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
//