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L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (LDH muscle subunit) (LDH-M)

 LDHA_MOUSE              Reviewed;         332 AA.
P06151;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 177.
RecName: Full=L-lactate dehydrogenase A chain;
Short=LDH-A;
EC=1.1.1.27;
AltName: Full=LDH muscle subunit;
Short=LDH-M;
Name=Ldha; Synonyms=Ldh-1, Ldh1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/10; TISSUE=Liver;
PubMed=3036647;
Fukasawa K.M., Li S.S.-L.;
"Complete nucleotide sequence of the mouse lactate dehydrogenase-A
functional gene: comparison of the exon-intron organization of
dehydrogenase genes.";
Genetics 116:99-105(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3996406; DOI=10.1111/j.1432-1033.1985.tb08914.x;
Li S.S.-L., Tiano H.F., Fukasawa K.M., Yagi K., Shimizu M.,
Sharief F.S., Nakashima Y., Pan Y.E.;
"Protein structure and gene organization of mouse lactate
dehydrogenase-A isozyme.";
Eur. J. Biochem. 149:215-225(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=DBA/2J;
Hiraoka Y., Li S.S.-L.;
"Lactate dehydrogenase-A mRNAs in mouse testis and somatic tissues
containing different 5' noncoding sequences.";
J. Genet. Mol. Biol. 1:1-6(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
PubMed=3017306; DOI=10.1042/bj2350435;
Fukasawa K.M., Li S.S.-L.;
"Nucleotide sequence of the putative regulatory region of mouse
lactate dehydrogenase-A gene.";
Biochem. J. 235:435-439(1986).
[5]
PROTEIN SEQUENCE OF 6-14; 23-73; 82-99; 107-126; 133-149; 158-169;
172-177; 213-228; 233-243; 246-265; 269-315 AND 319-328, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 202-332.
PubMed=2993055; DOI=10.1016/0020-711X(85)90298-8;
Akai K., Yagi K., Tiano H.F., Pan Y.-C.E., Shimizu M., Fong K.,
Jungmann R.A., Li S.S.-L.;
"Isolation and characterization of a cDNA and a pseudogene for mouse
lactate dehydrogenase-A isozyme.";
Int. J. Biochem. 17:645-648(1985).
[7]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-5; LYS-81; LYS-118;
LYS-126; LYS-224; LYS-232; LYS-243 AND LYS-318, SUCCINYLATION [LARGE
SCALE ANALYSIS] AT LYS-5; LYS-118 AND LYS-318, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast, and 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).
-!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
-!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
lactate from pyruvate: step 1/1.
-!- SUBUNIT: Homotetramer.
-!- INTERACTION:
Q60668:Hnrnpd; NbExp=2; IntAct=EBI-444940, EBI-299932;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y00309; CAA68410.1; -; Genomic_DNA.
EMBL; X02520; CAA26360.1; -; Genomic_DNA.
EMBL; X02521; CAA26360.1; JOINED; Genomic_DNA.
EMBL; X02522; CAA26360.1; JOINED; Genomic_DNA.
EMBL; X02523; CAA26360.1; JOINED; Genomic_DNA.
EMBL; X02524; CAA26360.1; JOINED; Genomic_DNA.
EMBL; X02525; CAA26360.1; JOINED; Genomic_DNA.
EMBL; X02526; CAA26360.1; JOINED; Genomic_DNA.
EMBL; U13687; AAA21466.1; -; mRNA.
EMBL; X03753; CAA27387.1; -; Genomic_DNA.
EMBL; M17516; AAA39424.1; -; mRNA.
CCDS; CCDS21289.1; -.
PIR; A25205; DEMSLM.
PIR; I48240; I48240.
RefSeq; NP_034829.1; NM_010699.2.
UniGene; Mm.29324; -.
ProteinModelPortal; P06151; -.
SMR; P06151; -.
BioGrid; 201127; 9.
IntAct; P06151; 22.
