; 16828; -.
DR   GeneID; 16828; -.
DR   KEGG; mmu:16828; -.
DR   UCSC; uc009gzo.2; mouse.
DR   AGR; MGI:96759; -.
DR   CTD; 3939; -.
DR   MGI; MGI:96759; Ldha.
DR   VEuPathDB; HostDB:ENSMUSG00000063229; -.
DR   HOGENOM; CLU_045401_0_2_1; -.
DR   OMA; IKKHCPQ; -.
DR   OrthoDB; 5344346at2759; -.
DR   UniPathway; UPA00554; UER00611.
DR   BioGRID-ORCS; 16828; 24 hits in 75 CRISPR screens.
DR   ChiTaRS; Ldha; mouse.
DR   ExpressionAtlas; Q564E2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006089; P:lactate metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   CDD; cd05293; LDH_1; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00488; Lactate_dehydrog; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR011304; L-lactate_DH.
DR   InterPro; IPR018177; L-lactate_DH_AS.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01771; L-LDH-NAD; 1.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF10; L-LACTATE DEHYDROGENASE A CHAIN; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00064; L_LDH; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000496}.
FT   DOMAIN          22..160
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          164..324
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         27..32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         52
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         136..138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   332 AA;  36499 MW;  5AEB41E1E0B95100 CRC64;
     MATLKDQLIV NLLKEEQAPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVMEDKLKG
     EMMDLQHGSL FLKTPKIVSS KDYCVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI
     IPNIVKYSPH CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV
     HALSCHGWVL GEHGDSSVPV WSGVNVAGVS LKSLNPELGT DADKEQWKEV HKQVVDSAYE
     VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGINEDVFLS VPCILGQNGI
     SDVVKVTLTP EEEARLKKSA DTLWGIQKEL QF
//
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