DLDH_MOUSE
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 03-AUG-2022, entry version 190.
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, Pancreas,
RC 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).
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=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-
CC lipoyl-L-lysyl-[protein] + H(+) + 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) and
CC DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies
CC of the three enzymatic components (E1, E2 and E3). In the nucleus, the
CC 2-oxoglutarate dehydrogenase complex associates with KAT2A. Interacts
CC with PDHX. {ECO:0000250|UniProtKB:P09622}.
CC -!- INTERACTION:
CC O08749; O54910: Nfkbie; NbExp=4; IntAct=EBI-773199, EBI-6688774;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:9169128}. Nucleus {ECO:0000250|UniProtKB:P09622}.
CC Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome
CC {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}.
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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; 63.
DR IntAct; O08749; 37.
DR MINT; O08749; -.
DR STRING; 10090.ENSMUSP00000106481; -.
DR ChEMBL; CHEMBL2176826; -.
DR iPTMnet; O08749; -.
DR PhosphoSitePlus; O08749; -.
DR SwissPalm; O08749; -.
DR REPRODUCTION-2DPAGE; O08749; -.
DR SWISS-2DPAGE; O08749; -.
DR CPTAC; non-CPTAC-3704; -.
DR EPD; O08749; -.
DR jPOST; O08749; -.
DR MaxQB; O08749; -.
DR PaxDb; O08749; -.
DR PeptideAtlas; O08749; -.
DR PRIDE; O08749; -.
DR ProteomicsDB; 277461; -.
DR Antibodypedia; 17237; 536 antibodies from 36 providers.
DR DNASU; 13382; -.
DR Ensembl; ENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664.
DR GeneID; 13382; -.
DR KEGG; mmu:13382; -.
DR UCSC; uc007nhg.3; mouse.
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; DAKYGEW; -.
DR OrthoDB; 581771at2759; -.
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 76 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 280 other tissues.
DR Genevisible; O08749; MM.
DR GO; GO:0043159; C:acrosomal matrix; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISO:MGI.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISO: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; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISO:MGI.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISO:MGI.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; ISO:MGI.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
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:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; 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; -; 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 Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
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
