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

 LDHA_RAT                Reviewed;         332 AA.
P04642;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
23-MAY-2018, entry version 168.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3873645; DOI=10.1093/nar/13.3.711;
Matrisian L.M., Rautmann G., Magun B.E., Breathnach R.;
"Epidermal growth factor or serum stimulation of rat fibroblasts
induces an elevation in mRNA levels for lactate dehydrogenase and
other glycolytic enzymes.";
Nucleic Acids Res. 13:711-726(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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]
PROTEIN SEQUENCE OF 2-14; 43-57; 91-99; 107-112; 119-126; 233-243;
306-315 AND 319-328, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fibroblast, and Pheochromocytoma;
Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
Submitted (JUN-2009) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 82-99; 127-132; 156-157; 170-190; 234-245; 306-315
AND 319-328.
PubMed=2991914; DOI=10.1073/pnas.82.16.5260;
Williams K.R., Reddigari S., Patel G.L.;
"Identification of a nucleic acid helix-destabilizing protein from rat
liver as lactate dehydrogenase-5.";
Proc. Natl. Acad. Sci. U.S.A. 82:5260-5264(1985).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 274-332.
TISSUE=Liver;
Bae S.C., Lee S.K.;
"Characterization of the folding structure of 3'-end of lactate
dehydrogenase A-mRNA isolated from hormone stimulated rat C-6 glioma
cell culture.";
J. Microbiol. 25:94-102(1987).
[6]
PROTEIN SEQUENCE OF 319-328, AND IDENTIFICATION BY MASS SPECTROMETRY.
Lubec G., Chen W.-Q.;
Submitted (SEP-2006) to UniProtKB.
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; TYR-239; THR-309
AND THR-322, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
-!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
lactate from pyruvate: step 1/1.
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- PTM: ISGylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
{ECO:0000305}.
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EMBL; X01964; CAA26000.1; -; mRNA.
EMBL; BC084698; AAH84698.1; -; mRNA.
EMBL; M54926; AAA41508.1; -; mRNA.
PIR; A23083; A23083.
RefSeq; NP_058721.1; NM_017025.1.
UniGene; Rn.107896; -.
PDB; 4AJ1; X-ray; 1.87 A; A/B/C/D=2-332.
PDB; 4AJ2; X-ray; 1.75 A; A/B/C/D=2-332.
PDB; 4AJ4; X-ray; 1.90 A; A/B/C/D=1-332.
PDB; 4AJE; X-ray; 2.35 A; A/B/C/D=2-332.
PDB; 4AJH; X-ray; 1.93 A; A/B/C/D=2-332.
PDB; 4AJI; X-ray; 1.93 A; A/B/C/D=2-332.
PDB; 4AJJ; X-ray; 1.75 A; A/B/C/D=2-332.
PDB; 4AJK; X-ray; 2.03 A; A/B/C/D=2-332.
PDB; 4AJL; X-ray; 1.77 A; A/B/C/D=2-332.
PDB; 4AJN; X-ray; 2.10 A; A/B/C/D=2-332.
PDB; 4AJO; X-ray; 1.96 A; A/B/C/D=2-332.
PDB; 4AL4; X-ray; 1.78 A; A/B/C/D=2-332.
PDB; 5ES3; X-ray; 2.29 A; A/B/C/D/E/F/G/H=2-332.
PDBsum; 4AJ1; -.
PDBsum; 4AJ2; -.
PDBsum; 4AJ4; -.
PDBsum; 4AJE; -.
PDBsum; 4AJH; -.
PDBsum; 4AJI; -.
PDBsum; 4AJJ; -.
PDBsum; 4AJK; -.
PDBsum; 4AJL; -.
PDBsum; 4AJN; -.
PDBsum; 4AJO; -.
PDBsum; 4AL4; -.
PDBsum; 5ES3; -.
ProteinModelPortal; P04642; -.
SMR; P04642; -.
BioGrid; 246686; 3.
IntAct; P04642; 6.
MINT; P04642; -.
STRING; 10116.ENSRNOP00000017468; -.
BindingDB; P04642; -.
ChEMBL; CHEMBL2176824; -.
iPTMnet; P04642; -.
PhosphoSitePlus; P04642; -.
SwissPalm; P04642; -.
PaxDb; P04642; -.
PRIDE; P04642; -.
Ensembl; ENSRNOT00000017468; ENSRNOP00000017468; ENSRNOG00000013009.
GeneID; 24533; -.
KEGG; rno:24533; -.
CTD; 3939; -.
RGD; 2996; Ldha.
eggNOG; KOG1495; Eukaryota.
eggNOG; COG0039; LUCA.
