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Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadm

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

Functioni

Acyl-CoA dehydrogenase specific for acyl chain lengths of 4 to 16 that catalyzes the initial step of fatty acid beta-oxidation. Utilizes the electron transfer flavoprotein (ETF) as an electron acceptor to transfer electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).By similarity

Catalytic activityi

A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

Cofactori

FADBy similarity

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671Substrate; via carbonyl oxygenBy similarity
Active sitei401 – 4011Proton acceptorBy similarity
Binding sitei402 – 4021Substrate; via amide nitrogenBy similarity
Binding sitei413 – 4131SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 16710FADBy similarity
Nucleotide bindingi191 – 1933FADBy similarity
Nucleotide bindingi306 – 3083FADBy similarity
Nucleotide bindingi316 – 3172FADBy similarity
Nucleotide bindingi374 – 3785FADBy similarity
Nucleotide bindingi403 – 4053FADBy similarity

GO - Molecular functioni

GO - Biological processi

  • cardiac muscle cell differentiation Source: MGI
  • carnitine biosynthetic process Source: MGI
  • carnitine metabolic process Source: MGI
  • carnitine metabolic process, CoA-linked Source: BHF-UCL
  • fatty acid beta-oxidation Source: UniProtKB
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: UniProtKB
  • glycogen biosynthetic process Source: BHF-UCL
  • heart development Source: MGI
  • liver development Source: MGI
  • medium-chain fatty acid catabolic process Source: MGI
  • medium-chain fatty acid metabolic process Source: BHF-UCL
  • organic acid metabolic process Source: MGI
  • oxidation-reduction process Source: MGI
  • post-embryonic development Source: MGI
  • protein homotetramerization Source: Ensembl
  • regulation of gluconeogenesis Source: BHF-UCL
  • response to cold Source: MGI
  • response to copper ion Source: Ensembl
  • response to drug Source: Ensembl
  • response to glucocorticoid Source: Ensembl
  • response to nutrient Source: Ensembl
  • response to starvation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
R-MMU-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-MMU-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
UniPathwayiUPA00660.

Names & Taxonomyi

Protein namesi
Recommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.7)
Short name:
MCAD
Gene namesi
Name:Acadm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:87867. Acadm.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionBy similarityAdd
BLAST
Chaini26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301N6-acetyllysine; alternateCombined sources
Modified residuei30 – 301N6-succinyllysine; alternateCombined sources
Modified residuei69 – 691N6-acetyllysine; alternateCombined sources
Modified residuei69 – 691N6-succinyllysine; alternateCombined sources
Modified residuei79 – 791N6-acetyllysineCombined sources
Modified residuei179 – 1791N6-succinyllysineCombined sources
Modified residuei212 – 2121N6-acetyllysine; alternateCombined sources
Modified residuei212 – 2121N6-succinyllysine; alternateCombined sources
Modified residuei217 – 2171N6-acetyllysine; alternateCombined sources
Modified residuei217 – 2171N6-succinyllysine; alternateCombined sources
Modified residuei235 – 2351N6-acetyllysine; alternateCombined sources
Modified residuei235 – 2351N6-succinyllysine; alternateCombined sources
Modified residuei259 – 2591N6-acetyllysine; alternateCombined sources
Modified residuei259 – 2591N6-succinyllysine; alternateCombined sources
Modified residuei271 – 2711N6-acetyllysine; alternateCombined sources
Modified residuei271 – 2711N6-succinyllysine; alternateCombined sources
Modified residuei301 – 3011N6-acetyllysineCombined sources
Modified residuei351 – 3511PhosphothreonineCombined sources

Post-translational modificationi

Acetylation at Lys-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity. These sites are deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP45952.
MaxQBiP45952.
PaxDbiP45952.
PRIDEiP45952.

2D gel databases

SWISS-2DPAGEP45952.

PTM databases

iPTMnetiP45952.
PhosphoSiteiP45952.
SwissPalmiP45952.

Expressioni

Gene expression databases

BgeeiP45952.
CleanExiMM_ACADM.
ExpressionAtlasiP45952. baseline and differential.
GenevisibleiP45952. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP45952. 2 interactions.
MINTiMINT-1860219.
STRINGi10090.ENSMUSP00000072483.

Structurei

3D structure databases

ProteinModelPortaliP45952.
SMRiP45952. Positions 35-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 2814Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0140. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP45952.
KOiK00249.
OMAiSAWEVDQ.
OrthoDBiEOG74FF0S.
PhylomeDBiP45952.
TreeFamiTF105020.

