LDHC_MOUSE
ID LDHC_MOUSE Reviewed; 332 AA.
AC P00342;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 194.
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; Synonyms=Ldh-3, Ldh3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J; TISSUE=Testis;
RX PubMed=2439071; DOI=10.1042/bj2420619;
RA Sakai I., Sharief F.S., Li S.S.-L.;
RT "Molecular cloning and nucleotide sequence of the cDNA for sperm-specific
RT lactate dehydrogenase-C from mouse.";
RL Biochem. J. 242:619-622(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3619944; DOI=10.1016/0006-291x(87)90741-8;
RA Wu K.C., Chan K., Lee C.-Y.G., Lau Y.-F.C.;
RT "Molecular isolation and sequence determination of the cDNA for the mouse
RT sperm-specific lactate dehydrogenase-X gene.";
RL Biochem. Biophys. Res. Commun. 146:964-970(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [4]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-332.
RX PubMed=468774; DOI=10.1016/s0021-9258(18)35990-8;
RA Musick W.D., Rossmann M.G.;
RT "The tentative amino acid sequencing of lactate dehydrogenase C4 by X-ray
RT diffraction analysis.";
RL J. Biol. Chem. 254:7621-7623(1979).
RN [5]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-332.
RX PubMed=7429427;
RA Pan Y.-C.E., Huang S., Marciniszyn J.P. Jr., Lee C.-Y., Li S.S.-L.;
RT "The preliminary amino acid sequence of mouse testicular lactate
RT dehydrogenase.";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:795-799(1980).
RN [6]
RP PROTEIN SEQUENCE OF 2-332.
RX PubMed=6343385; DOI=10.1016/s0021-9258(18)32325-1;
RA Pan Y.-C.E., Sharief F.S., Okabe M., Huang S., Li S.S.-L.;
RT "Amino acid sequence studies on lactate dehydrogenase C4 isozymes from
RT mouse and rat testes.";
RL J. Biol. Chem. 258:7005-7016(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 194-332.
RX PubMed=3754749; DOI=10.1016/0006-291x(86)90504-8;
RA Tanaka S., Fujimoto H.;
RT "A postmeiotically expressed clone encodes lactate dehydrogenase isozyme
RT X.";
RL Biochem. Biophys. Res. Commun. 136:760-766(1986).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH RABL2, AND TISSUE SPECIFICITY.
RX PubMed=23055941; DOI=10.1371/journal.pgen.1002969;
RA Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., Whisstock J.C.,
RA Field M.C., Adams V., Ishikawa T., Aitken R.J., Whittle B., Goodnow C.C.,
RA Ormandy C.J., O'Bryan M.K.;
RT "RAB-like 2 has an essential role in male fertility, sperm intra-flagellar
RT transport, and tail assembly.";
RL PLoS Genet. 8:E1002969-E1002969(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=468772; DOI=10.2210/pdb1ldx/pdb;
RA Musick W.D.L., Rossmann M.G.;
RT "The structure of mouse testicular lactate dehydrogenase isoenzyme C4 at
RT 2.9-A resolution.";
RL J. Biol. Chem. 254:7611-7620(1979).
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:0000269|PubMed:23055941}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed within the midpiece of sperm tail (at
CC protein level). {ECO:0000269|PubMed:23055941}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; X04752; CAA28449.1; -; mRNA.
DR EMBL; M17587; AAA39425.1; -; mRNA.
DR EMBL; BC049602; AAH49602.1; -; mRNA.
DR EMBL; M12781; AAA88315.1; -; mRNA.
DR CCDS; CCDS21290.1; -.
DR PIR; A26824; DEMSLC.
DR RefSeq; NP_038608.1; NM_013580.4.
DR RefSeq; XP_006540742.1; XM_006540679.1.
DR RefSeq; XP_006540743.1; XM_006540680.1.
DR RefSeq; XP_006540744.1; XM_006540681.1.
DR PDB; 2LDX; X-ray; 2.96 A; A/B/C/D=2-332.
DR PDBsum; 2LDX; -.
