P45952 (ACADM_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

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 By similarity.
Pathway	Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion matrix 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 process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cardiac muscle cell differentiation Inferred from mutant phenotype PubMed 16121256. Source: MGI carnitine biosynthetic process Inferred from electronic annotation. Source: Compara carnitine metabolic process, CoA-linked Inferred from mutant phenotype PubMed 18459129. Source: BHF-UCL 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 liver development Inferred from mutant phenotype PubMed 16121256. Source: MGI medium-chain fatty acid metabolic process Inferred from mutant phenotype PubMed 18459129. Source: BHF-UCL 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_component	axon Inferred from electronic annotation. Source: Compara mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI
Molecular_function	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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Mitochondrion By similarity
	Chain	26 – 421	396	Medium-chain specific acyl-CoA dehydrogenase, mitochondrial		PRO_0000000504
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
Experimental info
	Sequence conflict	135	1	L → I in S48759. Ref.2
	Sequence conflict	184	1	V → A in S48761. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P45952 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 36976704E3E48CBB	FASTA	421	46,481
	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

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.
+	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.
IPI	IPI00134961.
PIR	A55724.
RefSeq	NP_031408.1. NM_007382.5.
UniGene	Mm.10530.
3D structure databases
ProteinModelPortal	P45952.
SMR	P45952. Positions 35-421.
ModBase	Search...
PTM databases
PhosphoSite	P45952.
2D gel databases
SWISS-2DPAGE	P45952.
Proteomic databases
PaxDb	P45952.
PRIDE	P45952.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000072697; ENSMUSP00000072483; ENSMUSG00000062908.
GeneID	11364.
KEGG	mmu:11364.
UCSC	uc008ruj.1. mouse.
Organism-specific databases
CTD	34.
MGI	MGI:87867. Acadm.
Phylogenomic databases
eggNOG	COG1960.
GeneTree	ENSGT00680000099623.
HOGENOM	HOG000131659.
HOVERGEN	HBG000224.
InParanoid	P45952.
KO	K00249.
OMA	IAMGTFD.
Enzyme and pathway databases
UniPathway	UPA00660.
Gene expression databases
ArrayExpress	P45952.
Bgee	P45952.
CleanEx	MM_ACADM.
Genevestigator	P45952.
GermOnline	ENSMUSG00000062908. Mus musculus.
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	278640.
SOURCE	Search...

Entry information

Entry name

ACADM_MOUSE

Accession

Primary (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 3, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program