ID   LDHC_PIG                Reviewed;         332 AA.
AC   Q9TSX5;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=L-lactate dehydrogenase C chain;
DE            Short=LDH-C;
DE            EC=1.1.1.27;
DE   AltName: Full=LDH testis subunit;
DE   AltName: Full=LDH-X;
GN   Name=LDHC;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li S.S.-L., Huang H.-W.;
RT   "Pig LDH-C mRNA complete sequence.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Possible role in sperm motility. {ECO:0000250}.
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   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1.
CC   -!- SUBUNIT: Homotetramer. Interacts with RABL2/RABL2A; binds
CC       preferentially to GTP-bound RABL2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
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DR   EMBL; U95378; AAF22363.1; -; mRNA.
DR   RefSeq; NP_001182704.1; NM_001195775.1.
DR   AlphaFoldDB; Q9TSX5; -.
DR   SMR; Q9TSX5; -.
DR   STRING; 9823.ENSSSCP00000014199; -.
DR   PaxDb; Q9TSX5; -.
DR   PeptideAtlas; Q9TSX5; -.
DR   PRIDE; Q9TSX5; -.
DR   GeneID; 100502559; -.
DR   KEGG; ssc:100502559; -.
DR   CTD; 3948; -.
DR   eggNOG; KOG1495; Eukaryota.
DR   InParanoid; Q9TSX5; -.
DR   UniPathway; UPA00554; UER00611.
DR   ChiTaRS; LDHC; pig.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.110.10; -; 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   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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..332
FT                   /note="L-lactate dehydrogenase C chain"
FT                   /id="PRO_0000168481"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..57
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07864"
SQ   SEQUENCE   332 AA;  36053 MW;  880ECD7EEB6434DC CRC64;
     MSTVKEQLIE NLIEEDEVSQ SKITIVGTGA VGMACAICIL LKDLADELAL VDVAVDKLKG
     ETMDLQHGSL FFNTSKIVSG KDYSVSANSK IVIVTAGARQ QEGESRLALV QRNVNIMKSI
     IPTIVQHSPD CKMLIVSNPV DILTYVAWKL SGLPATRVIG SGCNLDSARF RYLIGKKLGV
     HPTSCHGWII GEHGDSSVPL WSGVNVAGVA LKTLDPKLGT DSDKDQWKNI HKQVIGSAYE
     IIKLKGYTSW AIGLSVTDLV GSILKNLRRV HPVSTMVKGL YGIKEEIFLS IPCVLGRNGV
     SDIVKVNLNA EEEALFKKSA NTLWNVQKDL TF