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Protein

L-lactate dehydrogenase C chain

Gene

Ldhc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Possible role in sperm motility.By similarity

Catalytic activityi

(S)-lactate + NAD+ = pyruvate + NADH.

Pathwayi: pyruvate fermentation to lactate

This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.
Proteins known to be involved in this subpathway in this organism are:
  1. L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldhb), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase B chain (Ldhb), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldhal6b), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase A chain (Ldha), L-lactate dehydrogenase (Ldhb), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase C chain (Ldhc), L-lactate dehydrogenase (Ldhc)
This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate, the pathway pyruvate fermentation to lactate and in Fermentation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991NADBy similarity
Binding sitei106 – 1061SubstrateBy similarity
Binding sitei138 – 1381NAD or substrateBy similarity
Binding sitei169 – 1691SubstrateBy similarity
Active sitei193 – 1931Proton acceptorBy similarity
Binding sitei248 – 2481SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 5729NADBy similarityAdd
BLAST

GO - Molecular functioni

  • L-lactate dehydrogenase activity Source: MGI

GO - Biological processi

  • ATP biosynthetic process Source: MGI
  • carbohydrate metabolic process Source: InterPro
  • lactate biosynthetic process from pyruvate Source: MGI
  • lactate oxidation Source: MGI
  • pyruvate metabolic process Source: MGI
  • sperm motility Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-MMU-70268. Pyruvate metabolism.
UniPathwayiUPA00554; UER00611.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase C chain (EC:1.1.1.27)
Short name:
LDH-C
Alternative name(s):
LDH testis subunit
LDH-X
Gene namesi
Name:Ldhc
Synonyms:Ldh-3, Ldh3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:96764. Ldhc.

Subcellular locationi

GO - Cellular componenti

  • cilium Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • motile cilium Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 332331L-lactate dehydrogenase C chainPRO_0000168480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Blocked amino end (Ser)

Proteomic databases

EPDiP00342.
PaxDbiP00342.
PRIDEiP00342.

2D gel databases

REPRODUCTION-2DPAGEP00342.

PTM databases

iPTMnetiP00342.
PhosphoSiteiP00342.

Expressioni

Tissue specificityi

Expressed within the midpiece of sperm tail (at protein level).1 Publication

Gene expression databases

BgeeiP00342.
CleanExiMM_LDHC.
ExpressionAtlasiP00342. baseline and differential.
GenevisibleiP00342. MM.

Interactioni

Subunit structurei

Homotetramer. Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2.1 Publication

Protein-protein interaction databases

IntActiP00342. 2 interactions.
MINTiMINT-6611882.
STRINGi10090.ENSMUSP00000014545.

Structurei

Secondary structure

1
332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 85Combined sources
Beta strandi9 – 113Combined sources
Beta strandi22 – 265Combined sources
Helixi30 – 4011Combined sources
Turni41 – 433Combined sources
Beta strandi46 – 516Combined sources
Helixi55 – 6713Combined sources
Turni68 – 714Combined sources
Beta strandi76 – 827Combined sources
Helixi83 – 864Combined sources
Beta strandi89 – 946Combined sources
Turni102 – 1043Combined sources
Helixi111 – 12010Combined sources
Turni121 – 1233Combined sources
Helixi124 – 1274Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi137 – 1393Combined sources
Helixi140 – 15112Combined sources
Turni155 – 1573Combined sources
Beta strandi158 – 1603Combined sources
Helixi164 – 17815Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi197 – 1993Combined sources
Helixi201 – 2033Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi209 – 2146Combined sources
Turni215 – 2173Combined sources
Beta strandi221 – 2266Combined sources
Helixi228 – 24518Combined sources
Helixi250 – 26415Combined sources
Beta strandi269 – 2768Combined sources
Beta strandi288 – 2969Combined sources
Beta strandi299 – 3046Combined sources
Helixi310 – 32617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LDXX-ray2.96A/B/C/D2-332[»]
ProteinModelPortaliP00342.
SMRiP00342. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00342.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. LDH family.Curated