DR AlphaFoldDB; P00342; -.
DR SMR; P00342; -.
DR BioGRID; 201131; 4.
DR IntAct; P00342; 3.
DR MINT; P00342; -.
DR STRING; 10090.ENSMUSP00000014545; -.
DR BindingDB; P00342; -.
DR iPTMnet; P00342; -.
DR PhosphoSitePlus; P00342; -.
DR SwissPalm; P00342; -.
DR REPRODUCTION-2DPAGE; P00342; -.
DR jPOST; P00342; -.
DR PaxDb; P00342; -.
DR PeptideAtlas; P00342; -.
DR PRIDE; P00342; -.
DR ProteomicsDB; 292249; -.
DR Antibodypedia; 25085; 253 antibodies from 33 providers.
DR DNASU; 16833; -.
DR Ensembl; ENSMUST00000014545; ENSMUSP00000014545; ENSMUSG00000030851.
DR GeneID; 16833; -.
DR KEGG; mmu:16833; -.
DR UCSC; uc009gzp.1; mouse.
DR CTD; 3948; -.
DR MGI; MGI:96764; Ldhc.
DR VEuPathDB; HostDB:ENSMUSG00000030851; -.
DR eggNOG; KOG1495; Eukaryota.
DR GeneTree; ENSGT00940000161479; -.
DR HOGENOM; CLU_045401_0_2_1; -.
DR InParanoid; P00342; -.
DR OMA; AWSHVTI; -.
DR OrthoDB; 1204514at2759; -.
DR PhylomeDB; P00342; -.
DR TreeFam; TF314963; -.
DR Reactome; R-MMU-70268; Pyruvate metabolism.
DR UniPathway; UPA00554; UER00611.
DR BioGRID-ORCS; 16833; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ldhc; mouse.
DR EvolutionaryTrace; P00342; -.
DR PRO; PR:P00342; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P00342; protein.
DR Bgee; ENSMUSG00000030851; Expressed in spermatid and 83 other tissues.
DR ExpressionAtlas; P00342; baseline and differential.
DR Genevisible; P00342; MM.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IMP:MGI.
DR GO; GO:0006754; P:ATP biosynthetic process; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0019244; P:lactate biosynthetic process from pyruvate; IDA:MGI.
DR GO; GO:0019516; P:lactate oxidation; IDA:MGI.
DR GO; GO:0006090; P:pyruvate metabolic process; IDA:MGI.
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; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6343385"
FT CHAIN 2..332
FT /note="L-lactate dehydrogenase C chain"
FT /id="PRO_0000168480"
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 2
FT /note="Blocked amino end (Ser)"
FT CONFLICT 7
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="Missing (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="N -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="N -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="E -> Q (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 124..125
FT /note="IV -> VI (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="I -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..225
FT /note="DKE -> NKQ (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="N -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..331
FT /note="DLQ -> NLE (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:2LDX"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:2LDX"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2LDX"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:2LDX"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:2LDX"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2LDX"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 228..245
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:2LDX"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:2LDX"
FT HELIX 310..326
FT /evidence="ECO:0007829|PDB:2LDX"
SQ SEQUENCE 332 AA; 35912 MW; 367A7EA8B2A6D86A CRC64;
MSTVKEQLIQ NLVPEDKLSR CKITVVGVGN VGMACAISIL LKGLADELAL VDADTNKLRG
EALDLLHGSL FLSTPKIVFG KDYNVSANSK LVIITAGARM VSGETRLDLL QRNVAIMKAI
VPGIVQNSPD CKIIIVTNPV DILTYVVWKI SGFPVGRVIG SGCNLDSARF RYLIGEKLGV
NPTSCHGWVL GEHGDSSVPI WSGVNVAGVT LKSLNPAIGT DSDKEHWKNV HKQVVEGGYE
VLNMKGYTSW AIGLSVTDLA RSILKNLKRV HPVTTLVKGF HGIKEEVFLS IPCVLGQSGI
TDFVKVNMTA EEEGLLKKSA DTLWNMQKDL QL