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.

P45952-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAFRRGCR VLRSVSHFEC RTQHSKAAHK QEPGLGFSFE LTEQQKEFQA
60 70 80 90 100
TARKFAREEI IPVAPEYDKS GEYPFPLIKR AWELGLINAH IPESCGGLGL
110 120 130 140 150
GTFDACLITE ELAYGCTGVQ TAIEANSLGQ MPVILAGNDQ QKKKYLGRMT
160 170 180 190 200
EQPMMCAYCV TEPSAGSDVA AIKTKAEKKG DEYVINGQKM WITNGGKANW
210 220 230 240 250
YFLLARSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM GQRCSDTRGI
260 270 280 290 300
AFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT
310 320 330 340 350
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN
360 370 380 390 400
TYYASIAKAF AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY
410 420
EGTAQIQRLI IAREHIEKYK N
Length:421
Mass (Da):46,481
Last modified:November 1, 1995 - v1
Checksum:i36976704E3E48CBB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351L → I in S48759 (PubMed:1438358).Curated
Sequence conflicti184 – 1841V → A in S48761 (PubMed:1438358).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07159 mRNA. Translation: AAA76733.1.
S48761 Genomic DNA. No translation available.
S48759 Genomic DNA. No translation available.
CCDSiCCDS17924.1.
PIRiA55724.
RefSeqiNP_031408.1. NM_007382.5.
UniGeneiMm.10530.

Genome annotation databases

EnsembliENSMUST00000072697; ENSMUSP00000072483; ENSMUSG00000062908.
GeneIDi11364.
KEGGimmu:11364.
UCSCiuc008ruj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07159 mRNA. Translation: AAA76733.1.
S48761 Genomic DNA. No translation available.
S48759 Genomic DNA. No translation available.
CCDSiCCDS17924.1.
PIRiA55724.
RefSeqiNP_031408.1. NM_007382.5.
UniGeneiMm.10530.

3D structure databases

ProteinModelPortaliP45952.
SMRiP45952. Positions 35-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP45952. 2 interactions.
MINTiMINT-1860219.
STRINGi10090.ENSMUSP00000072483.

PTM databases

iPTMnetiP45952.
PhosphoSiteiP45952.
SwissPalmiP45952.

2D gel databases

SWISS-2DPAGEP45952.

Proteomic databases

EPDiP45952.
MaxQBiP45952.
PaxDbiP45952.
PRIDEiP45952.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072697; ENSMUSP00000072483; ENSMUSG00000062908.
GeneIDi11364.
KEGGimmu:11364.
UCSCiuc008ruj.2. mouse.

Organism-specific databases

CTDi34.
MGIiMGI:87867. Acadm.

Phylogenomic databases

eggNOGiKOG0140. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP45952.
KOiK00249.
OMAiSAWEVDQ.
OrthoDBiEOG74FF0S.
PhylomeDBiP45952.
TreeFamiTF105020.

Enzyme and pathway databases

UniPathwayiUPA00660.
ReactomeiR-MMU-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
R-MMU-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-MMU-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.

Miscellaneous databases

PROiP45952.
SOURCEiSearch...

Gene expression databases

BgeeiP45952.
CleanExiMM_ACADM.
ExpressionAtlasiP45952. baseline and differential.
GenevisibleiP45952. MM.

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 characterization of the mouse medium-chain acyl-CoA dehydrogenase cDNA."
    Tolwani R.J., Farmer S.C., Wood P.A.
    Genomics 23:247-249(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Liver.
  2. "Molecular studies of mouse medium and long-chain acyl-CoA dehydrogenase genes for site-directed mutagenesis of embryonic stem cells."
    Wood P.A., Farmer S.C., Tolwani R.J., Warren J.R., Steinkampf M.P., Johnson L.W., Mountz J.D., Kelly D.P.
    Prog. Clin. Biol. Res. 375:151-160(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-193.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "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-30; LYS-69; LYS-179; LYS-212; LYS-217; LYS-235; LYS-259 AND LYS-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "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-30; LYS-69; LYS-79; LYS-212; LYS-217; LYS-235; LYS-259; LYS-271 AND LYS-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACADM_MOUSE
AccessioniPrimary (citable) accession number: P45952
Secondary accession number(s): Q64235
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 153 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, 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.