ID LDHA_HUMAN Reviewed; 332 AA. AC P00338; B4DKQ2; B7Z5E3; D3DQY3; F8W819; Q53G53; Q6IBM7; Q6ZNV1; Q9UDE8; AC Q9UDE9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 259. DE RecName: Full=L-lactate dehydrogenase A chain {ECO:0000305}; DE Short=LDH-A; DE EC=1.1.1.27 {ECO:0000269|PubMed:11276087}; DE AltName: Full=Cell proliferation-inducing gene 19 protein; DE AltName: Full=LDH muscle subunit; DE Short=LDH-M {ECO:0000303|PubMed:11276087}; DE AltName: Full=Renal carcinoma antigen NY-REN-59; GN Name=LDHA {ECO:0000312|HGNC:HGNC:6535}; ORFNames=PIG19; 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] (ISOFORM 1). RX PubMed=3838278; DOI=10.1111/j.1432-1033.1985.tb08711.x; RA Tsujibo H., Tiano H.F., Li S.S.-L.; RT "Nucleotide sequences of the cDNA and an intronless pseudogene for human RT lactate dehydrogenase-A isozyme."; RL Eur. J. Biochem. 147:9-15(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=3000353; DOI=10.1042/bj2310537; RA Chung F.Z., Tsujibo H., Bhattacharyya U., Sharief F.S., Li S.S.-L.; RT "Genomic organization of human lactate dehydrogenase-A gene."; RL Biochem. J. 231:537-541(1985). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kim J.W.; RT "Identification of a human proliferation-inducing gene."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4). RC TISSUE=Umbilical cord; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-222. RC TISSUE=Gastric carcinoma; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] 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. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PROTEIN SEQUENCE OF 2-14; 43-57; 60-73; 77-112; 133-149; 158-169; 233-243; RP 306-315 AND 319-328, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (MAR-2005) to UniProtKB. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-121 AND 160-175. RX PubMed=1953713; DOI=10.1016/s0006-291x(05)81177-5; RA Maekawa M., Sudo K., Li S.S., Kanno T.; RT "Analysis of genetic mutations in human lactate dehydrogenase-A(M) RT deficiency using DNA conformation polymorphism in combination with RT polyacrylamide gradient gel and silver staining."; RL Biochem. Biophys. Res. Commun. 180:1083-1090(1991). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-254. RX PubMed=1959923; DOI=10.1007/bf00204925; RA Maekawa M., Sudo K., Li S.S., Kanno T.; RT "Genotypic analysis of families with lactate dehydrogenase A (M) deficiency RT by selective DNA amplification."; RL Hum. Genet. 88:34-38(1991). RN [13] RP INVOLVEMENT IN GSD11. RX PubMed=2334430; DOI=10.1016/0006-291x(90)92374-9; RA Maekawa M., Sudo K., Kanno T., Li S.S.; RT "Molecular characterization of genetic mutation in human lactate RT dehydrogenase-A (M) deficiency."; RL Biochem. Biophys. Res. Commun. 168:677-682(1990). RN [14] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal-cell RT carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [16] RP ISGYLATION. RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132; RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.; RT "Proteomic identification of proteins conjugated to ISG15 in mouse and RT human cells."; RL Biochem. Biophys. Res. Commun. 336:496-506(2005). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-10, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-14; LYS-57; LYS-81; RP LYS-118; LYS-126 AND LYS-318, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-310, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-57, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [28] RP INTERACTION WITH MP31, AND MUTAGENESIS OF ASP-56 AND ARG-99. RX PubMed=33406399; DOI=10.1016/j.cmet.2020.12.008; RA Huang N., Li F., Zhang M., Zhou H., Chen Z., Ma X., Yang L., Wu X., RA Zhong J., Xiao F., Yang X., Zhao K., Li X., Xia X., Liu Z., Gao S., RA Zhang N.; RT "An Upstream Open Reading Frame in Phosphatase and Tensin Homolog Encodes a RT Circuit Breaker of Lactate Metabolism."; RL Cell Metab. 33:128-144(2021). RN [29] RP ERRATUM OF PUBMED:33406399. RX PubMed=33535099; DOI=10.1016/j.cmet.2021.01.008; RA Huang N., Li F., Zhang M., Zhou H., Chen Z., Ma X., Yang L., Wu X., RA Zhong J., Xiao F., Yang X., Zhao K., Li X., Xia X., Liu Z., Gao S., RA Zhang N.; RL Cell Metab. 33:454-454(2021). RN [30] RP ACTIVITY REGULATION, INTERACTION WITH FLCN, AND MUTAGENESIS OF ARG-106. RX PubMed=34381247; DOI=10.1038/s41594-021-00633-2; RA Woodford M.R., Baker-Williams A.J., Sager R.A., Backe S.J., Blanden A.R., RA Hashmi F., Kancherla P., Gori A., Loiselle D.R., Castelli M., RA Serapian S.A., Colombo G., Haystead T.A., Jensen S.M., RA Stetler-Stevenson W.G., Loh S.N., Schmidt L.S., Linehan W.M., Bah A., RA Bourboulia D., Bratslavsky G., Mollapour M.; RT "The tumor suppressor folliculin inhibits lactate dehydrogenase A and RT regulates the Warburg effect."; RL Nat. Struct. Mol. Biol. 28:662-670(2021). RN [31] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADH AND SUBSTRATE RP ANALOG, HOMOTETRAMERIZATION, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=11276087; RX DOI=10.1002/1097-0134(20010501)43:2<175::aid-prot1029>3.0.co;2-#; RA Read J.A., Winter V.J., Eszes C.M., Sessions R.B., Brady R.L.; RT "Structural basis for altered activity of M- and H-isozyme forms of human RT lactate dehydrogenase."; RL Proteins 43:175-185(2001). RN [32] RP VARIANT CYS-315. RX PubMed=1445373; RA Sudo K., Maekawa M., Shioya M., Ikeda K., Takahashi N., Isogai Y., RA Li S.S.-L., Kanno T., Machida K., Toriumi J.; RT "Molecular analysis of genetic mutation in electrophoretic variant of human RT lactate dehydrogenase-A(M) subunit."; RL Biochem. Int. 27:1051-1057(1992). RN [33] RP VARIANT GLU-222. RX PubMed=7908613; RA Maekawa M., Sudo K., Kobayashi A., Sugiyama E., Li S.S.-L., Kanno T.; RT "Fast-type electrophoretic variant of lactate dehydrogenase M(A) and RT comparison with other missense mutations in lactate dehydrogenase M(A) and RT H(B) genes."; RL Clin. Chem. 40:665-668(1994). CC -!- FUNCTION: Interconverts simultaneously and stereospecifically pyruvate CC and lactate with concomitant interconversion of NADH and NAD(+). CC {ECO:0000269|PubMed:11276087}. 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:11276087}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445; CC Evidence={ECO:0000269|PubMed:11276087}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446; CC Evidence={ECO:0000269|PubMed:11276087}; CC -!