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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
  • fatty acid catabolic process Source: MGI
  • 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
  • response to cold Source: MGI
  • 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 databases

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)DescriptionActionsGraphical viewLength
Mutagenesisi42K → R: Reduces activity by 90% when associated with R-318 and R-322. 1 Publication1
Mutagenesisi318K → R: Reduces activity by 37%; reduces activity by 80% when associated with R-322. 1 Publication1
Mutagenesisi322K → R: Reduces activity by 23%; reduces activity by 80% when associated with R-318. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30MitochondrionBy similarityAdd BLAST30
ChainiPRO_000000051131 – 430Long-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42N6-acetyllysineCombined sources1 Publication1
Modified residuei54PhosphoserineBy similarity1
Modified residuei55PhosphoserineCombined sources1
Modified residuei66N6-acetyllysine; alternateCombined sources1
Modified residuei66N6-succinyllysine; alternateCombined sources1
Modified residuei81N6-acetyllysine; alternateCombined sources1
Modified residuei81N6-succinyllysine; alternateCombined sources1
Modified residuei92N6-acetyllysineCombined sources1
Modified residuei95N6-acetyllysineCombined sources1
Modified residuei165N6-succinyllysineCombined sources1
Modified residuei191PhosphoserineCombined sources1
Modified residuei240N6-succinyllysineCombined sources1
Modified residuei254N6-acetyllysine; alternateCombined sources1
Modified residuei254N6-succinyllysine; alternateCombined sources1
Modified residuei279N6-acetyllysine; alternateCombined sources1
Modified residuei279N6-succinyllysine; alternateCombined sources1
Modified residuei318N6-acetyllysine1 Publication1
Modified residuei322N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei322N6-succinyllysine; alternateCombined sources1
Modified residuei358N6-acetyllysineCombined sources1
Modified residuei362PhosphoserineCombined sources1

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.
PhosphoSitePlusiP51174.
SwissPalmiP51174.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026003.
CleanExiMM_ACADL.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi197911. 1 interactor.
IntActiP51174. 3 interactors.
MINTiMINT-1861818.
STRINGi10090.ENSMUSP00000027153.

Structurei

3D structure databases

ProteinModelPortaliP51174.
SMRiP51174.
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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti14 – 15KA → RP in AAC52329 (PubMed:8530022).Curated2
Sequence conflicti14 – 15KA → RP in AAC23587 (PubMed:9545492).Curated2
Sequence conflicti14K → S in BAB23838 (PubMed:16141072).Curated1
Sequence conflicti19 – 20PR → TL in AAC52329 (PubMed:8530022).Curated2
Sequence conflicti22P → L in AAC52329 (PubMed:8530022).Curated1
Sequence conflicti22P → L in BAB23838 (PubMed:16141072).Curated1
Sequence conflicti25A → S in AAC52329 (PubMed:8530022).Curated1
Sequence conflicti32A → P in AAC52329 (PubMed:8530022).Curated1
Sequence conflicti35R → G in AAC52329 (PubMed:8530022).Curated1
Sequence conflicti47V → I in AAC52329 (PubMed:8530022).Curated1
Sequence conflicti47V → I in BAB23838 (PubMed:16141072).Curated1
Sequence conflicti58D → E in BAB31161 (PubMed:16141072).Curated1
Sequence conflicti131 – 132GP → RA in AAC52329 (PubMed:8530022).Curated2
Sequence conflicti135S → T in AAC52329 (PubMed:8530022).Curated1
Sequence conflicti225S → W in AAC52329 (PubMed:8530022).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197911. 1 interactor.
IntActiP51174. 3 interactors.
MINTiMINT-1861818.
STRINGi10090.ENSMUSP00000027153.

Chemistry databases

SwissLipidsiSLP:000000934.

PTM databases

iPTMnetiP51174.
PhosphoSitePlusiP51174.
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.
PhylomeDBiP51174.
TreeFamiTF105054.

Enzyme and pathway databases

UniPathwayiUPA00660.
BRENDAi1.3.8.8. 3474.

Miscellaneous databases

ChiTaRSiAcadl. mouse.
PROiP51174.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026003.
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...

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: November 2, 2016
This is version 152 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.