LDH6A_HUMAN
ID LDH6A_HUMAN Reviewed; 332 AA.
AC Q6ZMR3; D3DQY5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=L-lactate dehydrogenase A-like 6A;
DE Short=LDHA-like protein 6A;
DE EC=1.1.1.27 {ECO:0000269|PubMed:18351441};
GN Name=LDHAL6A; Synonyms=LDHL2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=18351441; DOI=10.1007/s11033-008-9227-2;
RA Chen X., Gu X., Shan Y., Tang W., Yuan J., Zhong Z., Wang Y., Huang W.,
RA Wan B., Yu L.;
RT "Identification of a novel human lactate dehydrogenase gene LDHAL6A, which
RT activates transcriptional activities of AP1(PMA).";
RL Mol. Biol. Rep. 36:669-676(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of L-lactate and pyruvate with
CC nicotinamide adenine dinucleotide NAD(+) as a coenzyme
CC (PubMed:18351441). Significantly increases the transcriptional activity
CC of JUN, when overexpressed. {ECO:0000269|PubMed:18351441}.
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:0000269|PubMed:18351441};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445;
CC Evidence={ECO:0000250|UniProtKB:P00338};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446;
CC Evidence={ECO:0000305|PubMed:18351441};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18351441}.
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:18351441}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; AY581313; AAS93432.1; -; mRNA.
DR EMBL; AK131523; BAD18662.1; -; mRNA.
DR EMBL; CH471064; EAW68387.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68388.1; -; Genomic_DNA.
DR CCDS; CCDS7841.1; -.
DR RefSeq; NP_001137543.1; NM_001144071.1.
DR RefSeq; NP_659409.2; NM_144972.4.
DR AlphaFoldDB; Q6ZMR3; -.
DR SMR; Q6ZMR3; -.
DR BioGRID; 127750; 36.
DR IntAct; Q6ZMR3; 9.
DR STRING; 9606.ENSP00000280706; -.
DR DrugBank; DB00157; NADH.
DR iPTMnet; Q6ZMR3; -.
DR PhosphoSitePlus; Q6ZMR3; -.
DR SwissPalm; Q6ZMR3; -.
DR BioMuta; LDHAL6A; -.
DR DMDM; 51316252; -.
DR EPD; Q6ZMR3; -.
DR jPOST; Q6ZMR3; -.
DR MassIVE; Q6ZMR3; -.
DR MaxQB; Q6ZMR3; -.
DR PaxDb; Q6ZMR3; -.
DR PeptideAtlas; Q6ZMR3; -.
DR PRIDE; Q6ZMR3; -.
DR ProteomicsDB; 67905; -.
DR Antibodypedia; 25097; 123 antibodies from 23 providers.
DR DNASU; 160287; -.
DR Ensembl; ENST00000280706.3; ENSP00000280706.2; ENSG00000166800.11.
DR Ensembl; ENST00000396213.7; ENSP00000379516.3; ENSG00000166800.11.
DR GeneID; 160287; -.
DR KEGG; hsa:160287; -.
DR MANE-Select; ENST00000280706.3; ENSP00000280706.2; NM_144972.5; NP_659409.2.
DR UCSC; uc001mop.2; human.
DR CTD; 160287; -.
DR GeneCards; LDHAL6A; -.
DR HGNC; HGNC:28335; LDHAL6A.
DR HPA; ENSG00000166800; Tissue enriched (testis).
DR MIM; 618928; gene.
DR neXtProt; NX_Q6ZMR3; -.
DR OpenTargets; ENSG00000166800; -.
DR PharmGKB; PA134950539; -.
DR VEuPathDB; HostDB:ENSG00000166800; -.
DR eggNOG; KOG1495; Eukaryota.
DR GeneTree; ENSGT00940000164064; -.
DR HOGENOM; CLU_045401_0_2_1; -.
DR InParanoid; Q6ZMR3; -.
DR OMA; VDELVIC; -.
DR OrthoDB; 1204514at2759; -.
DR PhylomeDB; Q6ZMR3; -.
DR TreeFam; TF314963; -.
DR PathwayCommons; Q6ZMR3; -.
DR Reactome; R-HSA-70268; Pyruvate metabolism.
DR SignaLink; Q6ZMR3; -.
DR UniPathway; UPA00554; UER00611.
DR BioGRID-ORCS; 160287; 8 hits in 1069 CRISPR screens.
DR ChiTaRS; LDHAL6A; human.
DR GenomeRNAi; 160287; -.
DR Pharos; Q6ZMR3; Tbio.
DR PRO; PR:Q6ZMR3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6ZMR3; protein.
DR Bgee; ENSG00000166800; Expressed in secondary oocyte and 96 other tissues.
DR ExpressionAtlas; Q6ZMR3; baseline and differential.
DR Genevisible; Q6ZMR3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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 Acetylation; Cytoplasm; Isopeptide bond; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00338"
FT CHAIN 2..332
FT /note="L-lactate dehydrogenase A-like 6A"
FT /id="PRO_0000168457"
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|UniProtKB:P00338"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00338"
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|UniProtKB:P00338"
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="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P00338"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00338"
FT MOD_RES 5
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06151"
FT MOD_RES 57
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00338"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00338"
FT MOD_RES 118
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00338"
FT MOD_RES 118
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06151"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06151"
FT MOD_RES 239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06151"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06151"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04642"
FT MOD_RES 318
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00338"
FT MOD_RES 318
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06151"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04642"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P00338"
SQ SEQUENCE 332 AA; 36507 MW; 7C1B9FCAE9050A9B CRC64;
MATIKSELIK NFAEEEAIHH NKISIVGTGS VGVACAISIL LKGLSDELVL VDVDEGKLKG
ETMDLQHGSP FMKMPNIVSS KDYLVTANSN LVIITAGARQ KKGETRLDLV QRNVSIFKLM
IPNITQYSPH CKLLIVTNPV DILTYVAWKL SGFPKNRVIG SGCNLDSARF RYFIGQRLGI
HSESCHGLIL GEHGDSSVPV WSGVNIAGVP LKDLNPDIGT DKDPEQWENV HKKVISSGYE
MVKMKGYTSW GISLSVADLT ESILKNLRRV HPVSTLSKGL YGINEDIFLS VPCILGENGI
TDLIKVKLTL EEEACLQKSA ETLWEIQKEL KL