- ACTIVITY REGULATION: Fermentation of pyruvate to lactate is inhibited CC when bound to folliculin FLCN, perhaps partly by FLCN preventing CC binding of cofactor NADH (PubMed:34381247). CC {ECO:0000269|PubMed:34381247}. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate CC from pyruvate: step 1/1. {ECO:0000305|PubMed:11276087}. CC -!- SUBUNIT: Homotetramer (PubMed:11276087). Interacts with PTEN upstream CC reading frame protein MP31 (PubMed:33406399). Interacts with folliculin CC FLCN; the interaction is direct and inhibits enzymatic activity CC (PubMed:34381247). {ECO:0000269|PubMed:11276087, CC ECO:0000269|PubMed:33406399, ECO:0000269|PubMed:34381247}. CC -!- INTERACTION: CC P00338; P11142: HSPA8; NbExp=4; IntAct=EBI-372327, EBI-351896; CC P00338; P00338: LDHA; NbExp=3; IntAct=EBI-372327, EBI-372327; CC P00338; P07195: LDHB; NbExp=3; IntAct=EBI-372327, EBI-358748; CC P00338-3; P07195: LDHB; NbExp=9; IntAct=EBI-10195200, EBI-358748; CC P00338-3; A0A286YFD7: MAPK10; NbExp=5; IntAct=EBI-10195200, EBI-17232183; CC P00338-3; Q499Y8: MAPK10; NbExp=3; IntAct=EBI-10195200, EBI-10241715; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P00338-1; Sequence=Displayed; CC Name=2; CC IsoId=P00338-2; Sequence=VSP_014261, VSP_042787; CC Name=3; CC IsoId=P00338-3; Sequence=VSP_042206; CC Name=4; CC IsoId=P00338-4; Sequence=VSP_042786; CC Name=5; CC IsoId=P00338-5; Sequence=VSP_042788, VSP_042789; CC -!- TISSUE SPECIFICITY: Predominantly expressed in anaerobic tissues such CC as skeletal muscle and liver. {ECO:0000305|PubMed:11276087}. CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}. CC -!- DISEASE: Glycogen storage disease 11 (GSD11) [MIM:612933]: A metabolic CC disorder that results in exertional myoglobinuria, pain, cramps and CC easy fatigue. {ECO:0000269|PubMed:2334430}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Lactate dehydrogenase entry; CC URL="https://en.wikipedia.org/wiki/Lactate_dehydrogenase"; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Another dark horse - Issue CC 109 of September 2009; CC URL="https://web.expasy.org/spotlight/back_issues/109"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X02152; CAA26088.1; -; mRNA. DR EMBL; X03077; CAA26879.1; -; Genomic_DNA. DR EMBL; X03078; CAA26879.1; JOINED; Genomic_DNA. DR EMBL; X03079; CAA26879.1; JOINED; Genomic_DNA. DR EMBL; X03080; CAA26879.1; JOINED; Genomic_DNA. DR EMBL; X03081; CAA26879.1; JOINED; Genomic_DNA. DR EMBL; X03082; CAA26879.1; JOINED; Genomic_DNA. DR EMBL; X03083; CAA26879.1; JOINED; Genomic_DNA. DR EMBL; AY423727; AAS00490.1; -; mRNA. DR EMBL; AK130587; BAC85389.1; -; mRNA. DR EMBL; AK296667; BAG59264.1; -; mRNA. DR EMBL; AK298834; BAH12879.1; -; mRNA. DR EMBL; CR456775; CAG33056.1; -; mRNA. DR EMBL; CR541714; CAG46515.1; -; mRNA. DR EMBL; AK223078; BAD96798.1; -; mRNA. DR EMBL; AC084117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471064; EAW68395.