ID DLDH_MOUSE Reviewed; 509 AA. AC O08749; Q3TG55; Q3U5W5; Q3UWP7; Q99LD3; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 27-MAR-2024, entry version 199. DE RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial; DE EC=1.8.1.4 {ECO:0000250|UniProtKB:P09622}; DE AltName: Full=Dihydrolipoamide dehydrogenase; DE Flags: Precursor; GN Name=Dld; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=DBA/2J; RX PubMed=9169128; DOI=10.1006/geno.1997.4670; RA Johnson M., Yang H.S., Johanning G.L., Patel M.S.; RT "Characterization of the mouse dihydrolipoamide dehydrogenase (Dld) gene: RT genomic structure, promoter sequence, and chromosomal localization."; RL Genomics 41:320-326(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Heart; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary tumor; 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 [4] RP PROTEIN SEQUENCE OF 73-89; 216-259; 289-334; 316-334; 347-365; 421-428 AND RP 483-509, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP SUBCELLULAR LOCATION. RX PubMed=15888450; DOI=10.1074/jbc.m500310200; RA Mitra K., Rangaraj N., Shivaji S.; RT "Novelty of the pyruvate metabolic enzyme dihydrolipoamide dehydrogenase in RT spermatozoa: correlation of its localization, tyrosine phosphorylation, and RT activity during sperm capacitation."; RL J. Biol. Chem. 280:25743-25753(2005). RN [6] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=17404228; DOI=10.1073/pnas.0610618104; RA Babady N.E., Pang Y.P., Elpeleg O., Isaya G.; RT "Cryptic proteolytic activity of dihydrolipoamide dehydrogenase."; RL Proc. Natl. Acad. Sci. U.S.A. 104:6158-6163(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-410, SUCCINYLATION RP [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122; LYS-132; LYS-143; RP LYS-159; LYS-166; LYS-273; LYS-277; LYS-334; LYS-410; LYS-430 AND LYS-505, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122; LYS-132; RP LYS-143; LYS-334; LYS-346; LYS-410; LYS-420 AND LYS-505, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria RT identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [10] RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=36854377; DOI=10.1098/rsob.220363; RA Hevler J.F., Albanese P., Cabrera-Orefice A., Potter A., Jankevics A., RA Misic J., Scheltema R.A., Brandt U., Arnold S., Heck A.J.R.; RT "MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate RT dehydrogenase complex."; RL Open Biol. 13:220363-220363(2023). CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine CC cleavage system as well as an E3 component of three alpha-ketoacid CC dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched- CC chain amino acid-dehydrogenase complex) (By similarity). The 2- CC oxoglutarate dehydrogenase complex is mainly active in the CC mitochondrion (By similarity). A fraction of the 2-oxoglutarate CC dehydrogenase complex also localizes in the nucleus and is required for CC lysine succinylation of histones: associates with KAT2A on chromatin CC and provides succinyl-CoA to histone succinyltransferase KAT2A (By CC similarity). In monomeric form may have additional moonlighting CC function as serine protease (PubMed:17404228). Involved in the CC hyperactivation of spermatazoa during capacitation and in the CC spermatazoal acrosome reaction (By similarity). CC {ECO:0000250|UniProtKB:P09622, ECO:0000250|UniProtKB:Q811C4, CC ECO:0000269|PubMed:17404228}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + CC N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, CC ChEBI:CHEBI:83100; EC=1.8.1.4; CC Evidence={ECO:0000250|UniProtKB:P09622}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P09622}; CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P09622}; CC -!- SUBUNIT: Homodimer. Part of the multimeric pyruvate dehydrogenase CC complex that contains multiple copies of pyruvate dehydrogenase CC (subunits PDHA (PDHA1 or PDHA2) and PDHB, E1), dihydrolipoamide CC acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). CC These subunits are bound to an inner core composed of about 48 DLAT and CC 12 PDHX molecules (by non covalent bonds). The 2-oxoglutarate CC dehydrogenase complex is composed of OGDH (2-oxoglutarate CC dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2), CC DLD (dihydrolipoamide dehydrogenase; E3) and the assembly factor KGD4 CC (PubMed:36854377). It contains multiple copies of the three enzymatic CC components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate CC dehydrogenase complex associates with KAT2A. Interacts with PDHX. CC {ECO:0000250|UniProtKB:P09622, ECO:0000269|PubMed:36854377}. CC -!