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P08503 (ACADM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

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
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid beta-oxidation using acyl-CoA dehydrogenase

Inferred from direct assay PubMed 3968063. Source: RGD

medium-chain fatty acid catabolic process

Inferred from direct assay PubMed 3968063. Source: RGD

protein homotetramerization

Inferred from direct assay PubMed 3968063. Source: RGD

response to copper ion

Inferred from expression pattern PubMed 10958805. Source: RGD

response to drug

Inferred from expression pattern PubMed 15852996. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 8615829. Source: RGD

response to hormone

Inferred from expression pattern PubMed 9164869. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 15863369. Source: RGD

   Cellular_componentmitochondrial matrix

Inferred from direct assay PubMed 3813556. Source: BHF-UCL

mitochondrial membrane

Inferred from direct assay PubMed 3813556. Source: BHF-UCL

mitochondrion

Inferred from direct assay PubMed 3968063. Source: RGD

   Molecular_functionacyl-CoA dehydrogenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

fatty-acyl-CoA binding

Inferred from direct assay PubMed 3968063. Source: RGD

flavin adenine dinucleotide binding

Inferred from direct assay PubMed 3968063. Source: RGD

identical protein binding

Inferred from direct assay PubMed 3813556. Source: BHF-UCL

isomerase activity

Inferred from direct assay PubMed 15850406. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion
Chain26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000506

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 residue691N6-acetyllysine; alternate By similarity
Modified residue691N6-succinyllysine; alternate By similarity
Modified residue791N6-acetyllysine By similarity
Modified residue1791N6-succinyllysine By similarity
Modified residue2121N6-acetyllysine; alternate By similarity
Modified residue2121N6-succinyllysine; alternate By similarity
Modified residue2171N6-acetyllysine; alternate By similarity
Modified residue2171N6-succinyllysine; alternate By similarity
Modified residue2591N6-acetyllysine; alternate By similarity
Modified residue2591N6-succinyllysine; alternate By similarity
Modified residue2711N6-acetyllysine; alternate By similarity
Modified residue2711N6-succinyllysine; alternate By similarity
Modified residue3011N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P08503 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 2CF076F8C919BDE8

FASTA42146,555
        10         20         30         40         50         60 
MAAALRRGYK VLRSVSHFEC RAQHTKPSLK QEPGLGFSFE LTEQQKEFQT IARKFAREEI 

        70         80         90        100        110        120 
IPVAPDYDKS GEYPFPLIKR AWELGLINTH IPESCGGLGL GTFDACLITE ELAYGCTGVQ 

       130        140        150        160        170        180 
TAIEANSLGQ MPVIIAGNDQ QKKKYLGRMT EQPMMCAYCV TEPSAGSDVA GIKTKAEKKG 

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

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

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

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


N 

« Hide

References

[1]"Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat liver medium chain acyl coenzyme A dehydrogenase."
Matsubara Y., Kraus J.P., Ozasa H., Glassberg R., Finocchiaro G., Ikeda Y., Mole J., Rosenberg L.E., Tanaka K.
J. Biol. Chem. 262:10104-10108(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Structurally different rat liver medium-chain acyl CoA dehydrogenases directed by complementary DNAs differing in their 5'-region."
Inagaki T., Ohishi N., Tsukagoshi N., Udaka S., Ghisla S., Yagi K.
Biochim. Biophys. Acta 1077:285-290(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 11-81.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02791 mRNA. Translation: AAA40670.1.
PIRDERTCM. A28436.
RefSeqNP_058682.2. NM_016986.2.
UniGeneRn.6302.

3D structure databases

ProteinModelPortalP08503.
SMRP08503. Positions 34-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08503. 1 interaction.
STRING10116.ENSRNOP00000013238.

Chemistry

ChEMBLCHEMBL2176828.

Proteomic databases

PaxDbP08503.
PRIDEP08503.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24158.
KEGGrno:24158.

Organism-specific databases

CTD34.
RGD2012. Acadm.

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000131659.
HOVERGENHBG000224.
InParanoidP08503.
KOK00249.
PhylomeDBP08503.

Enzyme and pathway databases

SABIO-RKP08503.
UniPathwayUPA00660.

Gene expression databases

GenevestigatorP08503.

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

NextBio602449.
PROP08503.

Entry information

Entry nameACADM_RAT
AccessionPrimary (citable) accession number: P08503
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 128 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