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68396.1; -; Genomic_DNA. DR EMBL; BC067223; AAH67223.1; -; mRNA. DR EMBL; S66853; AAB20418.1; -; Genomic_DNA. DR CCDS; CCDS44549.1; -. [P00338-4] DR CCDS; CCDS53609.1; -. [P00338-3] DR CCDS; CCDS53610.1; -. [P00338-2] DR CCDS; CCDS53611.1; -. [P00338-5] DR CCDS; CCDS7839.1; -. [P00338-1] DR PIR; A00347; DEHULM. DR RefSeq; NP_001128711.1; NM_001135239.1. [P00338-4] DR RefSeq; NP_001158886.1; NM_001165414.1. [P00338-3] DR RefSeq; NP_001158887.1; NM_001165415.1. [P00338-2] DR RefSeq; NP_001158888.1; NM_001165416.1. [P00338-5] DR RefSeq; NP_005557.1; NM_005566.3. [P00338-1] DR PDB; 1I10; X-ray; 2.30 A; A/B/C/D/E/F/G/H=2-332. DR PDB; 4AJP; X-ray; 2.38 A; A/B/C/D=2-332. DR PDB; 4JNK; X-ray; 1.90 A; A/B/C/D=2-332. DR PDB; 4L4R; X-ray; 2.10 A; A/H=2-332. DR PDB; 4L4S; X-ray; 2.90 A; A/H=2-332. DR PDB; 4M49; X-ray; 2.05 A; A/B/C/D=2-332. DR PDB; 4OJN; X-ray; 2.40 A; A/B/C/D/E/F/G/H=2-332. DR PDB; 4OKN; X-ray; 2.10 A; A/B/C/D/E/F/G/H=2-332. DR PDB; 4QO7; X-ray; 2.14 A; A/B/C/D=2-332. DR PDB; 4QO8; X-ray; 2.00 A; A/B/C/D=2-332. DR PDB; 4QSM; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2-332. DR PDB; 4QT0; X-ray; 3.20 A; A/B/C/D/E/F/G/H=2-332. DR PDB; 4R68; X-ray; 2.11 A; A/B/C/D=2-332. DR PDB; 4R69; X-ray; 3.19 A; A/B/C/D=2-332. DR PDB; 4RLS; X-ray; 1.91 A; A/B/C/D=2-332. DR PDB; 4ZVV; X-ray; 2.20 A; A/B/C/D=1-332. DR PDB; 5IXS; X-ray; 2.05 A; A/B/C/D=2-332. DR PDB; 5IXY; X-ray; 3.00 A; A/B/C/D=2-332. DR PDB; 5W8H; X-ray; 1.80 A; A/B/C/D=1-332. DR PDB; 5W8I; X-ray; 1.95 A; A/B/C/D=1-332. DR PDB; 5W8J; X-ray; 1.55 A; A/B/C/D=1-332. DR PDB; 5W8K; X-ray; 1.60 A; A/B/C/D=1-332. DR PDB; 5W8L; X-ray; 1.95 A; A/B/C/D=1-332. DR PDB; 5ZJD; X-ray; 2.39 A; A/B/C/D/E/F/G/H=2-332. DR PDB; 5ZJE; X-ray; 2.93 A; A/B/C/D/E/F/G/H/I/J/K/L=2-332. DR PDB; 5ZJF; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=2-332. DR PDB; 6BAD; X-ray; 2.10 A; A/B/C/D=2-332. DR PDB; 6BAG; X-ray; 2.40 A; A/B/C/D=2-332. DR PDB; 6BAX; X-ray; 2.05 A; A/B/C/D=2-332. DR PDB; 6BAZ; X-ray; 2.70 A; A/B/C/D=2-332. DR PDB; 6BB0; X-ray; 1.95 A; A/B/C/D=2-332. DR PDB; 6BB1; X-ray; 2.30 A; A/B/C/D/E/F/G/H=2-332. DR PDB; 6BB2; X-ray; 2.47 A; A/B/C/D/E/F/G/H=2-332. DR PDB; 6BB3; X-ray; 2.40 A; A/B/C/D=2-332. DR PDB; 6MV8; X-ray; 1.95 A; A/B/C/D=1-332. DR PDB; 6MVA; X-ray; 2.02 A; A/B/C/D=1-332. DR PDB; 6Q0D; X-ray; 2.05 A; A/B/C/D/E/F=1-332. DR PDB; 6Q13; X-ray; 2.00 A; A/B/C/D=1-332. DR PDB; 6SBU; X-ray; 2.91 A; A/B/C/D/E/F/G/H=2-332. DR PDB; 6SBV; X-ray; 2.60 A; A/B/C/D/E/F/G/H=2-332. DR PDB; 6ZZR; X-ray; 2.65 A; AAA/BBB/CCC/DDD/EEE/FFF/GGG/HHH=2-332. DR PDB; 7M2N; X-ray; 2.50 A; A/B/C/D=1-332. DR PDBsum; 1I10; -. DR PDBsum; 4AJP; -. DR PDBsum; 4JNK; -. DR PDBsum; 4L4R; -. DR PDBsum; 4L4S; -. DR PDBsum; 4M49; -. DR PDBsum; 4OJN; -. DR PDBsum; 4OKN; -. DR PDBsum; 4QO7; -. DR PDBsum; 4QO8; -. DR PDBsum; 4QSM; -. DR PDBsum; 4QT0; -. DR PDBsum; 4R68; -. DR PDBsum; 4R69; -. DR PDBsum; 4RLS; -. DR PDBsum; 4ZVV; -. DR PDBsum; 5IXS; -. DR PDBsum; 5IXY; -. DR PDBsum; 5W8H; -. DR PDBsum; 5W8I; -. DR PDBsum; 5W8J; -. DR PDBsum; 5W8K; -. DR PDBsum; 5W8L; -. DR PDBsum; 5ZJD; -. DR PDBsum; 5ZJE; -. DR PDBsum; 5ZJF; -. DR PDBsum; 6BAD; -. DR PDBsum; 6BAG; -. DR PDBsum; 6BAX; -. DR PDBsum; 6BAZ; -. DR PDBsum; 6BB0; -. DR PDBsum; 6BB1; -. DR PDBsum; 6BB2; -. DR PDBsum; 6BB3; -. DR PDBsum; 6MV8; -. DR PDBsum; 6MVA; -. DR PDBsum; 6Q0D; -. DR PDBsum; 6Q13; -. DR PDBsum; 6SBU; -. DR PDBsum; 6SBV; -. DR PDBsum; 6ZZR; -. DR PDBsum; 7M2N; -. DR AlphaFoldDB; P00338; -. DR SMR; P00338; -. DR BioGRID; 110131; 325. DR ComplexPortal; CPX-6573; L-lactate dehydrogenase A complex. DR ComplexPortal; CPX-6592; L-lactate dehydrogenase complex, A3B1 variant. DR ComplexPortal; CPX-6594; L-lactate dehydrogenase complex, A2B2 variant. DR ComplexPortal; CPX-6598; L-lactate dehydrogenase complex, A1B3 variant. DR IntAct; P00338; 78. DR MINT; P00338; -. DR STRING; 9606.ENSP00000445175; -. DR BindingDB; P00338; -. DR ChEMBL; CHEMBL4835; -. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB09130; Copper. DR DrugBank; DB02483; Etheno-NAD. DR DrugBank; DB00157; NADH. DR DrugBank; DB02701; Nicotinamide. DR DrugBank; DB03940; Oxamic Acid. DR DrugBank; DB09118; Stiripentol. DR DrugCentral; P00338; -. DR GlyCosmos; P00338; 1 site, 2 glycans. DR GlyGen; P00338; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; P00338; -. DR MetOSite; P00338; -. DR PhosphoSitePlus; P00338; -. DR SwissPalm; P00338; -. DR BioMuta; LDHA; -. DR DMDM; 126047; -. DR DOSAC-COBS-2DPAGE; P00338; -. DR OGP; P00338; -. DR REPRODUCTION-2DPAGE; IPI00217966; -. DR CPTAC; CPTAC-2749; -. DR CPTAC; CPTAC-2750; -. DR CPTAC; CPTAC-91; -. DR EPD; P00338; -. DR jPOST; P00338; -. DR MassIVE; P00338; -. DR MaxQB; P00338; -. DR PaxDb; 9606-ENSP00000445175; -. DR PeptideAtlas; P00338; -. DR ProteomicsDB; 51230; -. [P00338-1] DR ProteomicsDB; 51231; -. [P00338-2] DR ProteomicsDB; 51232; -. [P00338-3] DR ProteomicsDB; 51233; -. [P00338-4] DR ProteomicsDB; 51234; -. [P00338-5] DR Pumba; P00338; -. DR TopDownProteomics; P00338-1; -. [P00338-1] DR TopDownProteomics; P00338-4; -. [P00338-4] DR TopDownProteomics; P00338-5; -. [P00338-5] DR Antibodypedia; 4200; 1029 antibodies from 40 providers. DR DNASU; 3939; -. DR Ensembl; ENST00000227157.8; ENSP00000227157.4; ENSG00000134333.15. [P00338-5] DR Ensembl; ENST00000379412.9; ENSP00000368722.6; ENSG00000134333.15. [P00338-3] DR Ensembl; ENST00000396222.6; ENSP00000379524.2; ENSG00000134333.15. [P00338-2] DR Ensembl; ENST00000422447.8; ENSP00000395337.3; ENSG00000134333.15. [P00338-1] DR Ensembl; ENST00000430553.6; ENSP00000406172.2; ENSG00000134333.15. [P00338-4] DR Ensembl; ENST00000542179.1; ENSP00000445331.1; ENSG00000134333.15. [P00338-1] DR Ensembl; ENST00000671981.1; ENSP00000499898.1; ENSG00000288299.1. [P00338-1] DR Ensembl; ENST00000672078.1; ENSP00000500354.1; ENSG00000288299.1. [P00338-5] DR Ensembl; ENST00000672405.1; ENSP00000500953.1; ENSG00000288299.1. [P00338-1] DR Ensembl; ENST00000672996.1; ENSP00000500284.1; ENSG00000288299.1. [P00338-4] DR Ensembl; ENST00000673007.1; ENSP00000500603.1; ENSG00000288299.1. [P00338-3] DR Ensembl; ENST00000673083.1; ENSP00000500168.1; ENSG00000288299.1. [P00338-2] DR Ensembl; ENST00000673204.1; ENSP00000499977.1; ENSG00000288299.1. [P00338-1] DR GeneID; 3939; -. DR KEGG; hsa:3939; -. DR MANE-Select; ENST00000422447.8; ENSP00000395337.3; NM_005566.4; NP_005557.1. DR UCSC; uc001mol.4; human. [P00338-1] DR AGR; HGNC:6535; -. DR CTD; 3939; -. DR DisGeNET; 3939; -. DR GeneCards; LDHA; -. DR HGNC; HGNC:6535; LDHA. DR HPA; ENSG00000134333; Low tissue specificity. DR MalaCards; LDHA; -. DR MIM; 150000; gene. DR MIM; 612933; phenotype. DR neXtProt; NX_P00338; -. DR OpenTargets; ENSG00000134333; -. DR Orphanet; 284426; Glycogen storage disease due to lactate dehydrogenase M-subunit deficiency. DR PharmGKB; PA30319; -. DR