MINT; MINT-1612559; -.
STRING; 10090.ENSMUSP00000103267; -.
iPTMnet; P06151; -.
PhosphoSitePlus; P06151; -.
SwissPalm; P06151; -.
REPRODUCTION-2DPAGE; P06151; -.
SWISS-2DPAGE; P06151; -.
UCD-2DPAGE; P06151; -.
EPD; P06151; -.
PaxDb; P06151; -.
PeptideAtlas; P06151; -.
PRIDE; P06151; -.
TopDownProteomics; P06151; -.
Ensembl; ENSMUST00000005051; ENSMUSP00000103267; ENSMUSG00000063229.
Ensembl; ENSMUST00000048209; ENSMUSP00000036386; ENSMUSG00000063229.
GeneID; 16828; -.
KEGG; mmu:16828; -.
UCSC; uc009gzm.2; mouse.
CTD; 3939; -.
MGI; MGI:96759; Ldha.
eggNOG; KOG1495; Eukaryota.
eggNOG; COG0039; LUCA.
GeneTree; ENSGT00550000074541; -.
HOGENOM; HOG000213793; -.
HOVERGEN; HBG000462; -.
InParanoid; P06151; -.
KO; K00016; -.
PhylomeDB; P06151; -.
Reactome; R-MMU-70268; Pyruvate metabolism.
UniPathway; UPA00554; UER00611.
ChiTaRS; Ldha; mouse.
PRO; PR:P06151; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000063229; -.
CleanEx; MM_LDHA; -.
ExpressionAtlas; P06151; baseline and differential.
Genevisible; P06151; MM.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0035686; C:sperm fibrous sheath; IDA:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:MGI.
GO; GO:0004457; F:lactate dehydrogenase activity; IMP:MGI.
GO; GO:0031668; P:cellular response to extracellular stimulus; IDA:MGI.
GO; GO:0019661; P:glucose catabolic process to lactate via pyruvate; IMP:MGI.
GO; GO:0019244; P:lactate biosynthetic process from pyruvate; IC:MGI.
Gene3D; 3.90.110.10; -; 1.
HAMAP; MF_00488; Lactate_dehydrog; 1.
InterPro; IPR001557; L-lactate/malate_DH.
InterPro; IPR011304; L-lactate_DH.
InterPro; IPR018177; L-lactate_DH_AS.
InterPro; IPR022383; Lactate/malate_DH_C.
InterPro; IPR001236; Lactate/malate_DH_N.
InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF02866; Ldh_1_C; 1.
Pfam; PF00056; Ldh_1_N; 1.
PIRSF; PIRSF000102; Lac_mal_DH; 1.
PRINTS; PR00086; LLDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF56327; SSF56327; 1.
TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
PROSITE; PS00064; L_LDH; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; NAD; Oxidoreductase; Phosphoprotein;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:23806337}.
CHAIN 2 332 L-lactate dehydrogenase A chain.
/FTId=PRO_0000168414.
NP_BIND 29 57 NAD. {ECO:0000250}.
ACT_SITE 193 193 Proton acceptor. {ECO:0000250}.
BINDING 99 99 NAD. {ECO:0000250}.
BINDING 106 106 Substrate. {ECO:0000250}.
BINDING 138 138 NAD or substrate. {ECO:0000250}.
BINDING 169 169 Substrate. {ECO:0000250}.
BINDING 248 248 Substrate. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 5 5 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 14 14 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 57 57 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 81 81 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 118 118 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 118 118 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 126 126 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 224 224 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 232 232 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 239 239 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 243 243 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 309 309 Phosphothreonine.
{ECO:0000250|UniProtKB:P04642}.
MOD_RES 318 318 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 318 318 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 322 322 Phosphothreonine.
{ECO:0000250|UniProtKB:P04642}.
CROSSLNK 57 57 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P00338}.
CONFLICT 11 11 N -> I (in Ref. 2). {ECO:0000305}.
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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