Reviewed, UniProtKB/Swiss-Prot P28330 (ACADL_HUMAN)

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

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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 transcript 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.
Involvement in disease	Impaired ACADL activity results in non-ketotic hypoglycemia, hypotonia, muscle weakness and episodes of cardiorespiratory arrest associated with fasting [MIM:201460].
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
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
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 Traceable author statement. Source: ProtInc
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_0000000509
Natural variations
	Natural variant	303	1	S → T: dbSNP rs1801204. Ref.7		VAR_000328
	Natural variant	333	1	K → Q: dbSNP rs2286963. Ref.7 Ref.3		VAR_000329

Sequences

	Sequence		Length	Mass (Da)
	P28330-1 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: 72F9803685406DF9	FASTA	430	47,656
	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 SASEFMFEET RNYVKQRKAF GKTVAHLQTV QHKLAELKTH ICVTRAFVDN CLQLHEAKRL 370 380 390 400 410 420 DSATACMAKY WASELQNSVA YDCVQLHGGW GYMWEYPIAK AYVDARVQPI YGGTNEIMKE 430 LIAREIVFDK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Indo Y., Yang-Feng T., Glassberg R., Tanaka K. Genomics 11:609-620(1991) [PubMed: 1774065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Erratum Indo Y., Yang-Feng T., Glassberg R., Tanaka K. Genomics 12:626-626(1992) [PubMed: 1559716] [Abstract]
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-333. Tissue: Brain.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Brain and Colon.
[7]	"The molecular basis of human long chain acyl-CoA dehydrogenase deficiency." Kelly D., Ogden M., Hale D., Hainline B., Strauss A. Am. J. Hum. Genet. 49:409-409(1991) Cited for: VARIANTS THR-303 AND GLN-333.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M74096 mRNA. Translation: AAA51565.1. AK313498 mRNA. Translation: BAG36280.1. AC006994 Genomic DNA. Translation: AAY14881.1. CH471063 Genomic DNA. Translation: EAW70481.1. BC039063 mRNA. Translation: AAH39063.1. BC064549 mRNA. Translation: AAH64549.1.
IPI	IPI00292695.
PIR	A40559.
RefSeq	NP_001599.1.
UniGene	Hs.471277
3D structure databases
HSSP	HSSP built from PDB template 1IVH based on UniProtKB P26440.
ModBase	Search...
Proteomic databases
PRIDE	P28330.
Genome annotation databases
Ensembl	ENSG00000115361. Homo sapiens. [Contig view]
GeneID	33.
Organism-specific databases
GeneCards	GC02M210760.
HGNC	HGNC:88. ACADL.
HPA	HPA010611. HPA011990.
MIM	201460. phenotype. 609576. gene.
Orphanet	99900. Acyl-CoA dehydrogenase, long chain, deficiency of.
PharmGKB	PA24424.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P28330.
HOVERGEN	P28330.
OMA	P28330. QTVQHKL.
Enzyme and pathway databases
BRENDA	1.3.99.13. 247.
Reactome	REACT_602. Lipid and lipoprotein metabolism.
Gene expression databases
ArrayExpress	P28330.
Bgee	P28330.
CleanEx	HS_ACADL.
GermOnline	ENSG00000115361. Homo sapiens.
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	127.
SOURCE	Search...

Entry information

Entry name

ACADL_HUMAN

Accession

Primary (citable) accession number: P28330
Secondary accession number(s): B2R8T3, Q8IUN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	February 10, 2009
Last modified:	June 16, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)