HCDH_MOUSE
ID HCDH_MOUSE Reviewed; 314 AA.
AC Q61425; Q3TF75; Q3THK8; Q3UFI0; Q8K149; Q925U9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial;
DE Short=HCDH;
DE EC=1.1.1.35 {ECO:0000250|UniProtKB:P00348};
DE AltName: Full=Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase {ECO:0000303|Ref.2};
DE AltName: Full=Short-chain 3-hydroxyacyl-CoA dehydrogenase;
DE Flags: Precursor;
GN Name=Hadh; Synonyms=Hadhsc, Mschad, Schad;
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].
RX PubMed=7642117; DOI=10.1016/0378-1119(95)00205-k;
RA Nomura M., Takihara Y., Shimada K.;
RT "Isolation of a cDNA clone encoding mouse 3-hydroxyacyl CoA
RT dehydrogenase.";
RL Gene 160:309-310(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA O'Brien L.K., Sims H.F., Strauss A.W.;
RT "Mouse medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase
RT gene.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Amnion, Extraembryonic tissue, Pancreas, and Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Liver;
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 [5]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP GLUD1.
RX PubMed=20670938; DOI=10.1074/jbc.m110.123638;
RA Li C., Chen P., Palladino A., Narayan S., Russell L.K., Sayed S., Xiong G.,
RA Chen J., Stokes D., Butt Y.M., Jones P.M., Collins H.W., Cohen N.A.,
RA Cohen A.S., Nissim I., Smith T.J., Strauss A.W., Matschinsky F.M.,
RA Bennett M.J., Stanley C.A.;
RT "Mechanism of hyperinsulinism in short-chain 3-hydroxyacyl-CoA
RT dehydrogenase deficiency involves activation of glutamate dehydrogenase.";
RL J. Biol. Chem. 285:31806-31818(2010).
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 AT LYS-81, DESUCCINYLATION BY SIRT5, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-241, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-80;
RP LYS-81; LYS-87; LYS-136; LYS-185; LYS-192; LYS-202; LYS-206; LYS-212;
RP LYS-241 AND LYS-312, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-75; LYS-81; LYS-87; LYS-125;
RP LYS-136; LYS-179; LYS-185; LYS-192; LYS-202; LYS-212 AND LYS-241, AND
RP 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).
CC -!- FUNCTION: Mitochondrial fatty acid beta-oxidation enzyme that catalyzes
CC the third step of the beta-oxidation cycle for medium and short-chain
CC 3-hydroxy fatty acyl-CoAs (C4 to C10) (By similarity). Plays a role in
CC the control of insulin secretion by inhibiting the activation of
CC glutamate dehydrogenase 1 (GLUD1), an enzyme that has an important role
CC in regulating amino acid-induced insulin secretion (PubMed:20670938).
CC {ECO:0000250|UniProtKB:P00348, ECO:0000269|PubMed:20670938}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000250|UniProtKB:P00348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:30799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286,
CC ChEBI:CHEBI:57316, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:P00348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:31187, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62548, ChEBI:CHEBI:62616;
CC Evidence={ECO:0000250|UniProtKB:P00348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA
CC + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:62613; Evidence={ECO:0000250|UniProtKB:P00348};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with GLUD1; this
CC interaction inhibits the activation of glutamate dehydrogenase 1
CC (GLUD1) (PubMed:20670938). {ECO:0000250|UniProtKB:P00348,
CC ECO:0000269|PubMed:20670938}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P00348}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, brain, and pancreatic
CC islets. {ECO:0000269|PubMed:20670938}.
CC -!- PTM: Succinylation at Lys-81, adjacent to a coenzyme A binding site.
CC Desuccinylated by SIRT5. {ECO:0000269|PubMed:23806337}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice display reduced levels of plasma
CC glucose, elevated plasma insulin levels, increased plasma 3-
CC hydroxybutyrylcarnitine and increased urinary 3-hydroxyglutarate.
CC Islets isolated from knockout mice have increased amino acid-stimulated
CC insulin secretion and higher sensitivity to leucine-stimulated insulin
CC secretion. {ECO:0000269|PubMed:20670938}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06122.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D29639; BAA06122.1; ALT_INIT; mRNA.
DR EMBL; AF375597; AAK54642.1; -; Genomic_DNA.
DR EMBL; AF375596; AAK54642.1; JOINED; Genomic_DNA.
DR EMBL; AK132260; BAE21064.1; -; mRNA.
DR EMBL; AK148486; BAE28581.1; -; mRNA.
