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Protein

Long-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Long-chain-acyl-CoA + electron-transfer flavoprotein = long-chain-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

Cofactori

Pathwayi: mitochondrial fatty acid beta-oxidation

This protein is involved in the pathway mitochondrial fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway mitochondrial fatty acid beta-oxidation and in Lipid metabolism.

GO - Molecular functioni

  • electron carrier activity Source: GO_Central
  • fatty-acyl-CoA binding Source: GO_Central
  • flavin adenine dinucleotide binding Source: GO_Central
  • long-chain-acyl-CoA dehydrogenase activity Source: BHF-UCL
  • oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor Source: GO_Central
  • palmitoyl-CoA oxidase activity Source: BHF-UCL

GO - Biological processi

  • carnitine catabolic process Source: BHF-UCL
  • carnitine metabolic process, CoA-linked Source: BHF-UCL
  • cellular lipid catabolic process Source: BHF-UCL
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: BHF-UCL
  • lipid homeostasis Source: GO_Central
  • long-chain fatty acid catabolic process Source: GO_Central
  • negative regulation of fatty acid biosynthetic process Source: BHF-UCL
  • negative regulation of fatty acid oxidation Source: BHF-UCL
  • oxidation-reduction process Source: BHF-UCL
  • regulation of cholesterol metabolic process Source: BHF-UCL
  • temperature homeostasis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.3.8.8. 3474.
UniPathwayiUPA00660.

Chemistry

SwissLipidsiSLP:000000934.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.8)
Short name:
LCAD
Gene namesi
Name:Acadl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:87866. Acadl.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421K → R: Reduces activity by 90% when associated with R-318 and R-322. 1 Publication
Mutagenesisi318 – 3181K → R: Reduces activity by 37%; reduces activity by 80% when associated with R-322. 1 Publication
Mutagenesisi322 – 3221K → R: Reduces activity by 23%; reduces activity by 80% when associated with R-318. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionBy similarityAdd
BLAST
Chaini31 – 430400Long-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-acetyllysineCombined sources1 Publication
Modified residuei54 – 541PhosphoserineBy similarity
Modified residuei55 – 551PhosphoserineCombined sources
Modified residuei66 – 661N6-acetyllysine; alternateCombined sources
Modified residuei66 – 661N6-succinyllysine; alternateCombined sources
Modified residuei81 – 811N6-acetyllysine; alternateCombined sources
Modified residuei81 – 811N6-succinyllysine; alternateCombined sources
Modified residuei92 – 921N6-acetyllysineCombined sources
Modified residuei95 – 951N6-acetyllysineCombined sources
Modified residuei165 – 1651N6-succinyllysineCombined sources
Modified residuei191 – 1911PhosphoserineCombined sources
Modified residuei240 – 2401N6-succinyllysineCombined sources
Modified residuei254 – 2541N6-acetyllysine; alternateCombined sources
Modified residuei254 – 2541N6-succinyllysine; alternateCombined sources
Modified residuei279 – 2791N6-acetyllysine; alternateCombined sources
Modified residuei279 – 2791N6-succinyllysine; alternateCombined sources
Modified residuei318 – 3181N6-acetyllysine1 Publication
Modified residuei322 – 3221N6-acetyllysine; alternateCombined sources1 Publication
Modified residuei322 – 3221N6-succinyllysine; alternateCombined sources
Modified residuei358 – 3581N6-acetyllysineCombined sources
Modified residuei362 – 3621PhosphoserineCombined sources

Post-translational modificationi

Acetylation at Lys-318 and Lys-322 in proximity of the cofactor-binding sites strongly reduces catalytic activity. These sites are deacetylated by SIRT3.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP51174.
MaxQBiP51174.
PaxDbiP51174.
PeptideAtlasiP51174.
PRIDEiP51174.

PTM databases

iPTMnetiP51174.
PhosphoSiteiP51174.
SwissPalmiP51174.

Expressioni

Gene expression databases

BgeeiP51174.
CleanExiMM_ACADL.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP51174. 3 interactions.
MINTiMINT-1861818.
STRINGi10090.ENSMUSP00000027153.

Structurei

3D structure databases

ProteinModelPortaliP51174.
SMRiP51174. Positions 51-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0141. Eukaryota.
ENOG410XNMY. LUCA.
HOGENOMiHOG000131659.
HOVERGENiHBG104903.
InParanoidiP51174.
KOiK00255.
OrthoDBiEOG77126W.
PhylomeDBiP51174.
TreeFamiTF105054.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51174-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARLLLRSL RVLKARSAPR PPPSARCSHS GAEARLETPS AKKLTDVGIR
60 70 80 90 100
RIFSSEHDIF RESVRKFFQE EVIPHHTEWE KAGEVSREVW EKAGKQGLLG
110 120 130 140 150
INIAEKHGGI GGDLLSTAVT WEEQAYSNCT GPGFSLHSDI VMPYIANYGT
160 170 180 190 200
KEQIEKFIPQ MTAGKCIGAI AMTEPGAGSD LQGVRTNAKR SGSDWILNGS
210 220 230 240 250
KVFITNGWLS DLVIVVAVTN REARSPAHGI SLFLVENGMK GFIKGRKLHK
260 270 280 290 300
MGMKAQDTAE LFFEDVRLPA NALLGEENKG FYYLMQELPQ ERLLIAELAI
310 320 330 340 350
SACEFMFEET RNYVKQRKAF GKTVAHIQTV QHKLAELKTH ICVTRAFVDS
360 370 380 390 400
CLQLHETKRL DSGSASMAKY WASELQNSVA YECVQLHGGW GYMWEYPIAK
410 420 430
AYVDARVQPI YGGTNEIMKE LIARQIVSDS
Length:430
Mass (Da):47,908
Last modified:June 16, 2003 - v2
Checksum:i45CFED51640EAFFB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152KA → RP in AAC52329 (PubMed:8530022).Curated
Sequence conflicti14 – 152KA → RP in AAC23587 (PubMed:9545492).Curated
Sequence conflicti14 – 141K → S in BAB23838 (PubMed:16141072).Curated
Sequence conflicti19 – 202PR → TL in AAC52329 (PubMed:8530022).Curated
Sequence conflicti22 – 221P → L in AAC52329 (PubMed:8530022).Curated
Sequence conflicti22 – 221P → L in BAB23838 (PubMed:16141072).Curated
Sequence conflicti25 – 251A → S in AAC52329 (PubMed:8530022).Curated
Sequence conflicti32 – 321A → P in AAC52329 (PubMed:8530022).Curated
Sequence conflicti35 – 351R → G in AAC52329 (PubMed:8530022).Curated
Sequence conflicti47 – 471V → I in AAC52329 (PubMed:8530022).Curated
Sequence conflicti47 – 471V → I in BAB23838 (PubMed:16141072).Curated
Sequence conflicti58 – 581D → E in BAB31161 (PubMed:16141072).Curated
Sequence conflicti131 – 1322GP → RA in AAC52329 (PubMed:8530022).Curated
Sequence conflicti135 – 1351S → T in AAC52329 (PubMed:8530022).Curated
Sequence conflicti225 – 2251S → W in AAC52329 (PubMed:8530022).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21489 mRNA. Translation: AAC52329.1.
AK005140 mRNA. Translation: BAB23838.1.
AK018319 mRNA. Translation: BAB31161.1.
CU302198 Genomic DNA. Translation: CAQ52312.1.
BC027412 mRNA. Translation: AAH27412.1.
AH006178 Genomic DNA. Translation: AAC23587.1.
CCDSiCCDS15023.1.
RefSeqiNP_031407.2. NM_007381.4.
UniGeneiMm.2445.

Genome annotation databases

GeneIDi11363.
KEGGimmu:11363.
UCSCiuc007bir.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21489 mRNA. Translation: AAC52329.1.
AK005140 mRNA. Translation: BAB23838.1.
AK018319 mRNA. Translation: BAB31161.1.
CU302198 Genomic DNA. Translation: CAQ52312.1.
BC027412 mRNA. Translation: AAH27412.1.
AH006178 Genomic DNA. Translation: AAC23587.1.
CCDSiCCDS15023.1.
RefSeqiNP_031407.2. NM_007381.4.
UniGeneiMm.2445.

3D structure databases

ProteinModelPortaliP51174.
SMRiP51174. Positions 51-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP51174. 3 interactions.
MINTiMINT-1861818.
STRINGi10090.ENSMUSP00000027153.

Chemistry

SwissLipidsiSLP:000000934.

PTM databases

iPTMnetiP51174.
PhosphoSiteiP51174.
SwissPalmiP51174.

Proteomic databases

EPDiP51174.
MaxQBiP51174.
PaxDbiP51174.
PeptideAtlasiP51174.
PRIDEiP51174.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi11363.
KEGGimmu:11363.
UCSCiuc007bir.2. mouse.

Organism-specific databases

CTDi33.
MGIiMGI:87866. Acadl.

Phylogenomic databases

eggNOGiKOG0141. Eukaryota.
ENOG410XNMY. LUCA.
HOGENOMiHOG000131659.
HOVERGENiHBG104903.
InParanoidiP51174.
KOiK00255.
OrthoDBiEOG77126W.
PhylomeDBiP51174.
TreeFamiTF105054.

Enzyme and pathway databases

UniPathwayiUPA00660.
BRENDAi1.3.8.8. 3474.

Miscellaneous databases

ChiTaRSiAcadl. mouse.
PROiP51174.
SOURCEiSearch...

Gene expression databases

BgeeiP51174.
CleanExiMM_ACADL.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RNA expression and chromosomal location of the mouse long-chain acyl-CoA dehydrogenase gene."
    Hinsdale M.E., Farmer S.C., Johnson K.R., Davisson M.T., Hamm D.A., Tolwani R.J., Wood P.A.
    Genomics 28:163-170(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  5. "Structural characterization of the mouse long-chain acyl-CoA dehydrogenase gene and 5' regulatory region."
    Kurtz D.M., Tolwani R.J., Wood P.A.
    Mamm. Genome 9:361-365(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
    Strain: 129/Sv.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-191 AND SER-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "SIRT3 regulates long-chain acyl-coA dehydrogenase by deacetylating conserved lysines near the active site."
    Bharathi S.S., Zhang Y., Mohsen A.W., Uppala R., Balasubramani M., Schreiber E., Uechi G., Beck M.E., Rardin M.J., Vockley J., Verdin E., Gibson B.W., Hirschey M.D., Goetzman E.S.
    J. Biol. Chem. 288:33837-33847(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-42; LYS-318 AND LYS-322, DEACETYLATION BY SIRT3, MUTAGENESIS OF LYS-42; LYS-318 AND LYS-322.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-81; LYS-165; LYS-240; LYS-254; LYS-279 AND LYS-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-66; LYS-81; LYS-92; LYS-95; LYS-254; LYS-279; LYS-322 AND LYS-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACADL_MOUSE
AccessioniPrimary (citable) accession number: P51174
Secondary accession number(s): B2KGC6
, O35302, Q8QZR6, Q9CU29, Q9DB83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 16, 2003
Last modified: July 6, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.