ACADV_MOUSE
ID ACADV_MOUSE Reviewed; 656 AA.
AC P50544; O35289; O55133;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Very long-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000305|Ref.1};
DE EC=1.3.8.9 {ECO:0000250|UniProtKB:P49748};
DE AltName: Full=MVLCAD {ECO:0000312|EMBL:CAA94919.2};
DE Short=VLCAD {ECO:0000312|EMBL:CAA94919.2};
DE Flags: Precursor;
GN Name=Acadvl {ECO:0000312|MGI:MGI:895149};
GN Synonyms=Vlcad {ECO:0000312|EMBL:CAA72435.1};
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 [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Blood;
RA Andresen B.S., Lund H., Bross P., Gregersen N.;
RT "Mouse very-long-chain acyl-CoA dehydrogenase (VLCAD) gene.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Heart;
RA Andresen B., Lund H., Bross P., Corydon M., Gregersen N.;
RT "Cloning and characterization of mouse very-long-chain acyl-CoA
RT dehydrogenase.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 84-656.
RC STRAIN=ICR; TISSUE=Liver;
RX PubMed=9680378; DOI=10.1007/s003359900830;
RA Cox K.B., Johnson K.R., Wood P.A.;
RT "Chromosomal locations of the mouse fatty acid oxidation genes Cpt1a,
RT Cpt1b, Cpt2, Acadvl, and metabolically related Crat gene.";
RL Mamm. Genome 9:608-610(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 339-656.
RA Rao G., Krimer D., Krasikov T., Austin C., Skoultchi A.I.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY 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 [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-72; LYS-128; LYS-196; LYS-240;
RP LYS-269; LYS-277; LYS-279; LYS-332; LYS-373; LYS-483; LYS-557 AND LYS-640,
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52; LYS-72; LYS-128; LYS-240;
RP LYS-277; LYS-279; LYS-299; LYS-317; LYS-332; LYS-483; LYS-551 AND LYS-557,
RP AND IDENTIFICATION 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 [9]
RP S-NITROSYLATION AT CYS-238.
RX PubMed=23281369; DOI=10.1126/scisignal.2003252;
RA Doulias P.T., Tenopoulou M., Greene J.L., Raju K., Ischiropoulos H.;
RT "Nitric oxide regulates mitochondrial Fatty Acid metabolism through
RT reversible protein s-nitrosylation.";
RL Sci. Signal. 6:RS1-RS1(2013).
CC -!- FUNCTION: Very long-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. The
CC first step of fatty acid beta-oxidation consists in the removal of one
CC hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA
CC thioester, resulting in the formation of trans-2-enoyl-CoA. Among the
CC different mitochondrial acyl-CoA dehydrogenases, very long-chain
CC specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with
CC saturated 12 to 24 carbons long primary chains.
CC {ECO:0000250|UniProtKB:P49748}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain 2,3-saturated fatty acyl-CoA + H(+) +
CC oxidized [electron-transfer flavoprotein] = a very-long-chain (2E)-
CC enoyl-CoA + reduced [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:19181, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:83724, ChEBI:CHEBI:83728; EC=1.3.8.9;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19182;
CC Evidence={ECO:0000250|UniProtKB:P49748};
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:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297;
CC Evidence={ECO:0000250|UniProtKB:P49748};
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:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC Evidence={ECO:0000250|UniProtKB:P49748};
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:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:71412;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:74691;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:65059, ChEBI:CHEBI:74692;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P49748};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P49748}.
CC -!- SUBUNIT: Homodimer. Homodimerizes after import into the mitochondrion.
CC {ECO:0000250|UniProtKB:P49748}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P49748}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49748}.
CC -!- PTM: S-nitrosylation at Cys-238 in liver improves catalytic efficiency.
CC {ECO:0000269|PubMed:23281369}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Y11770; CAA72435.1; -; Genomic_DNA.
DR EMBL; Z71189; CAA94919.2; -; mRNA.
DR EMBL; BC026559; AAH26559.1; -; mRNA.
DR EMBL; AF017176; AAC31642.1; -; mRNA.
DR EMBL; U41497; AAA85185.1; -; mRNA.
DR CCDS; CCDS24931.1; -.
DR RefSeq; NP_059062.1; NM_017366.3.
DR AlphaFoldDB; P50544; -.
DR SMR; P50544; -.
DR BioGRID; 197914; 28.
DR IntAct; P50544; 2.
DR STRING; 10090.ENSMUSP00000099634; -.
DR iPTMnet; P50544; -.
DR PhosphoSitePlus; P50544; -.
DR SwissPalm; P50544; -.
DR SWISS-2DPAGE; P50544; -.