DR EMBL; AK167024; BAE39197.1; -; mRNA.
DR EMBL; AK168238; BAE40188.1; -; mRNA.
DR EMBL; AK168877; BAE40695.1; -; mRNA.
DR EMBL; AK169261; BAE41023.1; -; mRNA.
DR EMBL; BC028833; AAH28833.1; -; mRNA.
DR EMBL; BC064712; AAH64712.1; -; mRNA.
DR CCDS; CCDS38640.1; -.
DR PIR; JC4210; JC4210.
DR RefSeq; NP_032238.2; NM_008212.4.
DR AlphaFoldDB; Q61425; -.
DR SMR; Q61425; -.
DR BioGRID; 200201; 30.
DR IntAct; Q61425; 3.
DR MINT; Q61425; -.
DR STRING; 10090.ENSMUSP00000029610; -.
DR iPTMnet; Q61425; -.
DR PhosphoSitePlus; Q61425; -.
DR SwissPalm; Q61425; -.
DR REPRODUCTION-2DPAGE; Q61425; -.
DR SWISS-2DPAGE; Q61425; -.
DR EPD; Q61425; -.
DR jPOST; Q61425; -.
DR MaxQB; Q61425; -.
DR PaxDb; Q61425; -.
DR PeptideAtlas; Q61425; -.
DR PRIDE; Q61425; -.
DR ProteomicsDB; 269767; -.
DR Antibodypedia; 26260; 575 antibodies from 34 providers.
DR DNASU; 15107; -.
DR Ensembl; ENSMUST00000029610; ENSMUSP00000029610; ENSMUSG00000027984.
DR GeneID; 15107; -.
DR KEGG; mmu:15107; -.
DR UCSC; uc008rjl.2; mouse.
DR CTD; 3033; -.
DR MGI; MGI:96009; Hadh.
DR VEuPathDB; HostDB:ENSMUSG00000027984; -.
DR eggNOG; KOG2304; Eukaryota.
DR GeneTree; ENSGT00940000159984; -.
DR HOGENOM; CLU_009834_2_0_1; -.
DR InParanoid; Q61425; -.
DR OMA; FYDYSES; -.
DR OrthoDB; 938257at2759; -.
DR PhylomeDB; Q61425; -.
DR TreeFam; TF300886; -.
DR Reactome; R-MMU-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
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 Reactome; R-MMU-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
DR Reactome; R-MMU-77352; Beta oxidation of butanoyl-CoA to acetyl-CoA.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 15107; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Hadh; mouse.
DR PRO; PR:Q61425; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q61425; protein.
DR Bgee; ENSMUSG00000027984; Expressed in paneth cell and 273 other tissues.
DR Genevisible; Q61425; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0050796; P:regulation of insulin secretion; IMP:UniProtKB.
DR GO; GO:0014823; P:response to activity; ISO:MGI.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00067; 3HCDH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Fatty acid metabolism; Hydroxylation; Lipid metabolism;
KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT CHAIN 13..314
FT /note="Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial"
FT /id="PRO_0000007407"
FT BINDING 34..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT BINDING 57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT BINDING 73
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT BINDING 80
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT BINDING 149
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT BINDING 173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT BINDING 305
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT SITE 170
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 80
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 81
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 81
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 87
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 87
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 127
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT MOD_RES 136
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 136
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 185
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 185
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 192
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 192
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 202
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 202
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 206
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 241
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 241
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 312
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16836"
FT MOD_RES 312
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 11
FT /note="S -> Y (in Ref. 3; BAE40188)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="V -> M (in Ref. 3; BAE41023)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="H -> D (in Ref. 1; BAA06122)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="S -> G (in Ref. 3; BAE40188)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="C -> S (in Ref. 1; BAA06122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 34464 MW; 366A4C075F708BC1 CRC64;
MAFVTRQFLR SMSSSSSASA AAKKILIKHV TVIGGGLMGA GIAQVAAATG HTVVLVDQTE
DILAKSKKGI EESLKRMAKK KFTENPKAGD EFVEKTLSCL STSTDAASVV HSTDLVVEAI
VENLKLKNEL FQRLDKFAAE HTIFASNTSS LQITNIANAT TRQDRFAGLH FFNPVPMMKL
VEVIKTPMTS QKTFESLVDF CKTLGKHPVS CKDTPGFIVN RLLVPYLIEA VRLHERGDAS
KEDIDTAMKL GAGYPMGPFE LLDYVGLDTT KFILDGWHEM EPENPLFQPS PSMNNLVAQK
KLGKKTGEGF YKYK
