NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=3611054 [NCBI, ExPASy, EBI, Israel, Japan]
Matsubara Y., Kraus J.P., Ozasa H., Glassberg R., Finocchiaro G., Ikeda Y., Mole J., Rosenberg L.E., Tanaka K.;
"Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat liver medium chain acyl coenzyme A dehydrogenase.";
J. Biol. Chem. 262:10104-10108(1987).

[2]

PROTEIN SEQUENCE OF 11-81.
DOI=10.1016/0167-4838(91)90542-8; PubMed=2029527 [NCBI, ExPASy, EBI, Israel, Japan]
Inagaki T., Ohishi N., Tsukagoshi N., Udaka S., Ghisla S., Yagi K.;
"Structurally different rat liver medium-chain acyl CoA dehydrogenases directed by complementary DNAs differing in their 5'-region.";
Biochim. Biophys. Acta 1077:285-290(1991).

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: Homotetramer.
SUBCELLULAR LOCATION: Mitochondrion matrix.
MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.
SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J02791; AAA40670.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A28436; DERTCM.

NP_058682.1; -.

3D structure databases

HSSP

P11310; 1EGD. [HSSP ENTRY / PDB]

SMR

P08503; 35-421.

ModBase

P08503.

Protein-protein interaction databases

IntAct

P08503; -.

Organism-specific databases

RGD

2012; Acadm.

Gene expression databases

ArrayExpress

P08503; -.

GermOnline

ENSRNOG00000009845; Rattus norvegicus.

Ontologies

GO:0003995;	Molecular function: acyl-CoA dehydrogenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006635;	Biological process: fatty acid beta-oxidation (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR006089; Acyl-CoA_DHase_CS.
IPR006092; Acyl-CoA_DHase_N.
IPR006090; Acyl-CoA_Oxase/DHase_1.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1.

Pfam

PF00441; Acyl-CoA_dh_1; 1.
PF02770; Acyl-CoA_dh_M; 1.
PF02771; Acyl-CoA_dh_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00072; ACYL_COA_DH_1; 1.
PS00073; ACYL_COA_DH_2; 1.

BLOCKS

P08503.

Genome annotation databases

Ensembl

ENSRNOG00000009845; Rattus norvegicus. [Contig view]

GeneID

24158; -.

KEGG

rno:24158; -.

Phylogenomic databases

HOVERGEN

P08503; -.

Other

ProtoNet

P08503.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 25`	`25`	`Mitochondrion.`
`CHAIN`	`26 421`	`396`	`Medium-chain specific acyl-CoA dehydrogenase, mitochondrial.`	`PRO_0000000506`
`NP_BIND`	`158 167`	`10`	`FAD (By similarity).`
`NP_BIND`	`191 193`	`3`	`FAD (By similarity).`
`NP_BIND`	`306 308`	`3`	`FAD (By similarity).`
`NP_BIND`	`316 317`	`2`	`FAD (By similarity).`
`NP_BIND`	`374 378`	`5`	`FAD (By similarity).`
`NP_BIND`	`403 405`	`3`	`FAD (By similarity).`
`REGION`	`278 281`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`401 401`		`Proton acceptor (By similarity).`
`BINDING`	`167 167`		`Substrate; via carbonyl oxygen (By similarity).`
`BINDING`	`402 402`		`Substrate; via amide nitrogen (By similarity).`

Sequence information

Length: 421 AA [This is the length of the unprocessed precursor]

Molecular weight: 46555 Da [This is the MW of the unprocessed precursor]

CRC64: 2CF076F8C919BDE8 [This is a checksum on the sequence]

        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

P08503 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools