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 14-OCT-2015, entry version 155. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=DBA/2J; TISSUE=Testis; RX PubMed=2439071; RA Sakai I., Sharief F.S., Li S.S.-L.; RT "Molecular cloning and nucleotide sequence of the cDNA for sperm- RT specific 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 RT mouse 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PRELIMINARY PROTEIN SEQUENCE OF 2-332. RX PubMed=468774; RA Musick W.D., Rossmann M.G.; RT "The tentative amino acid sequencing of lactate dehydrogenase C4 by X- RT ray 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; 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 RT isozyme 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 RT 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., RA Whisstock J.C., Field M.C., Adams V., Ishikawa T., Aitken R.J., RA Whittle B., Goodnow C.C., Ormandy C.J., O'Bryan M.K.; RT "RAB-like 2 has an essential role in male fertility, sperm intra- RT flagellar transport, and tail assembly."; RL PLoS Genet. 8:E1002969-E1002969(2012). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX PubMed=468772; RA Musick W.D.L., Rossmann M.G.; RT "The structure of mouse testicular lactate dehydrogenase isoenzyme C4 RT at 2.9-A resolution."; RL J. Biol. Chem. 254:7611-7620(1979). CC -!- FUNCTION: Possible role in sperm motility. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)- CC lactate 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 CC (at protein level). {ECO:0000269|PubMed:23055941}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Mm.16563; -. DR PDB; 2LDX; X-ray; 2.96 A; A/B/C/D=2-332. DR PDBsum; 2LDX; -. DR ProteinModelPortal; P00342; -. DR SMR; P00342; 2-332. DR IntAct; P00342; 2. DR MINT; MINT-6611882; -. DR STRING; 10090.ENSMUSP00000014545; -. DR PhosphoSite; P00342; -. DR REPRODUCTION-2DPAGE; P00342; -. DR PaxDb; P00342; -. DR PRIDE; P00342; -. DR GeneID; 16833; -. DR KEGG; mmu:16833; -. DR UCSC; uc009gzp.1; mouse. DR CTD; 3948; -. DR MGI; MGI:96764; Ldhc. DR eggNOG; COG0039; -. DR HOGENOM; HOG000213793; -. DR HOVERGEN; HBG000462; -. DR InParanoid; P00342; -. DR KO; K00016; -. DR OMA; RICESII; -. DR OrthoDB; EOG7X0VH3; -. DR PhylomeDB; P00342; -. DR TreeFam; TF314963; -. DR UniPathway; UPA00554; UER00611. DR ChiTaRS; Ldhc; mouse. DR EvolutionaryTrace; P00342; -. DR NextBio; 290746; -. DR PRO; PR:P00342; -. DR Proteomes; UP000000589; Unplaced. DR Bgee; P00342; -. DR CleanEx; MM_LDHC; -. 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:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0031514; C:motile cilium; IDA:MGI. DR GO; GO:0005634; C:nucleus; ISO: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:0005975; P:carbohydrate metabolic process; IEA:InterPro. 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 GO; GO:0030317; P:sperm motility; IMP:MGI. DR Gene3D; 3.40.50.720; -; 1. 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; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11540; PTHR11540; 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; SSF56327; 1. DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1. DR PROSITE; PS00064; L_LDH; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6343385}. FT CHAIN 2 332 L-lactate dehydrogenase C chain. FT /FTId=PRO_0000168480. FT NP_BIND 29 57 NAD. {ECO:0000250}. FT ACT_SITE 193 193 Proton acceptor. {ECO:0000250}. FT BINDING 99 99 NAD. {ECO:0000250}. FT BINDING 106 106 Substrate. {ECO:0000250}. FT BINDING 138 138 NAD or substrate. {ECO:0000250}. FT BINDING 169 169 Substrate. {ECO:0000250}. FT BINDING 248 248 Substrate. {ECO:0000250}. FT MOD_RES 2 2 Blocked amino end (Ser). FT MOD_RES 239 239 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P16125}. FT CONFLICT 7 7 Q -> E (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 15 15 Missing (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 30 30 N -> D (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 56 56 N -> D (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 104 104 E -> Q (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 124 125 IV -> VI (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 135 135 I -> V (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 223 225 DKE -> NKQ (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 243 243 N -> D (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 297 297 Q -> E (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 329 331 DLQ -> NLE (in Ref. 6; AA sequence). FT {ECO:0000305}. FT HELIX 4 8 {ECO:0000244|PDB:2LDX}. FT STRAND 9 11 {ECO:0000244|PDB:2LDX}. FT STRAND 22 26 {ECO:0000244|PDB:2LDX}. FT HELIX 30 40 {ECO:0000244|PDB:2LDX}. FT TURN 41 43 {ECO:0000244|PDB:2LDX}. FT STRAND 46 51 {ECO:0000244|PDB:2LDX}. FT HELIX 55 67 {ECO:0000244|PDB:2LDX}. FT TURN 68 71 {ECO:0000244|PDB:2LDX}. FT STRAND 76 82 {ECO:0000244|PDB:2LDX}. FT HELIX 83 86 {ECO:0000244|PDB:2LDX}. FT STRAND 89 94 {ECO:0000244|PDB:2LDX}. FT TURN 102 104 {ECO:0000244|PDB:2LDX}. FT HELIX 111 120 {ECO:0000244|PDB:2LDX}. FT TURN 121 123 {ECO:0000244|PDB:2LDX}. FT HELIX 124 127 {ECO:0000244|PDB:2LDX}. FT STRAND 132 135 {ECO:0000244|PDB:2LDX}. FT STRAND 137 139 {ECO:0000244|PDB:2LDX}. FT HELIX 140 151 {ECO:0000244|PDB:2LDX}. FT TURN 155 157 {ECO:0000244|PDB:2LDX}. FT STRAND 158 160 {ECO:0000244|PDB:2LDX}. FT HELIX 164 178 {ECO:0000244|PDB:2LDX}. FT STRAND 189 191 {ECO:0000244|PDB:2LDX}. FT STRAND 193 195 {ECO:0000244|PDB:2LDX}. FT STRAND 197 199 {ECO:0000244|PDB:2LDX}. FT HELIX 201 203 {ECO:0000244|PDB:2LDX}. FT STRAND 205 207 {ECO:0000244|PDB:2LDX}. FT STRAND 209 214 {ECO:0000244|PDB:2LDX}. FT TURN 215 217 {ECO:0000244|PDB:2LDX}. FT STRAND 221 226 {ECO:0000244|PDB:2LDX}. FT HELIX 228 245 {ECO:0000244|PDB:2LDX}. FT HELIX 250 264 {ECO:0000244|PDB:2LDX}. FT STRAND 269 276 {ECO:0000244|PDB:2LDX}. FT STRAND 288 296 {ECO:0000244|PDB:2LDX}. FT STRAND 299 304 {ECO:0000244|PDB:2LDX}. FT HELIX 310 326 {ECO:0000244|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 //