ACADM_MOUSE
ID ACADM_MOUSE Reviewed; 421 AA.
AC P45952; Q64235;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000305|PubMed:7829081};
DE Short=MCAD {ECO:0000303|PubMed:7829081};
DE EC=1.3.8.7 {ECO:0000269|PubMed:16121256};
DE Flags: Precursor;
GN Name=Acadm {ECO:0000312|MGI:MGI:87867};
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=BALB/cJ; TISSUE=Liver;
RX PubMed=7829081; DOI=10.1006/geno.1994.1486;
RA Tolwani R.J., Farmer S.C., Wood P.A.;
RT "Molecular cloning and characterization of the mouse medium-chain acyl-CoA
RT dehydrogenase cDNA.";
RL Genomics 23:247-249(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-193.
RX PubMed=1438358;
RA Wood P.A., Farmer S.C., Tolwani R.J., Warren J.R., Steinkampf M.P.,
RA Johnson L.W., Mountz J.D., Kelly D.P.;
RT "Molecular studies of mouse medium and long-chain acyl-CoA dehydrogenase
RT genes for site-directed mutagenesis of embryonic stem cells.";
RL Prog. Clin. Biol. Res. 375:151-160(1992).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=16121256; DOI=10.1371/journal.pgen.0010023;
RA Tolwani R.J., Hamm D.A., Tian L., Sharer J.D., Vockley J., Rinaldo P.,
RA Matern D., Schoeb T.R., Wood P.A.;
RT "Medium-chain acyl-CoA dehydrogenase deficiency in gene-targeted mice.";
RL PLoS Genet. 1:e23-e23(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-351, 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 [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-69; LYS-179; LYS-212;
RP LYS-217; LYS-235; LYS-259 AND LYS-271, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-69; LYS-79; LYS-212;
RP LYS-217; LYS-235; LYS-259; LYS-271 AND LYS-301, AND IDENTIFICATION BY MASS
RP 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: Medium-chain specific acyl-CoA dehydrogenase is one of the
CC acyl-CoA dehydrogenases that catalyze the first step of mitochondrial
CC fatty acid beta-oxidation, an aerobic process breaking down fatty acids
CC into acetyl-CoA and allowing the production of energy from fats
CC (PubMed:16121256). The first step of fatty acid beta-oxidation consists
CC in the removal of one hydrogen from C-2 and C-3 of the straight-chain
CC fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-
CC CoA (PubMed:16121256). Electron transfer flavoprotein (ETF) is the
CC electron acceptor that transfers electrons to the main mitochondrial
CC respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase)
CC (By similarity). Among the different mitochondrial acyl-CoA
CC dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts
CC specifically on acyl-CoAs with saturated 6 to 12 carbons long primary
CC chains (PubMed:16121256). {ECO:0000250|UniProtKB:P11310,
CC ECO:0000269|PubMed:16121256}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC ChEBI:CHEBI:83726; EC=1.3.8.7;
CC Evidence={ECO:0000269|PubMed:16121256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14478;
CC Evidence={ECO:0000269|PubMed:16121256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentanoyl-
CC CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:43456, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57389, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:86160;
CC Evidence={ECO:0000250|UniProtKB:P08503};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457;
CC Evidence={ECO:0000250|UniProtKB:P08503};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + octanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-octenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48180, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:62242;
CC Evidence={ECO:0000269|PubMed:16121256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181;
CC Evidence={ECO:0000269|PubMed:16121256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:61406, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61405;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:61526;
CC Evidence={ECO:0000269|PubMed:16121256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC Evidence={ECO:0000269|PubMed:16121256};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:16121256}.
CC -!- SUBUNIT: Homotetramer. Interacts with the heterodimeric electron
CC transfer flavoprotein ETF. {ECO:0000250|UniProtKB:P11310}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P08503}.
CC -!- PTM: Acetylated. Could occur at proximity of the cofactor-binding sites
CC and reduce the catalytic activity. Could be deacetylated by SIRT3.
CC {ECO:0000250|UniProtKB:P11310}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Mcad show increased neonatal
CC mortality (PubMed:16121256). They display hypothermia and cold
CC intolerance upon fasting (PubMed:16121256). Their serum and bile
CC acylcarnitine profile is also different from wild-type mice, with an
CC elevation of serum decenoylcarnitine compared to wild-type mice
CC (PubMed:16121256). They also display hepatic steatosis following fast
CC periods (PubMed:16121256). They develop significantly elevated
CC concentrations of urinary adipic, suberic, and sebacic acids and
CC hexanoylglycine (PubMed:16121256). {ECO:0000269|PubMed:16121256}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {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; U07159; AAA76733.1; -; mRNA.