- INTERACTION: CC O08749; O54910: Nfkbie; NbExp=4; IntAct=EBI-773199, EBI-6688774; CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000305|PubMed:36854377, ECO:0000305|PubMed:9169128}. Nucleus CC {ECO:0000250|UniProtKB:P09622}. Cell projection, cilium, flagellum CC {ECO:0000250|UniProtKB:Q811C4}. Cytoplasmic vesicle, secretory vesicle, CC acrosome {ECO:0000269|PubMed:15888450}. Note=Mainly localizes in the CC mitochondrion. A small fraction localizes to the nucleus, where the 2- CC oxoglutarate dehydrogenase complex is required for histone CC succinylation. {ECO:0000250|UniProtKB:P09622}. CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level). CC {ECO:0000269|PubMed:17404228}. CC -!- PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC {ECO:0000250|UniProtKB:P09624}. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000305}. 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; U73445; AAC53170.1; -; mRNA. DR EMBL; AK117104; BAE43405.1; -; mRNA. DR EMBL; AK136193; BAE22867.1; -; mRNA. DR EMBL; AK153399; BAE31961.1; -; mRNA. DR EMBL; AK168875; BAE40693.1; -; mRNA. DR EMBL; BC003368; AAH03368.1; -; mRNA. DR CCDS; CCDS36428.1; -. DR RefSeq; NP_031887.2; NM_007861.5. DR AlphaFoldDB; O08749; -. DR SMR; O08749; -. DR BioGRID; 199227; 67. DR IntAct; O08749; 37. DR MINT; O08749; -. DR STRING; 10090.ENSMUSP00000106481; -. DR ChEMBL; CHEMBL2176826; -. DR GlyGen; O08749; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O08749; -. DR MetOSite; O08749; -. DR PhosphoSitePlus; O08749; -. DR SwissPalm; O08749; -. DR REPRODUCTION-2DPAGE; O08749; -. DR CPTAC; non-CPTAC-3704; -. DR EPD; O08749; -. DR jPOST; O08749; -. DR MaxQB; O08749; -. DR PaxDb; 10090-ENSMUSP00000106481; -. DR PeptideAtlas; O08749; -. DR ProteomicsDB; 277461; -. DR Pumba; O08749; -. DR Antibodypedia; 17237; 586 antibodies from 36 providers. DR DNASU; 13382; -. DR Ensembl; ENSMUST00000110857.5; ENSMUSP00000106481.4; ENSMUSG00000020664.11. DR GeneID; 13382; -. DR KEGG; mmu:13382; -. DR UCSC; uc007nhg.3; mouse. DR AGR; MGI:107450; -. DR CTD; 1738; -. DR MGI; MGI:107450; Dld. DR VEuPathDB; HostDB:ENSMUSG00000020664; -. DR eggNOG; KOG1335; Eukaryota. DR GeneTree; ENSGT00550000074844; -. DR HOGENOM; CLU_016755_0_1_1; -. DR InParanoid; O08749; -. DR OMA; CAQLGMK; -. DR OrthoDB; 5473641at2759; -. DR PhylomeDB; O08749; -. DR TreeFam; TF300414; -. DR BRENDA; 1.4.1.27; 3474. DR Reactome; R-MMU-204174; Regulation of pyruvate dehydrogenase (PDH) complex. DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation. DR Reactome; R-MMU-5362517; Signaling by Retinoic Acid. DR Reactome; R-MMU-6783984; Glycine degradation. DR Reactome; R-MMU-70268; Pyruvate metabolism. DR Reactome; R-MMU-70895; Branched-chain amino acid catabolism. DR Reactome; R-MMU-71064; Lysine catabolism. DR Reactome; R-MMU-71403; Citric acid cycle (TCA cycle). DR BioGRID-ORCS; 13382; 24 hits in 81 CRISPR screens. DR ChiTaRS; Dld; mouse. DR PRO; PR:O08749; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; O08749; Protein. DR Bgee; ENSMUSG00000020664; Expressed in saccule of membranous labyrinth and 284 other cell types or tissues. DR GO; GO:1902493; C:acetyltransferase complex; IMP:MGI. DR GO; GO:0043159; C:acrosomal matrix; IDA:MGI. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0045240; C:dihydrolipoyl dehydrogenase complex; IMP:MGI. DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISO:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IDA:MGI. DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IMP:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IMP:MGI. DR GO; GO:0045254; C:pyruvate dehydrogenase complex; ISO:MGI. DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IMP:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI. DR GO; GO:0043544; F:lipoamide binding; ISO:MGI. DR GO; GO:0051287; F:NAD binding; ISO:MGI. DR GO; GO:0034604; F:pyruvate dehydrogenase (NAD+) activity; IEA:Ensembl. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISO:MGI. DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IMP:MGI. DR GO; GO:0009083; P:branched-chain amino acid catabolic process; ISO:MGI. DR GO; GO:0051068; P:dihydrolipoamide metabolic process; ISO:MGI. DR GO; GO:0007369; P:gastrulation; IMP:MGI. DR GO; GO:0106077; P:histone succinylation; ISS:UniProtKB. DR GO; GO:0009106; P:lipoate metabolic process; ISO:MGI. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:MGI. DR GO; GO:0006508; P:proteolysis; IDA:MGI. DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI. DR GO; GO:0048240; P:sperm capacitation; IDA:MGI. