ACADL_MOUSE
ID ACADL_MOUSE Reviewed; 430 AA.
AC P51174; B2KGC6; O35302; Q8QZR6; Q9CU29; Q9DB83;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Long-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE Short=LCAD;
DE EC=1.3.8.8 {ECO:0000269|PubMed:9861014};
DE Flags: Precursor;
GN Name=Acadl {ECO:0000312|MGI:MGI:87866};
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=8530022; DOI=10.1006/geno.1995.1127;
RA Hinsdale M.E., Farmer S.C., Johnson K.R., Davisson M.T., Hamm D.A.,
RA Tolwani R.J., Wood P.A.;
RT "RNA expression and chromosomal location of the mouse long-chain acyl-CoA
RT dehydrogenase gene.";
RL Genomics 28:163-170(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
RC STRAIN=129/Sv;
RX PubMed=9545492; DOI=10.1007/s003359900770;
RA Kurtz D.M., Tolwani R.J., Wood P.A.;
RT "Structural characterization of the mouse long-chain acyl-CoA dehydrogenase
RT gene and 5' regulatory region.";
RL Mamm. Genome 9:361-365(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=9861014; DOI=10.1073/pnas.95.26.15592;
RA Kurtz D.M., Rinaldo P., Rhead W.J., Tian L., Millington D.S., Vockley J.,
RA Hamm D.A., Brix A.E., Lindsey J.R., Pinkert C.A., O'Brien W.E., Wood P.A.;
RT "Targeted disruption of mouse long-chain acyl-CoA dehydrogenase gene
RT reveals crucial roles for fatty acid oxidation.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15592-15597(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-191 AND SER-362, AND
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 [8]
RP ACETYLATION AT LYS-42; LYS-318 AND LYS-322, DEACETYLATION BY SIRT3, AND
RP MUTAGENESIS OF LYS-42; LYS-318 AND LYS-322.
RX PubMed=24121500; DOI=10.1074/jbc.m113.510354;
RA Bharathi S.S., Zhang Y., Mohsen A.W., Uppala R., Balasubramani M.,
RA Schreiber E., Uechi G., Beck M.E., Rardin M.J., Vockley J., Verdin E.,
RA Gibson B.W., Hirschey M.D., Goetzman E.S.;
RT "SIRT3 regulates long-chain acyl-coA dehydrogenase by deacetylating
RT conserved lysines near the active site.";
RL J. Biol. Chem. 288:33837-33847(2013).
RN [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-81; LYS-165; LYS-240;
RP LYS-254; LYS-279 AND LYS-322, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-66; LYS-81; LYS-92;
RP LYS-95; LYS-254; LYS-279; LYS-322 AND LYS-358, 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: 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 (By
CC similarity). Among the different mitochondrial acyl-CoA dehydrogenases,
CC long-chain specific acyl-CoA dehydrogenase can act on saturated and
CC unsaturated acyl-CoAs with 6 to 24 carbons with a preference for 8 to
CC 18 carbons long primary chains (PubMed:9861014).
CC {ECO:0000250|UniProtKB:P15650, ECO:0000269|PubMed:9861014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC ChEBI:CHEBI:83727; EC=1.3.8.8; Evidence={ECO:0000269|PubMed:9861014};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17722;
CC Evidence={ECO:0000269|PubMed:9861014};
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:9861014};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC Evidence={ECO:0000269|PubMed:9861014};
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:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC Evidence={ECO:0000250|UniProtKB:P28330};
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:0000250|UniProtKB:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181;
CC Evidence={ECO:0000250|UniProtKB:P28330};
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:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177;
CC Evidence={ECO:0000250|UniProtKB:P28330};
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:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297;
CC Evidence={ECO:0000250|UniProtKB:P28330};
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:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC Evidence={ECO:0000250|UniProtKB:P28330};
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:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241;
CC Evidence={ECO:0000250|UniProtKB:P28330};
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:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC Evidence={ECO:0000250|UniProtKB:P28330};
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:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229;
CC Evidence={ECO:0000250|UniProtKB:P28330};
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:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233;
CC Evidence={ECO:0000250|UniProtKB:P28330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5E)-tetradecenoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E,5E)-tetradecadienoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:49828, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:131943, ChEBI:CHEBI:131944;
CC Evidence={ECO:0000250|UniProtKB:P15650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49829;
CC Evidence={ECO:0000250|UniProtKB:P15650};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z)-tetradecenoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E,5Z)-tetradecadienoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47448, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:84650, ChEBI:CHEBI:87701;
CC Evidence={ECO:0000250|UniProtKB:P15650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47449;
CC Evidence={ECO:0000250|UniProtKB:P15650};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E,9Z)-octadecadienoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47300, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77553;
CC Evidence={ECO:0000250|UniProtKB:P15650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47301;
CC Evidence={ECO:0000250|UniProtKB:P15650};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P15650};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:9861014}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P15650}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P15650}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, kidney, and
CC brain (PubMed:9861014). Expressed in liver (at protein level)
CC (PubMed:9861014). {ECO:0000269|PubMed:9861014}.
CC -!- PTM: Acetylation at Lys-318 and Lys-322 in proximity of the cofactor-
CC binding sites strongly reduces catalytic activity. These sites are
CC deacetylated by SIRT3. {ECO:0000269|PubMed:24121500}.
CC -!- DISRUPTION PHENOTYPE: Acadl deficiency results in significant
CC gestational loss of embryos (PubMed:9861014). Homozygous knockout mice
CC that achieve birth display severe fasting intolerance with subsequent
CC hepatic and cardiac lipidosis, hypoglycemia, elevated serum free fatty
CC acids, non-ketotic dicarboxylic aciduria, and myocardial degeneration
CC (PubMed:9861014). {ECO:0000269|PubMed:9861014}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U21489; AAC52329.1; -; mRNA.