VEuPathDB; HostDB:ENSG00000134333; -. DR eggNOG; KOG1495; Eukaryota. DR GeneTree; ENSGT00940000153201; -. DR HOGENOM; CLU_045401_0_2_1; -. DR InParanoid; P00338; -. DR OMA; IKKHCPQ; -. DR OrthoDB; 5344346at2759; -. DR PhylomeDB; P00338; -. DR TreeFam; TF314963; -. DR BRENDA; 1.1.1.27; 2681. DR PathwayCommons; P00338; -. DR Reactome; R-HSA-70268; Pyruvate metabolism. DR SABIO-RK; P00338; -. DR SignaLink; P00338; -. DR SIGNOR; P00338; -. DR UniPathway; UPA00554; UER00611. DR BioGRID-ORCS; 3939; 203 hits in 1153 CRISPR screens. DR ChiTaRS; LDHA; human. DR EvolutionaryTrace; P00338; -. DR GeneWiki; LDHA; -. DR GenomeRNAi; 3939; -. DR Pharos; P00338; Tchem. DR PRO; PR:P00338; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P00338; Protein. DR Bgee; ENSG00000134333; Expressed in ventricular zone and 117 other cell types or tissues. DR ExpressionAtlas; P00338; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:1990204; C:oxidoreductase complex; IPI:ComplexPortal. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IMP:UniProtKB. DR GO; GO:0006096; P:glycolytic process; NAS:UniProtKB. DR GO; GO:0006089; P:lactate metabolic process; IDA:ComplexPortal. DR GO; GO:0006090; P:pyruvate metabolic process; IDA:ComplexPortal. DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB. DR CDD; cd05293; LDH_1; 1. 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 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 NCBIfam; TIGR01771; L-LDH-NAD; 1. DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1. DR PANTHER; PTHR43128:SF10; L-LACTATE DEHYDROGENASE A CHAIN; 1. 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; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00064; L_LDH; 1. DR Genevisible; P00338; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; Disease variant; Glycogen storage disease; KW Isopeptide bond; NAD; Oxidoreductase; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT CHAIN 2..332 FT /note="L-lactate dehydrogenase A chain" FT /id="PRO_0000168411" FT ACT_SITE 193 FT /note="Proton acceptor" FT BINDING 29..57 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:11276087" FT BINDING 99 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:11276087" FT BINDING 106 FT /ligand="substrate" FT BINDING 138 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:11276087" FT BINDING 138 FT /ligand="substrate" FT BINDING 169 FT /ligand="substrate" FT BINDING 248 FT /ligand="substrate" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 5 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 5 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06151" FT MOD_RES 10 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 14 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 18 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 57 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 81 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 118 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 118 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06151" FT MOD_RES 126 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 224 FT /note="N6-acetyllysine" 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 310 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 