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L-lactate dehydrogenase C chain (LDH-C) (EC 1.1.1.27) (Cancer/testis antigen 32) (CT32) (LDH testis subunit) (LDH-X)

 LDHC_HUMAN              Reviewed;         332 AA.
P07864; D3DQY4; Q6GSG8; Q7Z7J4;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 180.
RecName: Full=L-lactate dehydrogenase C chain;
Short=LDH-C;
EC=1.1.1.27;
AltName: Full=Cancer/testis antigen 32;
Short=CT32;
AltName: Full=LDH testis subunit;
AltName: Full=LDH-X;
Name=LDHC; Synonyms=LDH3, LDHX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=2440048; DOI=10.1073/pnas.84.15.5311;
Millan J.L., Driscoll C.E., Goldberg E.;
"Epitopes of human testis-specific lactate dehydrogenase deduced from
a cDNA sequence.";
Proc. Natl. Acad. Sci. U.S.A. 84:5311-5315(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2930531; DOI=10.1016/0006-291X(89)90033-8;
Takano T., Li S.S.-L.;
"Human testicular lactate dehydrogenase-C gene is interrupted by six
introns at positions homologous to those of LDH-A (muscle) and LDH-B
(heart) genes.";
Biochem. Biophys. Res. Commun. 159:579-583(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Wu K., Li S.S.-L.;
"Human testicular lactate dehydrogenase-C gene: cDNA sequence and
putative alternative splicing at the 5' noncoding region.";
J. Genet. Mol. Biol. 1:72-76(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND POSSIBLE FUNCTION.
TISSUE=Testis;
PubMed=14985855; DOI=10.1007/s00109-004-0526-3;
Wang H., Zhou Z., Xu M., Li J., Xiao J., Xu Z.-Y., Sha J.;
"A spermatogenesis-related gene expression profile in human
spermatozoa and its potential clinical applications.";
J. Mol. Med. 82:317-324(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
-!- FUNCTION: Possible role in sperm motility.
-!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
-!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
lactate from pyruvate: step 1/1.
-!- SUBUNIT: Homotetramer. Interacts with RABL2/RABL2A; binds
preferentially to GTP-bound RABL2 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Lactate dehydrogenase entry;
URL="https://en.wikipedia.org/wiki/Lactate_dehydrogenase";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; J02938; AAA59507.1; -; mRNA.
EMBL; AH002865; AAA59508.1; -; Genomic_DNA.
EMBL; U13680; AAA21348.1; -; mRNA.
EMBL; AY286300; AAP37402.1; -; mRNA.
EMBL; CH471064; EAW68392.1; -; Genomic_DNA.
EMBL; CH471064; EAW68394.1; -; Genomic_DNA.
EMBL; BC019249; AAH19249.3; -; mRNA.
EMBL; BC064388; AAH64388.1; -; mRNA.
EMBL; BC090043; AAH90043.1; -; mRNA.
CCDS; CCDS7840.1; -.
PIR; A30933; DEHULC.
RefSeq; NP_002292.1; NM_002301.4.
RefSeq; NP_059144.1; NM_017448.3.
UniGene; Hs.654377; -.
ProteinModelPortal; P07864; -.
SMR; P07864; -.
BioGrid; 110140; 24.
STRING; 9606.ENSP00000280704; -.
DrugBank; DB00157; NADH.
iPTMnet; P07864; -.
PhosphoSitePlus; P07864; -.
BioMuta; LDHC; -.
DMDM; 76363520; -.
EPD; P07864; -.
MaxQB; P07864; -.
PaxDb; P07864; -.
PeptideAtlas; P07864; -.
PRIDE; P07864; -.
DNASU; 3948; -.
Ensembl; ENST00000280704; ENSP00000280704; ENSG00000166796.
Ensembl; ENST00000541669; ENSP00000437783; ENSG00000166796.
GeneID; 3948; -.
KEGG; hsa:3948; -.
UCSC; uc001mom.5; human.
CTD; 3948; -.
DisGeNET; 3948; -.
EuPathDB; HostDB:ENSG00000166796.11; -.
GeneCards; LDHC; -.
HGNC; HGNC:6544; LDHC.
HPA; HPA045442; -.
MIM; 150150; gene.
neXtProt; NX_P07864; -.
OpenTargets; ENSG00000166796; -.
PharmGKB; PA30328; -.
eggNOG; KOG1495; Eukaryota.
eggNOG; COG0039; LUCA.
GeneTree; ENSGT00550000074541; -.
HOGENOM; HOG000213793; -.
HOVERGEN; HBG000462; -.
InParanoid; P07864; -.
KO; K00016; -.
OMA; DQWKNIH; -.
OrthoDB; EOG091G0HME; -.
PhylomeDB; P07864; -.
TreeFam; TF314963; -.
Reactome; R-HSA-70268; Pyruvate metabolism.
UniPathway; UPA00554; UER00611.
ChiTaRS; LDHC; human.
GenomeRNAi; 3948; -.
PRO; PR:P07864; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000166796; -.
CleanEx; HS_LDHC; -.
ExpressionAtlas; P07864; baseline and differential.
Genevisible; P07864; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031514; C:motile cilium; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004459; F:L-lactate dehydrogenase activity; EXP:Reactome.
GO; GO:0006754; P:ATP biosynthetic process; IEA:Ensembl.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
GO; GO:0019244; P:lactate biosynthetic process from pyruvate; IEA:Ensembl.
GO; GO:0019516; P:lactate oxidation; IEA:Ensembl.
GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
Gene3D; 3.90.110.10; -; 1.
HAMAP; MF_00488; Lactate_dehydrog; 1.
InterPro; IPR001557; L-lactate/malate_DH.
InterPro; IPR011304; L-lactate_DH.
InterPro; IPR018177; L-lactate_DH_AS.
InterPro; IPR022383; Lactate/malate_DH_C.
InterPro; IPR001236; Lactate/malate_DH_N.
InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF02866; Ldh_1_C; 1.
Pfam; PF00056; Ldh_1_N; 1.
PIRSF; PIRSF000102; Lac_mal_DH; 1.
PRINTS; PR00086; LLDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF56327; SSF56327; 1.
TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
PROSITE; PS00064; L_LDH; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 332 L-lactate dehydrogenase C chain.
/FTId=PRO_0000168479.
NP_BIND 29 57 NAD. {ECO:0000250}.
ACT_SITE 193 193 Proton acceptor. {ECO:0000250}.
BINDING 99 99 NAD. {ECO:0000250}.
BINDING 106 106 Substrate. {ECO:0000250}.
BINDING 138 138 NAD or substrate. {ECO:0000250}.
BINDING 169 169 Substrate. {ECO:0000250}.
BINDING 248 248 Substrate. {ECO:0000250}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VARIANT 285 285 E -> Q (in dbSNP:rs2230150).
/FTId=VAR_034068.
CONFLICT 77 77 I -> V (in Ref. 1; AAA59507 and 2;
AAA59508). {ECO:0000305}.
CONFLICT 82 82 D -> G (in Ref. 4; AAP37402).
{ECO:0000305}.
CONFLICT 119 119 S -> I (in Ref. 1; AAA59507).
{ECO:0000305}.
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


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