Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P08503 (ACADM_RAT)

Last modified January 19, 2010. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=MCAD
    EC=1.3.99.3
Gene names
Name: Acadm
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Hide | Top

Protein attributes

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

Hide | Top

General annotation (Comments)

Function

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

Catalytic activity

Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.

Cofactor

FAD.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

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.

Hide | Top

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 residue2121N6-acetyllysine By similarity
Modified residue3011N6-acetyllysine By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P08503-1 [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

Hide | Top

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: 3611054] [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: 2029527] [Abstract]
Cited for: PROTEIN SEQUENCE OF 11-81.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J02791 mRNA. Translation: AAA40670.1.
IPIIPI00212015.
PIRDERTCM. A28436.
RefSeqNP_058682.1.
UniGeneRn.6302

3D structure databases

SMRP08503. Positions 34-421.
ModBaseSearch...

Protein-protein interaction databases

STRINGP08503.

Proteomic databases

PRIDEP08503.

Genome annotation databases

EnsemblENSRNOT00000013238; ENSRNOP00000013238; ENSRNOG00000009845; Rattus norvegicus. [Genome view]
GeneID24158.
KEGGrno:24158.
UCSCNM_016986. rat.

Organism-specific databases

CTD24158.
RGD2012. Acadm.

Phylogenomic databases

eggNOGroNOG13445.
HOVERGENP08503.
InParanoidP08503.

Enzyme and pathway databases

BRENDA1.3.99.3. 248.

Gene expression databases

ArrayExpressP08503.
GenevestigatorP08503.
GermOnlineENSRNOG00000009845. Rattus norvegicus.

Family and domain databases

InterProIPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio602449.

Hide | Top

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: January 19, 2010
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents