Reviewed, UniProtKB/Swiss-Prot P15650 (ACADL_RAT)

Names and origin

Protein names

Recommended name:
    Long-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=LCAD
    EC=1.3.99.13

Gene names

Name:

Acadl

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	430 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)

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.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro long-chain-acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 30	30	Mitochondrion
	Chain	31 – 430	400	Long-chain specific acyl-CoA dehydrogenase, mitochondrial		PRO_0000000513

Sequences

	Sequence		Length	Mass (Da)
	P15650-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: BEE1C7E0FDD84D2E	FASTA	430	47,873
	10 20 30 40 50 60 MAARLLLRSL RVLSARSATL PPPSARCSHS GAEARLETPS AKKLTDIGIR RIFSSEHDIF 70 80 90 100 110 120 RESVRKFFQE EVIPYHEEWE KAGEVSRELW EKAGKQGLLG INIAEKHGGI GGDLLSTAVT 130 140 150 160 170 180 WEEQAYSNCT GPGFSLHSDI VMPYIANYGT KEQIEQFIPQ MTAGKCIGAI AMTEPGAGSD 190 200 210 220 230 240 LQGVRTNAKR SGSDWILNGS KVFITNGWLS DLVIVVAVTN REARSPAHGI SLFLVENGMK 250 260 270 280 290 300 GFIKGKKLHK MGMKAQDTAE LFFEDVRLPA SALLGEENKG FYYLMQELPQ ERLLIADLAI 310 320 330 340 350 360 SACEFMFEET RNYVRQRKAF GKTVAHIQTV QHKLAELKTN ICVTRAFVDS CLQLHETKRL 370 380 390 400 410 420 DSASASMAKY WASELQNTVA YQCVQLHGGW GYMWEYPIAK AYVDARVQPI YGGTNEIMKE 430 LIARQIVSDS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family." Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K. J. Biol. Chem. 264:16321-16331(1989) [PubMed: 2777793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Tissue specific and developmental expression of rat long- and medium-chain acyl-CoA dehydrogenases." Hainline B.E., Kahlenbeck D.J., Grant J., Strauss A.W. Biochim. Biophys. Acta 1216:460-468(1993) [PubMed: 8268228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Aorta.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[4]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 52-61 AND 255-267, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J05029 mRNA. Translation: AAA40668.1. L11276 mRNA. Translation: AAA41514.1. BC062006 mRNA. Translation: AAH62006.1.
IPI	IPI00211225.
PIR	A34252.
RefSeq	NP_036951.1.
UniGene	Rn.174
3D structure databases
HSSP	HSSP built from PDB template 1IVH based on UniProtKB P26440.
ModBase	Search...
Proteomic databases
PRIDE	P15650.
Genome annotation databases
Ensembl	ENSRNOG00000012966. Rattus norvegicus. [Contig view]
GeneID	25287.
KEGG	rno:25287.
Organism-specific databases
RGD	2011. Acadl.
Phylogenomic databases
HOVERGEN	P15650.
OMA	P15650. QTVQHKL.
Enzyme and pathway databases
BRENDA	1.3.99.13. 248.
Gene expression databases
ArrayExpress	P15650.
GermOnline	ENSRNOG00000012966. Rattus norvegicus.
Family and domain databases
InterPro	IPR006089. Acyl-CoA_DH_CS. IPR006092. Acyl-CoA_DH_N. IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_M. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA: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.
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view]
PROSITE	PS00072. ACYL_COA_DH_1. 1 hit. PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	606021.

Entry information

Entry name

ACADL_RAT

Accession

Primary (citable) accession number: P15650

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)