LDHC_RAT
ID LDHC_RAT Reviewed; 332 AA.
AC P19629;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=7937776; DOI=10.1073/pnas.91.20.9392;
RA Tsuji S., Qureshi M.A., Hou E.W., Fitch W.M., Li S.S.-L.;
RT "Evolutionary relationships of lactate dehydrogenases (LDHs) from mammals,
RT birds, an amphibian, fish, barley, and bacteria: LDH cDNA sequences from
RT Xenopus, pig, and rat.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9392-9396(1994).
RN [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; U07177; AAA50435.1; -; mRNA.
DR PIR; I84639; I84639.
DR AlphaFoldDB; P19629; -.
DR SMR; P19629; -.
DR STRING; 10116.ENSRNOP00000017851; -.
DR iPTMnet; P19629; -.
DR PhosphoSitePlus; P19629; -.
DR jPOST; P19629; -.
DR PaxDb; P19629; -.
DR PRIDE; P19629; -.
DR UCSC; RGD:69366; rat.
DR RGD; 69366; Ldhc.
DR eggNOG; KOG1495; Eukaryota.
DR InParanoid; P19629; -.
DR PhylomeDB; P19629; -.
DR Reactome; R-RNO-70268; Pyruvate metabolism.
DR UniPathway; UPA00554; UER00611.
DR PRO; PR:P19629; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031514; C:motile cilium; ISO:RGD.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; ISO:RGD.
DR GO; GO:0006754; P:ATP biosynthetic process; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0019244; P:lactate biosynthetic process from pyruvate; ISO:RGD.
DR GO; GO:0019516; P:lactate oxidation; ISO:RGD.
DR GO; GO:0006090; P:pyruvate metabolic process; ISO:RGD.
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 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_0000168482"
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. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="I -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="I -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..226
FT /note="DKEQ -> NKQE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="A -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 259..261
FT /note="IAA -> LAE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..331
FT /note="DLQ -> NLE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 35687 MW; 7D4C818B7D40B822 CRC64;
MSTVKEQLIQ NLAPDEKQSR CKITVVGVGN VGMACAISIL LKGLADELAL VDADENKLKG
EALDLLHGSL FLSTPKIVFG KDYSVSANSK LVIITAGARM VSGESRLALL QRNVTSMKAI
VPGVIQNSPD CKIMIVTNPV DILTYVVWKI SGLPVSSVIG SGCNLDSARF RYLIGEKLGV
NPSSCHGWVL GEHGDSSVPI WSGVNIAGVT LKSLNPAIGS DSDKEQWKTV HKQVVDGGYE
VLNLKGYTSW AIALSVTDIA ASILKNLKRV HAVTTLVKGL YGIKEEIFLS IPCVLGQSGI
TDLVKVNMNT EEEALFKKSC DILWNIQKDL QL