GeneTree; ENSGT00550000074541; -.
HOGENOM; HOG000213793; -.
HOVERGEN; HBG000462; -.
InParanoid; P04642; -.
KO; K00016; -.
OMA; MDLMQTA; -.
OrthoDB; EOG091G0HME; -.
PhylomeDB; P04642; -.
TreeFam; TF314963; -.
BioCyc; MetaCyc:MONOMER-11604; -.
Reactome; R-RNO-70268; Pyruvate metabolism.
UniPathway; UPA00554; UER00611.
PRO; PR:P04642; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000013009; -.
ExpressionAtlas; P04642; baseline and differential.
Genevisible; P04642; RN.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IDA:RGD.
GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:RGD.
GO; GO:0004457; F:lactate dehydrogenase activity; IDA:RGD.
GO; GO:0051287; F:NAD binding; IDA:RGD.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0006089; P:lactate metabolic process; IDA:RGD.
GO; GO:0019674; P:NAD metabolic process; IDA:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
GO; GO:0048569; P:post-embryonic animal organ development; IEP:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
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;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; NAD; Oxidoreductase;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.3}.
CHAIN 2 332 L-lactate dehydrogenase A chain.
/FTId=PRO_0000168419.
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:0000269|Ref.3}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 5 5 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P06151}.
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:0000250|UniProtKB:P00338}.
MOD_RES 118 118 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 118 118 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 126 126 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 224 224 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 232 232 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 239 239 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 243 243 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 309 309 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 318 318 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 318 318 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 322 322 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
CROSSLNK 57 57 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P00338}.
CONFLICT 184 191 SCHGWVLG -> ADLGEVV (in Ref. 4; AA
sequence). {ECO:0000305}.
CONFLICT 324 324 W -> G (in Ref. 5; AAA41508).
{ECO:0000305}.
CONFLICT 326 326 I -> T (in Ref. 5; AAA41508).
{ECO:0000305}.
HELIX 4 8 {ECO:0000244|PDB:4AJ2}.
STRAND 9 11 {ECO:0000244|PDB:4AJ2}.
STRAND 20 26 {ECO:0000244|PDB:4AJ2}.
HELIX 30 41 {ECO:0000244|PDB:4AJ2}.
STRAND 46 51 {ECO:0000244|PDB:4AJ2}.
HELIX 55 67 {ECO:0000244|PDB:4AJ2}.
HELIX 68 71 {ECO:0000244|PDB:4AJ2}.
STRAND 76 79 {ECO:0000244|PDB:4AJ2}.
HELIX 83 86 {ECO:0000244|PDB:4AJ2}.
STRAND 89 94 {ECO:0000244|PDB:4AJ2}.
HELIX 106 109 {ECO:0000244|PDB:4AJ2}.
HELIX 110 127 {ECO:0000244|PDB:4AJ2}.
STRAND 132 135 {ECO:0000244|PDB:4AJ2}.
STRAND 137 139 {ECO:0000244|PDB:4AJ2}.
HELIX 140 151 {ECO:0000244|PDB:4AJ2}.
HELIX 155 157 {ECO:0000244|PDB:4AJ2}.
STRAND 158 160 {ECO:0000244|PDB:4AJ2}.
HELIX 164 178 {ECO:0000244|PDB:4AJ2}.
HELIX 182 184 {ECO:0000244|PDB:4AJ2}.
STRAND 189 191 {ECO:0000244|PDB:4AJ2}.
HELIX 201 203 {ECO:0000244|PDB:4AJ2}.
HELIX 211 214 {ECO:0000244|PDB:4AJ2}.
TURN 216 219 {ECO:0000244|PDB:4AJ2}.
HELIX 228 245 {ECO:0000244|PDB:4AJ2}.
HELIX 250 264 {ECO:0000244|PDB:4AJ2}.
STRAND 269 276 {ECO:0000244|PDB:4AJ2}.
HELIX 280 282 {ECO:0000244|PDB:4AJ2}.
STRAND 288 296 {ECO:0000244|PDB:4AJ2}.
STRAND 299 304 {ECO:0000244|PDB:4AJ2}.
HELIX 310 327 {ECO:0000244|PDB:4AJ2}.
SEQUENCE 332 AA; 36451 MW; 5E432659D032A4D3 CRC64;
MAALKDQLIV NLLKEEQVPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG
EMMDLQHGSL FLKTPKIVSS KDYSVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI
IPNVVKYSPQ CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV
HPLSCHGWVL GEHGDSSVPV WSGVNVAGVS LKSLNPQLGT DADKEQWKDV HKQVVDSAYE
VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI
SDVVKVTLTP DEEARLKKSA DTLWGIQKEL QF


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