ID   F5H155_HUMAN            Unreviewed;       225 AA.
AC   F5H155;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|RuleBase:RU000496};
DE            EC=1.1.1.27 {ECO:0000256|RuleBase:RU000496};
GN   Name=LDHC {ECO:0000313|Ensembl:ENSP00000443997.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000443997.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000443997.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000443997.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Possible role in sperm motility.
CC       {ECO:0000256|ARBA:ARBA00037359}.
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         Evidence={ECO:0000256|RuleBase:RU000496};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843,
CC       ECO:0000256|RuleBase:RU000496}.
CC   -!- SUBUNIT: Homotetramer. Interacts with RABL2/RABL2A; binds
CC       preferentially to GTP-bound RABL2. {ECO:0000256|ARBA:ARBA00038717}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054}.
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DR   EMBL; AC027544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC084117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F5H155; -.
DR   SMR; F5H155; -.
DR   SwissPalm; F5H155; -.
DR   MassIVE; F5H155; -.
DR   MaxQB; F5H155; -.
DR   PeptideAtlas; F5H155; -.
DR   ProteomicsDB; 25547; -.
DR   Antibodypedia; 25085; 287 antibodies from 33 providers.
DR   Ensembl; ENST00000535809.1; ENSP00000443997.1; ENSG00000166796.12.
DR   UCSC; uc057zrq.1; human.
DR   HGNC; HGNC:6544; LDHC.
DR   VEuPathDB; HostDB:ENSG00000166796; -.
DR   GeneTree; ENSGT00940000161479; -.
DR   UniPathway; UPA00554; UER00611.
DR   ChiTaRS; LDHC; human.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000166796; Expressed in left testis and 138 other cell types or tissues.
DR   ExpressionAtlas; F5H155; baseline and differential.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001557; L-lactate/malate_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   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF5; L-LACTATE DEHYDROGENASE C CHAIN; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00064; L_LDH; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU000496};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000496};
KW   Proteomics identification {ECO:0007829|EPD:F5H155,
KW   ECO:0007829|MaxQB:F5H155};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT   DOMAIN          21..160
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          164..201
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
SQ   SEQUENCE   225 AA;  24593 MW;  F9055A58F7BA3BA0 CRC64;
     MSTVKEQLIE KLIEDDENSQ CKITIVGTGA VGMACAISIL LKDLADELAL VDVALDKLKG
     EMMDLQHGSL FFSTSKITSG KDYSVSANSR IVIVTAGARQ QEGETRLALV QRNVAIMKSI
     IPAIVHYSPD CKILVVSNPV DILTYIVWKI SGLPVTRVIG SGCNLDSARF RYLIGEKLGV
     HPTSCHGWII GEHGDSSGII WNKRRTLSQY PLCLGAEWCL RCCEN
//