LDHC_HUMAN
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 03-AUG-2022, entry version 207.
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; 38.
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; P07864; -.
DR PeptideAtlas; P07864; -.
DR PRIDE; P07864; -.
DR ProteomicsDB; 52030; -.
DR Antibodypedia; 25085; 253 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 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; AWSHVTI; -.
DR OrthoDB; 1204514at2759; -.
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 1071 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 136 other tissues.
DR ExpressionAtlas; P07864; baseline and differential.
DR Genevisible; P07864; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:1990204; C:oxidoreductase complex; IC: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; IC:ComplexPortal.
DR GO; GO:0019516; P:lactate oxidation; IEA:Ensembl.
DR GO; GO:0006090; P:pyruvate metabolic process; IC:ComplexPortal.
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 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"
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
