LDHA_HUMAN
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 03-AUG-2022, entry version 250.
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";
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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; 271.
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; 75.
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 GlyGen; P00338; 1 site, 2 O-linked glycans (1 site).
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-91; -.
DR EPD; P00338; -.
DR jPOST; P00338; -.
DR MassIVE; P00338; -.
DR MaxQB; P00338; -.
DR PaxDb; P00338; -.
DR PeptideAtlas; P00338; -.
DR PRIDE; 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 TopDownProteomics; P00338-1; -. [P00338-1]
DR TopDownProteomics; P00338-4; -. [P00338-4]
DR TopDownProteomics; P00338-5; -. [P00338-5]
DR Antibodypedia; 4200; 911 antibodies from 40 providers.
DR DNASU; 3939; -.
DR Ensembl; ENST00000227157.8; ENSP00000227157.4; ENSG00000134333.14. [P00338-5]
DR Ensembl; ENST00000379412.9; ENSP00000368722.5; ENSG00000134333.14. [P00338-1]
DR Ensembl; ENST00000396222.6; ENSP00000379524.2; ENSG00000134333.14. [P00338-2]
DR Ensembl; ENST00000422447.8; ENSP00000395337.3; ENSG00000134333.14. [P00338-1]
DR Ensembl; ENST00000430553.6; ENSP00000406172.2; ENSG00000134333.14. [P00338-4]
DR Ensembl; ENST00000540430.5; ENSP00000445175.1; ENSG00000134333.14. [P00338-3]
DR Ensembl; ENST00000542179.1; ENSP00000445331.1; ENSG00000134333.14. [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 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; SICKYIL; -.
DR OrthoDB; 1204514at2759; -.
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 1073 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 115 other tissues.
DR ExpressionAtlas; P00338; baseline and differential.
DR Genevisible; P00338; HS.
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: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 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 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
