ID   LDHC_HUMAN              Reviewed;         332 AA.
AC   P07864; D3DQY4; Q6GSG8; Q7Z7J4;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 216.
DE   RecName: Full=L-lactate dehydrogenase C chain;
DE            Short=LDH-C;
DE            EC=1.1.1.27;
DE   AltName: Full=Cancer/testis antigen 32;
DE            Short=CT32;
DE   AltName: Full=LDH testis subunit;
DE   AltName: Full=LDH-X;
GN   Name=LDHC; Synonyms=LDH3, LDHX;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=2440048; DOI=10.1073/pnas.84.15.5311;
RA   Millan J.L., Driscoll C.E., Goldberg E.;
RT   "Epitopes of human testis-specific lactate dehydrogenase deduced from a
RT   cDNA sequence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:5311-5315(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2930531; DOI=10.1016/0006-291x(89)90033-8;
RA   Takano T., Li S.S.-L.;
RT   "Human testicular lactate dehydrogenase-C gene is interrupted by six
RT   introns at positions homologous to those of LDH-A (muscle) and LDH-B
RT   (heart) genes.";
RL   Biochem. Biophys. Res. Commun. 159:579-583(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wu K., Li S.S.-L.;
RT   "Human testicular lactate dehydrogenase-C gene: cDNA sequence and putative
RT   alternative splicing at the 5' noncoding region.";
RL   J. Genet. Mol. Biol. 1:72-76(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND POSSIBLE FUNCTION.
RC   TISSUE=Testis;
RX   PubMed=14985855; DOI=10.1007/s00109-004-0526-3;
RA   Wang H., Zhou Z., Xu M., Li J., Xiao J., Xu Z.-Y., Sha J.;
RT   "A spermatogenesis-related gene expression profile in human spermatozoa and
RT   its potential clinical applications.";
RL   J. Mol. Med. 82:317-324(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
CC   -!- FUNCTION: Possible role in sperm motility.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Lactate dehydrogenase entry;
CC       URL="https://en.wikipedia.org/wiki/Lactate_dehydrogenase";
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DR   EMBL; J02938; AAA59507.1; -; mRNA.
DR   EMBL; AH002865; AAA59508.1; -; Genomic_DNA.
DR   EMBL; U13680; AAA21348.1; -; mRNA.
DR   EMBL; AY286300; AAP37402.1; -; mRNA.
DR   EMBL; CH471064; EAW68392.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68394.1; -; Genomic_DNA.
DR   EMBL; BC019249; AAH19249.3; -; mRNA.
DR   EMBL; BC064388; AAH64388.1; -; mRNA.
DR   EMBL; BC090043; AAH90043.1; -; mRNA.
DR   CCDS; CCDS7840.1; -.
DR   PIR; A30933; DEHULC.
DR   RefSeq; NP_002292.1; NM_002301.4.
DR   RefSeq; NP_059144.1; NM_017448.3.
DR   PDB; 7EPM; X-ray; 3.00 A; A/B=2-332.
DR   PDBsum; 7EPM; -.
DR   AlphaFoldDB; P07864; -.
DR   SMR; P07864; -.
DR   BioGRID; 110140; 41.
DR   ComplexPortal; CPX-6602; L-lactate dehydrogenase C complex.
DR   IntAct; P07864; 7.
DR   STRING; 9606.ENSP00000437783; -.
DR   DrugBank; DB00157; NADH.
DR   iPTMnet; P07864; -.
DR   PhosphoSitePlus; P07864; -.
DR   SwissPalm; P07864; -.
DR   BioMuta; LDHC; -.
DR   DMDM; 76363520; -.
DR   EPD; P07864; -.
DR   jPOST; P07864; -.
DR   MassIVE; P07864; -.
DR   MaxQB; P07864; -.
DR   PaxDb; 9606-ENSP00000437783; -.
DR   PeptideAtlas; P07864; -.
DR   ProteomicsDB; 52030; -.
DR   Pumba; P07864; -.
DR   Antibodypedia; 25085; 287 antibodies from 33 providers.
DR   DNASU; 3948; -.
DR   Ensembl; ENST00000280704.8; ENSP00000280704.3; ENSG00000166796.12.
DR   Ensembl; ENST00000541669.6; ENSP00000437783.1; ENSG00000166796.12.
DR   GeneID; 3948; -.
DR   KEGG; hsa:3948; -.
DR   MANE-Select; ENST00000541669.6; ENSP00000437783.1; NM_017448.5; NP_059144.1.
DR   UCSC; uc001mom.5; human.
DR   AGR; HGNC:6544; -.
DR   CTD; 3948; -.
DR   DisGeNET; 3948; -.
DR   GeneCards; LDHC; -.
DR   HGNC; HGNC:6544; LDHC.
DR   HPA; ENSG00000166796; Tissue enriched (testis).
DR   MIM; 150150; gene.
DR   neXtProt; NX_P07864; -.
DR   OpenTargets; ENSG00000166796; -.
DR   PharmGKB; PA30328; -.
DR   VEuPathDB; HostDB:ENSG00000166796; -.
DR   eggNOG; KOG1495; Eukaryota.
DR   GeneTree; ENSGT00940000161479; -.
DR   HOGENOM; CLU_045401_0_2_1; -.
DR   InParanoid; P07864; -.
DR   OMA; HFSTIVG; -.
DR   OrthoDB; 5344346at2759; -.
DR   PhylomeDB; P07864; -.
DR   TreeFam; TF314963; -.
DR   BRENDA; 1.1.1.27; 2681.
DR   PathwayCommons; P07864; -.
DR   Reactome; R-HSA-70268; Pyruvate metabolism.
DR   SignaLink; P07864; -.
DR   UniPathway; UPA00554; UER00611.
DR   BioGRID-ORCS; 3948; 8 hits in 1151 CRISPR screens.
DR   ChiTaRS; LDHC; human.
DR   GenomeRNAi; 3948; -.
DR   Pharos; P07864; Tbio.
DR   PRO; PR:P07864; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P07864; Protein.
DR   Bgee; ENSG00000166796; Expressed in left testis and 138 other cell types or tissues.
DR   ExpressionAtlas; P07864; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:1990204; C:oxidoreductase complex; NAS:ComplexPortal.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
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:0006089; P:lactate metabolic process; IBA:GO_Central.
DR   GO; GO:0019516; P:lactate oxidation; IEA:Ensembl.
DR   GO; GO:0042867; P:pyruvate catabolic process; IEA:Ensembl.
DR   GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR   CDD; cd05293; LDH_1; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR01771; L-LDH-NAD; 1.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF5; L-LACTATE DEHYDROGENASE C CHAIN; 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   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00064; L_LDH; 1.
DR   Genevisible; P07864; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..332
FT                   /note="L-lactate dehydrogenase C chain"
FT                   /id="PRO_0000168479"
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:0007744|PubMed:20068231"
FT   VARIANT         285
FT                   /note="E -> Q (in dbSNP:rs2230150)"
FT                   /id="VAR_034068"
FT   CONFLICT        77
FT                   /note="I -> V (in Ref. 1; AAA59507 and 2; AAA59508)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="D -> G (in Ref. 4; AAP37402)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="S -> I (in Ref. 1; AAA59507)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..8
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          20..26
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           30..41
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           55..66
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           67..71
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          76..79
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           83..86
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          90..94
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           107..127
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          132..135
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           140..151
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           164..178
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   TURN            182..184
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          189..194
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   TURN            201..203
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           211..214
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   TURN            216..219
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           228..245
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           250..264
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          269..276
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          288..296
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   STRAND          299..303
FT                   /evidence="ECO:0007829|PDB:7EPM"
FT   HELIX           310..331
FT                   /evidence="ECO:0007829|PDB:7EPM"
SQ   SEQUENCE   332 AA;  36311 MW;  DF7047FF5BCB101B CRC64;
     MSTVKEQLIE KLIEDDENSQ CKITIVGTGA VGMACAISIL LKDLADELAL VDVALDKLKG
     EMMDLQHGSL FFSTSKITSG KDYSVSANSR IVIVTAGARQ QEGETRLALV QRNVAIMKSI
     IPAIVHYSPD CKILVVSNPV DILTYIVWKI SGLPVTRVIG SGCNLDSARF RYLIGEKLGV
     HPTSCHGWII GEHGDSSVPL WSGVNVAGVA LKTLDPKLGT DSDKEHWKNI HKQVIQSAYE
     IIKLKGYTSW AIGLSVMDLV GSILKNLRRV HPVSTMVKGL YGIKEELFLS IPCVLGRNGV
     SDVVKINLNS EEEALFKKSA ETLWNIQKDL IF
//