P08503 (ACADM_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Short name=MCAD
EC=1.3.8.7

Gene names

Name:

Acadm

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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 process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 stimulus Inferred from expression pattern PubMed 8615829. Source: RGD response to nutrient Inferred from expression pattern PubMed 15863369. Source: RGD
Cellular_component	mitochondrial matrix Inferred from direct assay PubMed 3813556. Source: BHF-UCL mitochondrial membrane Inferred from direct assay PubMed 3813556. Source: BHF-UCL
Molecular_function	acyl-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Mitochondrion
	Chain	26 – 421	396	Medium-chain specific acyl-CoA dehydrogenase, mitochondrial		PRO_0000000506
Regions
	Nucleotide binding	158 – 167	10	FAD By similarity
	Nucleotide binding	191 – 193	3	FAD By similarity
	Nucleotide binding	306 – 308	3	FAD By similarity
	Nucleotide binding	316 – 317	2	FAD By similarity
	Nucleotide binding	374 – 378	5	FAD By similarity
	Nucleotide binding	403 – 405	3	FAD By similarity
	Region	278 – 281	4	Substrate binding By similarity
Sites
	Active site	401	1	Proton acceptor By similarity
	Binding site	167	1	Substrate; via carbonyl oxygen By similarity
	Binding site	402	1	Substrate; via amide nitrogen By similarity
	Binding site	413	1	Substrate By similarity
Amino acid modifications
	Modified residue	301	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P08503 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 2CF076F8C919BDE8	FASTA	421	46,555
	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

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.
IPI	IPI00212015.
PIR	DERTCM. A28436.
RefSeq	NP_058682.2. NM_016986.2.
UniGene	Rn.6302.
3D structure databases
ProteinModelPortal	P08503.
SMR	P08503. Positions 34-421.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08503. 1 interaction.
STRING	10116.ENSRNOP00000013238.
Proteomic databases
PaxDb	P08503.
PRIDE	P08503.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	24158.
KEGG	rno:24158.
Organism-specific databases
CTD	34.
RGD	2012. Acadm.
Phylogenomic databases
eggNOG	COG1960.
HOGENOM	HOG000131659.
HOVERGEN	HBG000224.
InParanoid	P08503.
KO	K00249.
OrthoDB	EOG4G7BZB.
Enzyme and pathway databases
SABIO-RK	P08503.
UniPathway	UPA00660.
Gene expression databases
Genevestigator	P08503.
GermOnline	ENSRNOG00000009845. Rattus norvegicus.
Family and domain databases
Gene3D	1.10.540.10. 1 hit. 2.40.110.10. 1 hit.
InterPro	IPR006089. 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. [Graphical view]
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view]
SUPFAM	SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 1 hit.
PROSITE	PS00072. ACYL_COA_DH_1. 1 hit. PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	602449.

Entry information

Entry name

ACADM_RAT

Accession

Primary (citable) accession number: P08503

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	April 3, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program