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Protein

Long-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadl

Organism
Rattus norvegicus (Rat)
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

GO - Biological processi

  • carnitine metabolic process, CoA-linked Source: GO_Central
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: RGD
  • lipid homeostasis Source: GO_Central
  • long-chain fatty acid catabolic process Source: RGD
  • protein homotetramerization Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-RNO-77285. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
R-RNO-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
SABIO-RKP15650.
UniPathwayiUPA00660.

Chemistry

SwissLipidsiSLP:000001586.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi2011. Acadl.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: BHF-UCL
  • mitochondrial membrane Source: BHF-UCL
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2176836.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionAdd
BLAST
Chaini31 – 430400Long-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000513Add
BLAST

Amino acid modifications

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

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP15650.
PRIDEiP15650.

PTM databases

iPTMnetiP15650.
PhosphoSiteiP15650.

Expressioni

Gene expression databases

GenevisibleiP15650. RN.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi247326. 1 interaction.
IntActiP15650. 1 interaction.
STRINGi10116.ENSRNOP00000017686.

Structurei

3D structure databases

ProteinModelPortaliP15650.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0141. Eukaryota.
ENOG410XNMY. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG104903.
InParanoidiP15650.
KOiK00255.
OMAiKAGEAGM.
OrthoDBiEOG77126W.
PhylomeDBiP15650.
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.

P15650-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARLLLRSL RVLSARSATL PPPSARCSHS GAEARLETPS AKKLTDIGIR
60 70 80 90 100
RIFSSEHDIF RESVRKFFQE EVIPYHEEWE KAGEVSRELW EKAGKQGLLG
110 120 130 140 150
INIAEKHGGI GGDLLSTAVT WEEQAYSNCT GPGFSLHSDI VMPYIANYGT
160 170 180 190 200
KEQIEQFIPQ MTAGKCIGAI AMTEPGAGSD LQGVRTNAKR SGSDWILNGS
210 220 230 240 250
KVFITNGWLS DLVIVVAVTN REARSPAHGI SLFLVENGMK GFIKGKKLHK
260 270 280 290 300
MGMKAQDTAE LFFEDVRLPA SALLGEENKG FYYLMQELPQ ERLLIADLAI
310 320 330 340 350
SACEFMFEET RNYVRQRKAF GKTVAHIQTV QHKLAELKTN ICVTRAFVDS
360 370 380 390 400
CLQLHETKRL DSASASMAKY WASELQNTVA YQCVQLHGGW GYMWEYPIAK
410 420 430
AYVDARVQPI YGGTNEIMKE LIARQIVSDS
Length:430
Mass (Da):47,873
Last modified:April 1, 1990 - v1
Checksum:iBEE1C7E0FDD84D2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05029 mRNA. Translation: AAA40668.1.
L11276 mRNA. Translation: AAA41514.1.
BC062006 mRNA. Translation: AAH62006.1.
PIRiA34252.
RefSeqiNP_036951.1. NM_012819.1.
UniGeneiRn.174.

Genome annotation databases

EnsembliENSRNOT00000017686; ENSRNOP00000017686; ENSRNOG00000012966.
GeneIDi25287.
KEGGirno:25287.
UCSCiRGD:2011. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05029 mRNA. Translation: AAA40668.1.
L11276 mRNA. Translation: AAA41514.1.
BC062006 mRNA. Translation: AAH62006.1.
PIRiA34252.
RefSeqiNP_036951.1. NM_012819.1.
UniGeneiRn.174.

3D structure databases

ProteinModelPortaliP15650.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247326. 1 interaction.
IntActiP15650. 1 interaction.
STRINGi10116.ENSRNOP00000017686.

Chemistry

ChEMBLiCHEMBL2176836.
SwissLipidsiSLP:000001586.

PTM databases

iPTMnetiP15650.
PhosphoSiteiP15650.

Proteomic databases

PaxDbiP15650.
PRIDEiP15650.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017686; ENSRNOP00000017686; ENSRNOG00000012966.
GeneIDi25287.
KEGGirno:25287.
UCSCiRGD:2011. rat.

Organism-specific databases

CTDi33.
RGDi2011. Acadl.

Phylogenomic databases

eggNOGiKOG0141. Eukaryota.
ENOG410XNMY. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG104903.
InParanoidiP15650.
KOiK00255.
OMAiKAGEAGM.
OrthoDBiEOG77126W.
PhylomeDBiP15650.
TreeFamiTF105054.

Enzyme and pathway databases

UniPathwayiUPA00660.
ReactomeiR-RNO-77285. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
R-RNO-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
SABIO-RKP15650.

Miscellaneous databases

PROiP15650.

Gene expression databases

GenevisibleiP15650. RN.

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. "Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family."
    Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K.
    J. Biol. Chem. 264:16321-16331(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Tissue specific and developmental expression of rat long- and medium-chain acyl-CoA dehydrogenases."
    Hainline B.E., Kahlenbeck D.J., Grant J., Strauss A.W.
    Biochim. Biophys. Acta 1216:460-468(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Aorta.
  3. "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: Prostate.
  4. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 52-61 AND 255-267, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACADL_RAT
AccessioniPrimary (citable) accession number: P15650
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 6, 2016
This is version 142 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.