DR EMBL; S48761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S48759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS17924.1; -.
DR PIR; A55724; A55724.
DR RefSeq; NP_031408.1; NM_007382.5.
DR AlphaFoldDB; P45952; -.
DR SMR; P45952; -.
DR BioGRID; 197912; 24.
DR IntAct; P45952; 6.
DR MINT; P45952; -.
DR STRING; 10090.ENSMUSP00000072483; -.
DR iPTMnet; P45952; -.
DR PhosphoSitePlus; P45952; -.
DR SwissPalm; P45952; -.
DR SWISS-2DPAGE; P45952; -.
DR EPD; P45952; -.
DR jPOST; P45952; -.
DR MaxQB; P45952; -.
DR PaxDb; P45952; -.
DR PeptideAtlas; P45952; -.
DR PRIDE; P45952; -.
DR ProteomicsDB; 296438; -.
DR Antibodypedia; 1642; 468 antibodies from 38 providers.
DR DNASU; 11364; -.
DR Ensembl; ENSMUST00000072697; ENSMUSP00000072483; ENSMUSG00000062908.
DR GeneID; 11364; -.
DR KEGG; mmu:11364; -.
DR UCSC; uc008ruj.2; mouse.
DR CTD; 34; -.
DR MGI; MGI:87867; Acadm.
DR VEuPathDB; HostDB:ENSMUSG00000062908; -.
DR eggNOG; KOG0140; Eukaryota.
DR GeneTree; ENSGT00940000158429; -.
DR HOGENOM; CLU_018204_0_2_1; -.
DR InParanoid; P45952; -.
DR OMA; AMEELFW; -.
DR OrthoDB; 589058at2759; -.
DR PhylomeDB; P45952; -.
DR TreeFam; TF105020; -.
DR Reactome; R-MMU-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR Reactome; R-MMU-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR Reactome; R-MMU-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR UniPathway; UPA00660; -.
DR BioGRID-ORCS; 11364; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Acadm; mouse.
DR PRO; PR:P45952; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P45952; protein.
DR Bgee; ENSMUSG00000062908; Expressed in heart right ventricle and 265 other tissues.
DR ExpressionAtlas; P45952; baseline and differential.
DR Genevisible; P45952; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; ISO:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016853; F:isomerase activity; ISO:MGI.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IMP:BHF-UCL.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR GO; GO:0045329; P:carnitine biosynthetic process; ISO:MGI.
DR GO; GO:0009437; P:carnitine metabolic process; IMP:MGI.
DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IMP:BHF-UCL.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:BHF-UCL.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; ISO:MGI.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; IMP:BHF-UCL.
DR GO; GO:0006082; P:organic acid metabolic process; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IMP:BHF-UCL.
DR GO; GO:0009409; P:response to cold; IMP:MGI.
DR GO; GO:0042594; P:response to starvation; IMP:MGI.
DR CDD; cd01157; MCAD; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR034180; MCAD.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P08503"
FT CHAIN 26..421
FT /note="Medium-chain specific acyl-CoA dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000000504"
FT ACT_SITE 401
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 158..167
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 191..193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 278..281
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 306..308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 316..317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 374..378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 402..405
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT MOD_RES 30
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 30
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 69
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 69
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 179
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 212
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 212
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 217
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 217
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 235
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 235
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 259
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 259
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 271
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 271
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 301
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 135
FT /note="L -> I (in Ref. 2; S48759)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="V -> A (in Ref. 2; S48761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 46481 MW; 36976704E3E48CBB CRC64;
MAAAFRRGCR VLRSVSHFEC RTQHSKAAHK QEPGLGFSFE LTEQQKEFQA TARKFAREEI
IPVAPEYDKS GEYPFPLIKR AWELGLINAH IPESCGGLGL GTFDACLITE ELAYGCTGVQ
TAIEANSLGQ MPVILAGNDQ QKKKYLGRMT EQPMMCAYCV TEPSAGSDVA AIKTKAEKKG
DEYVINGQKM WITNGGKANW YFLLARSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM
GQRCSDTRGI AFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYYASIAKAF
AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIEKYK
N
