ID   LDHC_VULVU              Reviewed;         332 AA.
AC   Q29563;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 113.
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   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Bradley M.P.;
RT   "Cloning of LDHC4 from a fox testis cDNA library.";
RL   Submitted (FEB-1995) 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; U19868; AAA61912.1; -; mRNA.
DR   AlphaFoldDB; Q29563; -.
DR   SMR; Q29563; -.
DR   STRING; 9627.ENSVVUP00000003461; -.
DR   OMA; AWSHVTI; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:Ensembl.
DR   GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR   GO; GO:0019244; P:lactate biosynthetic process from pyruvate; IEA:Ensembl.
DR   GO; GO:0019516; P:lactate oxidation; IEA:Ensembl.
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_0000168483"
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;  36215 MW;  09E6B299786EE2AB CRC64;
     MSTVKEKLIE NLIEEDKISQ RKITIVGTGA VGMACAICIL LKDLADELAL VDVAVDKLKG
     EMMDLQHGSL FFNTSKITSG KDYSVSANSK LVIVTAGARQ QEGESRLALV QRNVNIMKSI
     IPAVVQHSPD CKMLIVSNPV DILTYVVWKL SGLPATRVFG SGCNLDSARF RYLIGEKLGV
     HPTSCHGWII GEHGDSSVPL WSGVNVAGVA LKTLDPKLGT DADKDQWKNI HKQVVESAYE
     IIKLKGYTSW AIGLSVTDLV GSVLKNLRRV HPVSTMVKGL YGIKEEIFLS IPCVLGQNGV
     SDIVKINLNS DEEALFKKSA DTLWNVQKEL VF