318 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" 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:0007744|PubMed:28112733" FT VAR_SEQ 1 FT /note="M -> MGEPSGGYTYTQTSIFLFHAKIPFGSKSNM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042206" FT VAR_SEQ 82..139 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042786" FT VAR_SEQ 230..274 FT /note="VHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVS -> CRY FT TLGDPKGAAILKSSDVISFHCLGYNRILGGGCACCPFYLICD (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_014261" FT VAR_SEQ 237..241 FT /note="SAYEV -> RVFTE (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_042788" FT VAR_SEQ 242..332 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_042789" FT VAR_SEQ 275..332 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042787" FT VARIANT 222 FT /note="K -> E (in dbSNP:rs748436361)" FT /evidence="ECO:0000269|PubMed:7908613, ECO:0000269|Ref.6" FT /id="VAR_004180" FT VARIANT 315 FT /note="R -> C (in dbSNP:rs200093825)" FT /evidence="ECO:0000269|PubMed:1445373" FT /id="VAR_004181" FT MUTAGEN 56 FT /note="D->A: Abolishes interaction with MP31." FT /evidence="ECO:0000269|PubMed:33406399" FT MUTAGEN 99 FT /note="R->A: Abolishes interaction with MP31." FT /evidence="ECO:0000269|PubMed:33406399" FT MUTAGEN 106 FT /note="R->A,K,Q: Increases binding to FLCN." FT /evidence="ECO:0000269|PubMed:34381247" FT HELIX 4..8 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 9..11 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 20..26 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 30..41 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 46..51 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 55..67 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 68..71 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 83..86 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 90..94 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 106..127 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 140..151 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 164..178 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 189..194 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:5W8I" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 211..214 FT /evidence="ECO:0007829|PDB:5W8J" FT TURN 216..219 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:6Q0D" FT HELIX 228..245 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 250..264 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 269..276 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:5ZJE" FT STRAND 288..296 FT /evidence="ECO:0007829|PDB:5W8J" FT STRAND 299..304 FT /evidence="ECO:0007829|PDB:5W8J" FT HELIX 310..327 FT /evidence="ECO:0007829|PDB:5W8J" SQ SEQUENCE 332 AA; 36689 MW; 401E8604CEB7F908 CRC64; MATLKDQLIY NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG EMMDLQHGSL FLRTPKIVSG KDYNVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI IPNVVKYSPN CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV HPLSCHGWVL GEHGDSSVPV WSGMNVAGVS LKTLHPDLGT DKDKEQWKEV HKQVVESAYE VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPVSTMIKGL YGIKDDVFLS VPCILGQNGI SDLVKVTLTS EEEARLKKSA DTLWGIQKEL QF //