ID LDHA_MOUSE Reviewed; 332 AA. AC P06151; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 99. DE RecName: Full=L-lactate dehydrogenase A chain; DE Short=LDH-A; DE EC=1.1.1.27; DE AltName: Full=LDH muscle subunit; DE Short=LDH-M; GN Name=Ldha; Synonyms=Ldh-1, Ldh1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/10; TISSUE=Liver; RX MEDLINE=87248042; PubMed=3036647; RA Fukasawa K.M., Li S.S.-L.; RT "Complete nucleotide sequence of the mouse lactate dehydrogenase-A RT functional gene: comparison of the exon-intron organization of RT dehydrogenase genes."; RL Genetics 116:99-105(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=85203900; PubMed=3996406; RX DOI=10.1111/j.1432-1033.1985.tb08914.x; RA Li S.S.-L., Tiano H.F., Fukasawa K.M., Yagi K., Shimizu M., RA Sharief F.S., Nakashima Y., Pan Y.E.; RT "Protein structure and gene organization of mouse lactate RT dehydrogenase-A isozyme."; RL Eur. J. Biochem. 149:215-225(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=DBA/2J; RA Hiraoka Y., Li S.S.-L.; RT "Lactate dehydrogenase-A mRNAs in mouse testis and somatic tissues RT containing different 5' noncoding sequences."; RL J. Genet. Mol. Biol. 1:1-6(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. RX MEDLINE=86295627; PubMed=3017306; RA Fukasawa K.M., Li S.S.-L.; RT "Nucleotide sequence of the putative regulatory region of mouse RT lactate dehydrogenase-A gene."; RL Biochem. J. 235:435-439(1986). RN [5] RP PROTEIN SEQUENCE OF 6-14; 23-73; 82-99; 107-126; 133-149; 158-169; RP 172-177; 213-228; 233-243; 246-265; 269-315 AND 319-328, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., RA Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 202-332. RX MEDLINE=85285968; PubMed=2993055; DOI=10.1016/0020-711X(85)90298-8; RA Akai K., Yagi K., Tiano H.F., Pan Y.-C.E., Shimizu M., Fong K., RA Jungmann R.A., Li S.S.-L.; RT "Isolation and characterization of a cDNA and a pseudogene for mouse RT lactate dehydrogenase-A isozyme."; RL Int. J. Biochem. 17:645-648(1985). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND MASS RP SPECTROMETRY. RC TISSUE=Mast cell; 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND MASS RP SPECTROMETRY. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)- CC lactate from pyruvate: step 1/1. CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC Q60668:Hnrnpd; NbExp=2; IntAct=EBI-444940, EBI-299932; CC Q9JHG7:Pik3cg; NbExp=2; IntAct=EBI-444940, EBI-644372; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y00309; CAA68410.1; -; Genomic_DNA. DR EMBL; X02520; CAA26360.1; -; Genomic_DNA. DR EMBL; X02521; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; X02522; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; X02523; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; X02524; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; X02525; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; X02526; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; U13687; AAA21466.1; -; mRNA. DR EMBL; X03753; CAA27387.1; -; Genomic_DNA. DR EMBL; M17516; AAA39424.1; -; mRNA. DR IPI; IPI00319994; -. DR PIR; A25205; DEMSLM. DR PIR; I48240; I48240. DR RefSeq; NP_001129541.1; -. DR RefSeq; NP_034829.1; -. DR UniGene; Mm.26751; -. DR UniGene; Mm.29324; -. DR HSSP; P00338; 1I10. DR SMR; P06151; 2-332. DR IntAct; P06151; 4. DR PhosphoSite; P06151; -. DR SWISS-2DPAGE; P06151; -. DR REPRODUCTION-2DPAGE; P06151; -. DR PRIDE; P06151; -. DR Ensembl; ENSMUSG00000063229; Mus musculus. DR GeneID; 16828; -. DR KEGG; mmu:16828; -. DR MGI; MGI:96759; Ldha. DR HOGENOM; P06151; -. DR HOVERGEN; P06151; -. DR BRENDA; 1.1.1.27; 244. DR NextBio; 290734; -. DR ArrayExpress; P06151; -. DR Bgee; P06151; -. DR CleanEx; MM_LDHA; -. DR GermOnline; ENSMUSG00000063229; Mus musculus. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0019861; C:flagellum; IDA:MGI. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:MGI. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0019642; P:anaerobic glycolysis; IEA:InterPro. DR GO; GO:0031668; P:cellular response to extracellular stimulus; IDA:MGI. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR011304; L-lactate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR001236; Lactate/malate_DH. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 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 TIGRFAMs; TIGR01771; L-LDH-NAD; 1. DR PROSITE; PS00064; L_LDH; 1. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Glycolysis; NAD; KW Oxidoreductase; Phosphoprotein. FT INIT_MET 1 1 Removed. FT CHAIN 2 332 L-lactate dehydrogenase A chain. FT /FTId=PRO_0000168414. FT NP_BIND 29 57 NAD (By similarity). FT ACT_SITE 193 193 Proton acceptor (By similarity). FT BINDING 99 99 NAD (By similarity). FT BINDING 106 106 Substrate (By similarity). FT BINDING 138 138 NAD or substrate (By similarity). FT BINDING 169 169 Substrate (By similarity). FT BINDING 248 248 Substrate (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 239 239 Phosphotyrosine. FT CONFLICT 11 11 N -> I (in Ref. 2). 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 //