DR EMBL; AK005140; BAB23838.1; -; mRNA.
DR EMBL; AK018319; BAB31161.1; -; mRNA.
DR EMBL; CU302198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027412; AAH27412.1; -; mRNA.
DR EMBL; AH006178; AAC23587.1; -; Genomic_DNA.
DR CCDS; CCDS15023.1; -.
DR RefSeq; NP_031407.2; NM_007381.4.
DR AlphaFoldDB; P51174; -.
DR SMR; P51174; -.
DR BioGRID; 197911; 20.
DR IntAct; P51174; 6.
DR MINT; P51174; -.
DR STRING; 10090.ENSMUSP00000027153; -.
DR SwissLipids; SLP:000000934; -.
DR iPTMnet; P51174; -.
DR PhosphoSitePlus; P51174; -.
DR SwissPalm; P51174; -.
DR EPD; P51174; -.
DR jPOST; P51174; -.
DR MaxQB; P51174; -.
DR PaxDb; P51174; -.
DR PeptideAtlas; P51174; -.
DR PRIDE; P51174; -.
DR ProteomicsDB; 285831; -.
DR DNASU; 11363; -.
DR GeneID; 11363; -.
DR KEGG; mmu:11363; -.
DR UCSC; uc007bir.2; mouse.
DR CTD; 33; -.
DR MGI; MGI:87866; Acadl.
DR eggNOG; KOG0141; Eukaryota.
DR InParanoid; P51174; -.
DR OrthoDB; 589058at2759; -.
DR PhylomeDB; P51174; -.
DR TreeFam; TF105054; -.
DR BRENDA; 1.3.8.8; 3474.
DR Reactome; R-MMU-77285; Beta oxidation of myristoyl-CoA to lauroyl-CoA.
DR Reactome; R-MMU-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
DR UniPathway; UPA00660; -.
DR BioGRID-ORCS; 11363; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Acadl; mouse.
DR PRO; PR:P51174; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P51174; protein.
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; IBA:GO_Central.
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:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IMP:BHF-UCL.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IMP:BHF-UCL.
DR GO; GO:0042413; P:carnitine catabolic process; IMP:BHF-UCL.
DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IMP:BHF-UCL.
DR GO; GO:0044242; P:cellular lipid catabolic process; IMP:BHF-UCL.
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:0042758; P:long-chain fatty acid catabolic process; ISO: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:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
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 CDD; cd01160; LCAD; 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; IPR034179; LCAD.
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..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P15650"
FT CHAIN 31..430
FT /note="Long-chain specific acyl-CoA dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000000511"
FT REGION 17..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 291
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 170..179
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 203..205
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 227..228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 289..292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 328
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 385..389
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 412..413
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 414..416
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:24121500,
FT ECO:0007744|PubMed:23576753"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15650"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 66
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 66
FT /note="N6-succinyllysine; alternate"
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 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 165
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 240
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 254
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 254
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 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:24121500"
FT MOD_RES 322
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24121500,
FT ECO:0007744|PubMed:23576753"
FT MOD_RES 322
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 358
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 42
FT /note="K->R: Reduces activity by 90% when associated with
FT R-318 and R-322."
FT /evidence="ECO:0000269|PubMed:24121500"
FT MUTAGEN 318
FT /note="K->R: Reduces activity by 37%; reduces activity by
FT 80% when associated with R-322."
FT /evidence="ECO:0000269|PubMed:24121500"
FT MUTAGEN 322
FT /note="K->R: Reduces activity by 23%; reduces activity by
FT 80% when associated with R-318."
FT /evidence="ECO:0000269|PubMed:24121500"
FT CONFLICT 14..15
FT /note="KA -> RP (in Ref. 1; AAC52329 and 5; AAC23587)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="K -> S (in Ref. 2; BAB23838)"
FT /evidence="ECO:0000305"
FT CONFLICT 19..20
FT /note="PR -> TL (in Ref. 1; AAC52329)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="P -> L (in Ref. 1; AAC52329 and 2; BAB23838)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="A -> S (in Ref. 1; AAC52329)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="A -> P (in Ref. 1; AAC52329)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="R -> G (in Ref. 1; AAC52329)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="V -> I (in Ref. 1; AAC52329 and 2; BAB23838)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="D -> E (in Ref. 2; BAB31161)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..132
FT /note="GP -> RA (in Ref. 1; AAC52329)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="S -> T (in Ref. 1; AAC52329)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="S -> W (in Ref. 1; AAC52329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47908 MW; 45CFED51640EAFFB CRC64;
MAARLLLRSL RVLKARSAPR PPPSARCSHS GAEARLETPS AKKLTDVGIR RIFSSEHDIF
RESVRKFFQE EVIPHHTEWE KAGEVSREVW EKAGKQGLLG INIAEKHGGI GGDLLSTAVT
WEEQAYSNCT GPGFSLHSDI VMPYIANYGT KEQIEKFIPQ MTAGKCIGAI AMTEPGAGSD
LQGVRTNAKR SGSDWILNGS KVFITNGWLS DLVIVVAVTN REARSPAHGI SLFLVENGMK
GFIKGRKLHK MGMKAQDTAE LFFEDVRLPA NALLGEENKG FYYLMQELPQ ERLLIAELAI
SACEFMFEET RNYVKQRKAF GKTVAHIQTV QHKLAELKTH ICVTRAFVDS CLQLHETKRL
DSGSASMAKY WASELQNSVA YECVQLHGGW GYMWEYPIAK AYVDARVQPI YGGTNEIMKE
LIARQIVSDS