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf. DR InterPro; IPR006258; Lipoamide_DH. DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR NCBIfam; TIGR01350; lipoamide_DH; 1. DR PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. DR SWISS-2DPAGE; O08749; -. DR Genevisible; O08749; MM. PE 1: Evidence at protein level; KW Acetylation; Cell projection; Cilium; Cytoplasmic vesicle; KW Direct protein sequencing; Disulfide bond; FAD; Flagellum; Flavoprotein; KW Mitochondrion; NAD; Nucleus; Oxidoreductase; Phosphoprotein; KW Redox-active center; Reference proteome; Transit peptide. FT TRANSIT 1..35 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 36..509 FT /note="Dihydrolipoyl dehydrogenase, mitochondrial" FT /id="PRO_0000030297" FT ACT_SITE 487 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P09624" FT BINDING 71..80 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P09622" FT BINDING 89 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P09622" FT BINDING 154 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P09622" FT BINDING 183..185 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P09622" FT BINDING 220..227 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P09622" FT BINDING 243 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P09622" FT BINDING 278 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P09622" FT BINDING 314 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P09622" FT BINDING 355 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P09622" FT BINDING 361..364 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P09622" FT SITE 448 FT /note="Important for interaction with PDHX and activity of FT pyruvate dehydrogenase complex" FT /evidence="ECO:0000250|UniProtKB:P09622" FT SITE 473 FT /note="Important for interaction with PDHX and activity of FT pyruvate dehydrogenase complex" FT /evidence="ECO:0000250|UniProtKB:P09622" FT MOD_RES 66 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753, FT ECO:0007744|PubMed:23806337" FT MOD_RES 66 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 104 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 104 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 122 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 122 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 132 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 132 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 143 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 143 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 159 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 166 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 273 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 277 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 285 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 297 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P6R2" FT MOD_RES 334 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 334 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 346 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 410 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753, FT ECO:0007744|PubMed:23806337" FT MOD_RES 410 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 417 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P09622" FT MOD_RES 420 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 430 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 505 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 505 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT DISULFID 80..85 FT /note="Redox-active" FT /evidence="ECO:0000250|UniProtKB:P09624" FT CONFLICT 54 FT /note="Y -> C (in Ref. 1; AAC53170)" FT /evidence="ECO:0000305" FT CONFLICT 144 FT /note="Q -> T (in Ref. 2; BAE22867)" FT /evidence="ECO:0000305" FT CONFLICT 149 FT /note="H -> L (in Ref. 2; BAE31961)" FT /evidence="ECO:0000305" FT CONFLICT 283 FT /note="K -> E (in Ref. 2; BAE40693)" FT /evidence="ECO:0000305" SQ SEQUENCE 509 AA; 54272 MW; 2C381852BAAD0441 CRC64; MQSWSRVYRS LAKKGHFNRI SHGLQGVSSV PLRTYADQPI EADVTVIGSG PGGYVAAIKS AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEIPEVRLNL EKMMEQKHSA VKALTGGIAH LFKQNKVVHV NGFGKITGKN QVTATKADGS TQVIDTKNIL VATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG IGIDMEISKN FQRILQRQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN NRFQTKIPNI YAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEFKIGK FPFAANSRAK TNADTDGMVK ILGHKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI ARVCHAHPTL SEAFREANLA AAFGKPINF //