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P45952 (ACADM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Short name=MCAD
EC=1.3.8.7
Gene names
Name:Acadm
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme is specific for acyl chain lengths of 4 to 16.

Catalytic activity

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

Cofactor

FAD By similarity.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Post-translational modification

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.

Miscellaneous

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

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell differentiation

Inferred from mutant phenotype PubMed 16121256. Source: MGI

carnitine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

carnitine metabolic process

Inferred from mutant phenotype PubMed 16121256. Source: MGI

carnitine metabolic process, CoA-linked

Inferred from mutant phenotype PubMed 18459129. Source: BHF-UCL

fatty acid beta-oxidation

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid beta-oxidation using acyl-CoA dehydrogenase

Inferred from mutant phenotype PubMed 18459129. Source: BHF-UCL

glycogen biosynthetic process

Inferred from mutant phenotype PubMed 18459129. Source: BHF-UCL

heart development

Inferred from mutant phenotype PubMed 16121256. Source: MGI

liver development

Inferred from mutant phenotype PubMed 16121256. Source: MGI

medium-chain fatty acid catabolic process

Inferred from electronic annotation. Source: Ensembl

medium-chain fatty acid metabolic process

Inferred from mutant phenotype PubMed 18459129. Source: BHF-UCL

organic acid metabolic process

Inferred from mutant phenotype PubMed 16121256. Source: MGI

post-embryonic development

Inferred from mutant phenotype PubMed 16121256. Source: MGI

regulation of gluconeogenesis

Inferred from mutant phenotype PubMed 18459129. Source: BHF-UCL

response to cold

Inferred from mutant phenotype PubMed 16121256. Source: MGI

response to starvation

Inferred from mutant phenotype PubMed 16121256. Source: MGI

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

   Molecular_functionacyl-CoA dehydrogenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

medium-chain-acyl-CoA dehydrogenase activity

Inferred from mutant phenotype PubMed 18459129. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion By similarity
Chain26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000504

Regions

Nucleotide binding158 – 16710FAD By similarity
Nucleotide binding191 – 1933FAD By similarity
Nucleotide binding306 – 3083FAD By similarity
Nucleotide binding316 – 3172FAD By similarity
Nucleotide binding374 – 3785FAD By similarity
Nucleotide binding403 – 4053FAD By similarity
Region278 – 2814Substrate binding By similarity

Sites

Active site4011Proton acceptor By similarity
Binding site1671Substrate; via carbonyl oxygen By similarity
Binding site4021Substrate; via amide nitrogen By similarity
Binding site4131Substrate By similarity

Amino acid modifications

Modified residue301N6-acetyllysine; alternate Ref.4
Modified residue301N6-succinyllysine; alternate Ref.3
Modified residue691N6-acetyllysine; alternate Ref.4
Modified residue691N6-succinyllysine; alternate Ref.3
Modified residue791N6-acetyllysine Ref.4
Modified residue1791N6-succinyllysine Ref.3
Modified residue2121N6-acetyllysine; alternate Ref.4
Modified residue2121N6-succinyllysine; alternate Ref.3
Modified residue2171N6-acetyllysine; alternate Ref.4
Modified residue2171N6-succinyllysine; alternate Ref.3
Modified residue2351N6-acetyllysine; alternate Ref.4
Modified residue2351N6-succinyllysine; alternate Ref.3
Modified residue2591N6-acetyllysine; alternate Ref.4
Modified residue2591N6-succinyllysine; alternate Ref.3
Modified residue2711N6-acetyllysine; alternate Ref.4
Modified residue2711N6-succinyllysine; alternate Ref.3
Modified residue3011N6-acetyllysine Ref.4

Experimental info

Sequence conflict1351L → I in S48759. Ref.2
Sequence conflict1841V → A in S48761. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P45952 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 36976704E3E48CBB

FASTA42146,481
        10         20         30         40         50         60 
MAAAFRRGCR VLRSVSHFEC RTQHSKAAHK QEPGLGFSFE LTEQQKEFQA TARKFAREEI 

        70         80         90        100        110        120 
IPVAPEYDKS GEYPFPLIKR AWELGLINAH IPESCGGLGL GTFDACLITE ELAYGCTGVQ 

       130        140        150        160        170        180 
TAIEANSLGQ MPVILAGNDQ QKKKYLGRMT EQPMMCAYCV TEPSAGSDVA AIKTKAEKKG 

       190        200        210        220        230        240 
DEYVINGQKM WITNGGKANW YFLLARSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM 

       250        260        270        280        290        300 
GQRCSDTRGI AFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT 

       310        320        330        340        350        360 
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYYASIAKAF 

       370        380        390        400        410        420 
AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIEKYK 


N 

« Hide

References

« Hide 'large scale' references
[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/c.
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]"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.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07159 mRNA. Translation: AAA76733.1.
S48761 Genomic DNA. No translation available.
S48759 Genomic DNA. No translation available.
PIRA55724.
RefSeqNP_031408.1. NM_007382.5.
UniGeneMm.10530.

3D structure databases

ProteinModelPortalP45952.
SMRP45952. Positions 35-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP45952. 2 interactions.
MINTMINT-1860219.

PTM databases

PhosphoSiteP45952.

2D gel databases

SWISS-2DPAGEP45952.

Proteomic databases

PaxDbP45952.
PRIDEP45952.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072697; ENSMUSP00000072483; ENSMUSG00000062908.
GeneID11364.
KEGGmmu:11364.
UCSCuc008ruj.1. mouse.

Organism-specific databases

CTD34.
MGIMGI:87867. Acadm.

Phylogenomic databases

eggNOGCOG1960.
GeneTreeENSGT00750000117417.
HOGENOMHOG000131659.
HOVERGENHBG000224.
InParanoidP45952.
KOK00249.
OMAIAMGTFD.
OrthoDBEOG74FF0S.
PhylomeDBP45952.
TreeFamTF105020.

Enzyme and pathway databases

UniPathwayUPA00660.

Gene expression databases

ArrayExpressP45952.
BgeeP45952.
CleanExMM_ACADM.
GenevestigatorP45952.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR006089. 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]
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio278640.
PROP45952.
SOURCESearch...

Entry information

Entry nameACADM_MOUSE
AccessionPrimary (citable) accession number: P45952
Secondary accession number(s): Q64235
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot