[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0888-7543(91)90068-P; PubMed=1774065 [NCBI, ExPASy, EBI, Israel, Japan] Indo Y., Yang-Feng T., Glassberg R., Tanaka K.; "Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2."; Genomics 11:609-620(1991).
[2]	ERRATUM. DOI=10.1016/0888-7543(92)90462-2; PubMed=1559716 [NCBI, ExPASy, EBI, Israel, Japan] Indo Y., Yang-Feng T., Glassberg R., Tanaka K.; Genomics 12:626-626(1992).
[3]	VARIANT SER-303, AND VARIANT LCAD DEFICIENCY LYS-333. Kelly D., Ogden M., Hale D., Hainline B., Strauss A.; "The molecular basis of human long chain acyl-CoA dehydrogenase deficiency."; Am. J. Hum. Genet. 49:409-409(1991).

Comments

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.
DISEASE: Defects in ACADL are the cause of long-chain acyl-CoA dehydrogenase deficiency (LCAD deficiency) [MIM:201460]. LCAD deficiency leads to non-ketotic hypoglycemia.
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.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ACADL";.

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

M74096; AAA51565.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Hs.471277

3D structure databases

HSSP

P26440; 1IVH. [HSSP ENTRY / PDB]

ModBase

P28330.

Enzyme and pathway databases

Reactome

REACT_602; Lipid and lipoprotein metabolism.

Organism-specific databases

HGNC:88; ACADL.

HPA010611; -.
HPA011990; -.

MIM

201460; phenotype. [NCBI / EBI]
609576; gene. [NCBI / EBI]

Orphanet

99900; Acyl-CoA dehydrogenase, long chain, deficiency of.

PharmGKB

PA24424; -.

GeneCards

P28330.

Gene expression databases

ArrayExpress

P28330; -.

CleanEx

HS_ACADL; -.

GermOnline

ENSG00000115361; Homo sapiens.

Ontologies

GO:0004466;	Molecular function: long-chain-acyl-CoA dehydrogenase activity (traceable author statement from ProtInc).
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.

Genome annotation databases

Ensembl

ENSG00000115361; Homo sapiens. [Contig view]

Phylogenomic databases

HOGENOM

P28330; -.

HOVERGEN

P28330; -.

Other

SOURCE

ACADL; Homo sapiens.

UniRef

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

Keywords

Disease mutation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Polymorphism; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 30`	`30`	`Mitochondrion.`
`CHAIN`	`31 430`	`400`	`Long-chain specific acyl-CoA dehydrogenase, mitochondrial.`	`PRO_0000000509`
`VARIANT`	`303 303`	`1`	`T -> S (in dbSNP:rs1801204 [NCBI]).`	`VAR_000328`
`VARIANT`	`333 333`	`1`	`Q -> K (in LCAD deficiency).`	`VAR_000329`

Sequence information

Length: 430 AA [This is the length of the unprocessed precursor]

Molecular weight: 47670 Da [This is the MW of the unprocessed precursor]

CRC64: EBE93BC23A0F8951 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAARLLRGSL RVLGGHRAPR QLPAARCSHS GGEERLETPS AKKLTDIGIR RIFSPEHDIF 

        70         80         90        100        110        120 
RKSVRKFFQE EVIPHHSEWE KAGEVSREVW EKAGKQGLLG VNIAEHLGGI GGDLYSAAIV 

       130        140        150        160        170        180 
WEEQAYSNCS GPGFSIHSGI VMSYITNHGS EEQIKHFIPQ MTAGKCIGAI AMTEPGAGSD 

       190        200        210        220        230        240 
LQGIKTNAKK DGSDWILNGS KVFISNGSLS DVVIVVAVTN HEAPSPAHGI SLFLVENGMK 

       250        260        270        280        290        300 
GFIKGRKLHK MGLKAQDTAE LFFEDIRLPA SALLGEENKG FYYIMKELPQ ERLLIADVAI 

       310        320        330        340        350        360 
SATEFMFEET RNYVKQRKAF GKTVAHLQTV QHQLAELKTH ICVTRAFVDN CLQLHEAKRL 

       370        380        390        400        410        420 
DSATACMAKY WASELQNSVA YDCVQLHGGW GYMWEYPIAK AYVDARVQPI YGGTNEIMKE 

       430 
LIAREIVFDK

P28330 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