Phylogenomic databases

eggNOGiKOG1495. Eukaryota.
COG0039. LUCA.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP00342.
KOiK00016.
OMAiRCKITVV.
OrthoDBiEOG7X0VH3.
PhylomeDBiP00342.
TreeFamiTF314963.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. L-lactate/malate_DH.
IPR011304. L-lactate_DH.
IPR018177. L-lactate_DH_AS.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00342-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTVKEQLIQ NLVPEDKLSR CKITVVGVGN VGMACAISIL LKGLADELAL
60 70 80 90 100
VDADTNKLRG EALDLLHGSL FLSTPKIVFG KDYNVSANSK LVIITAGARM
110 120 130 140 150
VSGETRLDLL QRNVAIMKAI VPGIVQNSPD CKIIIVTNPV DILTYVVWKI
160 170 180 190 200
SGFPVGRVIG SGCNLDSARF RYLIGEKLGV NPTSCHGWVL GEHGDSSVPI
210 220 230 240 250
WSGVNVAGVT LKSLNPAIGT DSDKEHWKNV HKQVVEGGYE VLNMKGYTSW
260 270 280 290 300
AIGLSVTDLA RSILKNLKRV HPVTTLVKGF HGIKEEVFLS IPCVLGQSGI
310 320 330
TDFVKVNMTA EEEGLLKKSA DTLWNMQKDL QL
Length:332
Mass (Da):35,912
Last modified:January 23, 2007 - v2
Checksum:i367A7EA8B2A6D86A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71Q → E AA sequence (PubMed:6343385).Curated
Sequence conflicti15 – 151Missing AA sequence (PubMed:6343385).Curated
Sequence conflicti30 – 301N → D AA sequence (PubMed:6343385).Curated
Sequence conflicti56 – 561N → D AA sequence (PubMed:6343385).Curated
Sequence conflicti104 – 1041E → Q AA sequence (PubMed:6343385).Curated
Sequence conflicti124 – 1252IV → VI AA sequence (PubMed:6343385).Curated
Sequence conflicti135 – 1351I → V AA sequence (PubMed:6343385).Curated
Sequence conflicti223 – 2253DKE → NKQ AA sequence (PubMed:6343385).Curated
Sequence conflicti243 – 2431N → D AA sequence (PubMed:6343385).Curated
Sequence conflicti297 – 2971Q → E AA sequence (PubMed:6343385).Curated
Sequence conflicti329 – 3313DLQ → NLE AA sequence (PubMed:6343385).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04752 mRNA. Translation: CAA28449.1.
M17587 mRNA. Translation: AAA39425.1.
BC049602 mRNA. Translation: AAH49602.1.
M12781 mRNA. Translation: AAA88315.1.
CCDSiCCDS21290.1.
PIRiA26824. DEMSLC.
RefSeqiNP_038608.1. NM_013580.4.
XP_006540742.1. XM_006540679.1.
XP_006540743.1. XM_006540680.1.
XP_006540744.1. XM_006540681.1.
UniGeneiMm.16563.

Genome annotation databases

EnsembliENSMUST00000014545; ENSMUSP00000014545; ENSMUSG00000030851.
GeneIDi16833.
KEGGimmu:16833.
UCSCiuc009gzp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04752 mRNA. Translation: CAA28449.1.
M17587 mRNA. Translation: AAA39425.1.
BC049602 mRNA. Translation: AAH49602.1.
M12781 mRNA. Translation: AAA88315.1.
CCDSiCCDS21290.1.
PIRiA26824. DEMSLC.
RefSeqiNP_038608.1. NM_013580.4.
XP_006540742.1. XM_006540679.1.
XP_006540743.1. XM_006540680.1.
XP_006540744.1. XM_006540681.1.
UniGeneiMm.16563.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LDXX-ray2.96A/B/C/D2-332[»]
ProteinModelPortaliP00342.
SMRiP00342. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00342. 2 interactions.
MINTiMINT-6611882.
STRINGi10090.ENSMUSP00000014545.

PTM databases

iPTMnetiP00342.
PhosphoSiteiP00342.

2D gel databases

REPRODUCTION-2DPAGEP00342.

Proteomic databases

EPDiP00342.
PaxDbiP00342.
PRIDEiP00342.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014545; ENSMUSP00000014545; ENSMUSG00000030851.
GeneIDi16833.
KEGGimmu:16833.
UCSCiuc009gzp.1. mouse.

Organism-specific databases

CTDi3948.
MGIiMGI:96764. Ldhc.

Phylogenomic databases

eggNOGiKOG1495. Eukaryota.
COG0039. LUCA.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP00342.
KOiK00016.
OMAiRCKITVV.
OrthoDBiEOG7X0VH3.
PhylomeDBiP00342.
TreeFamiTF314963.

Enzyme and pathway databases

UniPathwayiUPA00554; UER00611.
ReactomeiR-MMU-70268. Pyruvate metabolism.

Miscellaneous databases

ChiTaRSiLdhc. mouse.
EvolutionaryTraceiP00342.
NextBioi290746.
PROiP00342.
SOURCEiSearch...

Gene expression databases

BgeeiP00342.
CleanExiMM_LDHC.
ExpressionAtlasiP00342. baseline and differential.
GenevisibleiP00342. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. L-lactate/malate_DH.
IPR011304. L-lactate_DH.
IPR018177. L-lactate_DH_AS.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and nucleotide sequence of the cDNA for sperm-specific lactate dehydrogenase-C from mouse."
    Sakai I., Sharief F.S., Li S.S.-L.
    Biochem. J. 242:619-622(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: DBA/2J.
    Tissue: Testis.
  2. "Molecular isolation and sequence determination of the cDNA for the mouse sperm-specific lactate dehydrogenase-X gene."
    Wu K.C., Chan K., Lee C.-Y.G., Lau Y.-F.C.
    Biochem. Biophys. Res. Commun. 146:964-970(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  4. "The tentative amino acid sequencing of lactate dehydrogenase C4 by X-ray diffraction analysis."
    Musick W.D., Rossmann M.G.
    J. Biol. Chem. 254:7621-7623(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-332.
  5. "The preliminary amino acid sequence of mouse testicular lactate dehydrogenase."
    Pan Y.-C.E., Huang S., Marciniszyn J.P. Jr., Lee C.-Y., Li S.S.-L.
    Hoppe-Seyler's Z. Physiol. Chem. 361:795-799(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-332.
  6. "Amino acid sequence studies on lactate dehydrogenase C4 isozymes from mouse and rat testes."
    Pan Y.-C.E., Sharief F.S., Okabe M., Huang S., Li S.S.-L.
    J. Biol. Chem. 258:7005-7016(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-332.
  7. "A postmeiotically expressed clone encodes lactate dehydrogenase isozyme X."
    Tanaka S., Fujimoto H.
    Biochem. Biophys. Res. Commun. 136:760-766(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 194-332.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  9. "RAB-like 2 has an essential role in male fertility, sperm intra-flagellar transport, and tail assembly."
    Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., Whisstock J.C., Field M.C., Adams V., Ishikawa T., Aitken R.J., Whittle B., Goodnow C.C., Ormandy C.J., O'Bryan M.K.
    PLoS Genet. 8:E1002969-E1002969(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABL2, TISSUE SPECIFICITY.
  10. "The structure of mouse testicular lactate dehydrogenase isoenzyme C4 at 2.9-A resolution."
    Musick W.D.L., Rossmann M.G.
    J. Biol. Chem. 254:7611-7620(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

Entry informationi

Entry nameiLDHC_MOUSE
AccessioniPrimary (citable) accession number: P00342
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.