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Database: UniProt
Entry: A0A1B0GS79_MOUSE
LinkDB: A0A1B0GS79_MOUSE
Original site: A0A1B0GS79_MOUSE 
ID   A0A1B0GS79_MOUSE        Unreviewed;       205 AA.
AC   A0A1B0GS79;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=L-lactate dehydrogenase A chain {ECO:0000256|ARBA:ARBA00017655};
DE   AltName: Full=LDH muscle subunit {ECO:0000256|ARBA:ARBA00043238};
GN   Name=Ldha {ECO:0000313|Ensembl:ENSMUSP00000147825.2,
GN   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|Ensembl:ENSMUSP00000147825.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000147825.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000147825.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {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   [3] {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).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000147825.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000147825.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   AlphaFoldDB; A0A1B0GS79; -.
DR   SMR; A0A1B0GS79; -.
DR   jPOST; A0A1B0GS79; -.
DR   ProteomicsDB; 353260; -.
DR   Antibodypedia; 4200; 1029 antibodies from 40 providers.
DR   Ensembl; ENSMUST00000210631.2; ENSMUSP00000147825.2; ENSMUSG00000063229.16.
DR   AGR; MGI:96759; -.
DR   MGI; MGI:96759; Ldha.
DR   VEuPathDB; HostDB:ENSMUSG00000063229; -.
DR   GeneTree; ENSGT00940000153201; -.
DR   ChiTaRS; Ldha; mouse.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000063229; Expressed in otic placode and 272 other cell types or tissues.
DR   ExpressionAtlas; A0A1B0GS79; baseline and differential.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF10; L-LACTATE DEHYDROGENASE A CHAIN; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:A0A1B0GS79,
KW   ECO:0007829|MaxQB:A0A1B0GS79};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          22..84
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   REGION          81..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   205 AA;  22487 MW;  173B6C7012AD9C3F CRC64;
     MATLKDQLIV NLLKEEQAPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVMEDKLKG
     EMMDLQHGSL FLKTPKIVSS KAGHYHRGGP SARGGEPAQP GPAKREHLQV HHSQHCQVQS
     TLQAADRLQS SGYLDLRGLE NQWLSQKPSN WKWLQSGFSA VPLPDGREAG GSRAELSRLG
     PGRTWRLQCA CVEWCECCRR LPEVS
//
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