DR EPD; P50544; -.
DR jPOST; P50544; -.
DR MaxQB; P50544; -.
DR PaxDb; P50544; -.
DR PeptideAtlas; P50544; -.
DR PRIDE; P50544; -.
DR ProteomicsDB; 285633; -.
DR Antibodypedia; 11798; 304 antibodies from 34 providers.
DR DNASU; 11370; -.
DR Ensembl; ENSMUST00000102574; ENSMUSP00000099634; ENSMUSG00000018574.
DR GeneID; 11370; -.
DR KEGG; mmu:11370; -.
DR UCSC; uc007jto.2; mouse.
DR CTD; 37; -.
DR MGI; MGI:895149; Acadvl.
DR VEuPathDB; HostDB:ENSMUSG00000018574; -.
DR eggNOG; KOG0137; Eukaryota.
DR GeneTree; ENSGT00940000158535; -.
DR InParanoid; P50544; -.
DR OMA; NAFMGLR; -.
DR OrthoDB; 819314at2759; -.
DR PhylomeDB; P50544; -.
DR TreeFam; TF105053; -.
DR BRENDA; 1.3.8.9; 3474.
DR Reactome; R-MMU-77305; Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
DR UniPathway; UPA00660; -.
DR BioGRID-ORCS; 11370; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Acadvl; mouse.
DR PRO; PR:P50544; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P50544; protein.
DR Bgee; ENSMUSG00000018574; Expressed in myocardium of ventricle and 248 other tissues.
DR ExpressionAtlas; P50544; baseline and differential.
DR Genevisible; P50544; MM.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO: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; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; ISO:MGI.
DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:BHF-UCL.
DR GO; GO:0009062; P:fatty acid catabolic process; IMP:MGI.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IMP:BHF-UCL.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:BHF-UCL.
DR GO; GO:0009409; P:response to cold; IMP:MGI.
DR GO; GO:0001659; P:temperature homeostasis; IMP:BHF-UCL.
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 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 Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Phosphoprotein; Reference proteome; S-nitrosylation; Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 42..656
FT /note="Very long-chain specific acyl-CoA dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000000517"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..483
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT REGION 484..517
FT /note="Membrane-anchoring"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 463
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT BINDING 215..224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT BINDING 250..252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT BINDING 462..464
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT BINDING 465..467
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT BINDING 563
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 72
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 72
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 128
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 128
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 196
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 238
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:23281369"
FT MOD_RES 240
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 240
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 269
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 277
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 277
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 279
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 279
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 317
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 332
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 332
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 373
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 483
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 483
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT MOD_RES 551
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 557
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 557
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 640
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 339..341
FT /note="NNG -> GTR (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="C -> W (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="A -> G (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="M -> I (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="G -> A (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="R -> P (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="Q -> K (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 570..571
FT /note="AD -> GG (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="A -> P (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="G -> A (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="T -> A (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="A -> P (in Ref. 5; AAA85185)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="H -> Q (in Ref. 4; AAC31642)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 70875 MW; A0110CA5C6CF4F89 CRC64;
MQSARMTPSV GRQLLRLGAR SSRSTTVLQG QPRPISAQRL YAREATQAVL DKPETLSSDA
STREKPARAE SKSFAVGMFK GQLTIDQVFP YPSVLSEEQA QFLKELVGPV ARFFEEVNDP
AKNDALEKVE DDTLQGLKEL GAFGLQVPSE LGGLGLSNTQ YARLAEIVGM HDLGVSVTLG
AHQSIGFKGI LLYGTKAQRE KYLPRVASGQ ALAAFCLTEP SSGSDVASIR SSAIPSPCGK
YYTLNGSKIW ISNGGLADIF TVFAKTPIKD AATGAVKEKI TAFVVERSFG GVTHGLPEKK
MGIKASNTSE VYFDGVKVPS ENVLGEVGDG FKVAVNILNN GRFGMAATLA GTMKSLIAKA
VDHATNRTQF GDKIHNFGVI QEKLARMAIL QYVTESMAYM LSANMDQGFK DFQIEAAISK
IFCSEAAWKV ADECIQIMGG MGFMKEPGVE RVLRDIRIFR IFEGANDILR LFVALQGCMD
KGKELTGLGN ALKNPFGNVG LLMGEAGKQL RRRTGIGSGL SLSGIVHPEL SRSGELAVQA
LDQFATVVEA KLVKHKKGIV NEQFLLQRLA DGAIDLYAMV VVLSRASRSL SEGYPTAQHE
KMLCDSWCIE AATRIRENMA SLQSSPQHQE LFRNFRSISK AMVENGGLVT GNPLGI
