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L-lactate dehydrogenase C chain (LDH-C) (EC 1.1.1.27) (LDH testis subunit) (LDH-X)

 LDHC_RAT                Reviewed;         332 AA.
P19629;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 136.
RecName: Full=L-lactate dehydrogenase C chain;
Short=LDH-C;
EC=1.1.1.27;
AltName: Full=LDH testis subunit;
AltName: Full=LDH-X;
Name=Ldhc; Synonyms=Ldh-3, Ldh3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=7937776; DOI=10.1073/pnas.91.20.9392;
Tsuji S., Qureshi M.A., Hou E.W., Fitch W.M., Li S.S.-L.;
"Evolutionary relationships of lactate dehydrogenases (LDHs) from
mammals, birds, an amphibian, fish, barley, and bacteria: LDH cDNA
sequences from Xenopus, pig, and rat.";
Proc. Natl. Acad. Sci. U.S.A. 91:9392-9396(1994).
[2]
PROTEIN SEQUENCE OF 2-332.
PubMed=6343385;
Pan Y.-C.E., Sharief F.S., Okabe M., Huang S., Li S.S.-L.;
"Amino acid sequence studies on lactate dehydrogenase C4 isozymes from
mouse and rat testes.";
J. Biol. Chem. 258:7005-7016(1983).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Possible role in sperm motility. {ECO:0000250}.
-!- 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}.
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EMBL; U07177; AAA50435.1; -; mRNA.
PIR; I84639; I84639.
UniGene; Rn.9984; -.
ProteinModelPortal; P19629; -.
STRING; 10116.ENSRNOP00000017851; -.
iPTMnet; P19629; -.
PhosphoSitePlus; P19629; -.
PaxDb; P19629; -.
PRIDE; P19629; -.
UCSC; RGD:69366; rat.
RGD; 69366; Ldhc.
eggNOG; KOG1495; Eukaryota.
eggNOG; COG0039; LUCA.
HOGENOM; HOG000213793; -.
HOVERGEN; HBG000462; -.
InParanoid; P19629; -.
PhylomeDB; P19629; -.
UniPathway; UPA00554; UER00611.
PRO; PR:P19629; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005929; C:cilium; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031514; C:motile cilium; ISO:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0004459; F:L-lactate dehydrogenase activity; ISO:RGD.
GO; GO:0006754; P:ATP biosynthetic process; ISO:RGD.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
GO; GO:0019244; P:lactate biosynthetic process from pyruvate; ISO:RGD.
GO; GO:0019516; P:lactate oxidation; ISO:RGD.
GO; GO:0006090; P:pyruvate metabolic process; ISO:RGD.
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; Direct protein sequencing; NAD;
Oxidoreductase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6343385}.
CHAIN 2 332 L-lactate dehydrogenase C chain.
/FTId=PRO_0000168482.
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 2 2 Blocked amino end (Ser).
CONFLICT 7 7 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 16 16 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 30 30 N -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 56 56 N -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 104 104 E -> Q (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 116 116 S -> I (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 183 183 S -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 200 200 I -> V (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 206 206 I -> V (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 223 226 DKEQ -> NKQE (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 243 243 N -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 253 253 A -> G (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 259 261 IAA -> LAE (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 297 297 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 329 331 DLQ -> NLE (in Ref. 2; AA sequence).
{ECO:0000305}.
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


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