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P28330

- ACADL_HUMAN

UniProt

P28330 - ACADL_HUMAN

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Protein

Long-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Long-chain-acyl-CoA + electron-transfer flavoprotein = long-chain-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

Cofactori

Pathwayi

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: Reactome
  2. fatty-acyl-CoA binding Source: Ensembl
  3. flavin adenine dinucleotide binding Source: Ensembl
  4. long-chain-acyl-CoA dehydrogenase activity Source: BHF-UCL
  5. palmitoyl-CoA oxidase activity Source: BHF-UCL

GO - Biological processi

  1. carnitine catabolic process Source: BHF-UCL
  2. carnitine metabolic process, CoA-linked Source: BHF-UCL
  3. cellular lipid catabolic process Source: BHF-UCL
  4. cellular lipid metabolic process Source: Reactome
  5. fatty acid beta-oxidation Source: Reactome
  6. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: BHF-UCL
  7. long-chain fatty acid catabolic process Source: Ensembl
  8. negative regulation of fatty acid biosynthetic process Source: BHF-UCL
  9. negative regulation of fatty acid oxidation Source: BHF-UCL
  10. oxidation-reduction process Source: BHF-UCL
  11. protein homotetramerization Source: Ensembl
  12. regulation of cholesterol metabolic process Source: BHF-UCL
  13. small molecule metabolic process Source: Reactome
  14. temperature homeostasis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS03876-MONOMER.
ReactomeiREACT_2108. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
SABIO-RKP28330.
UniPathwayiUPA00660.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.8)
Short name:
LCAD
Gene namesi
Name:ACADL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:88. ACADL.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. mitochondrial matrix Source: Reactome
  3. mitochondrial membrane Source: Ensembl
  4. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Acyl-CoA dehydrogenase very long-chain deficiency (ACADVLD) [MIM:201475]: An inborn error of mitochondrial fatty acid beta-oxidation which leads to impaired long-chain fatty acid beta-oxidation. It is clinically heterogeneous, with three major phenotypes: a severe childhood form characterized by early onset, high mortality and high incidence of cardiomyopathy; a milder childhood form with later onset, characterized by hypoketotic hypoglycemia, low mortality and rare cardiomyopathy; an adult form, with isolated skeletal muscle involvement, rhabdomyolysis and myoglobinuria, usually triggered by exercise or fasting.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi201475. phenotype.
Orphaneti99900. Long chain acyl-CoA dehydrogenase deficiency.
PharmGKBiPA24424.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionAdd
BLAST
Chaini31 – 430400Long-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000509Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-acetyllysineBy similarity
Modified residuei66 – 661N6-acetyllysine; alternateBy similarity
Modified residuei66 – 661N6-succinyllysine; alternateBy similarity
Modified residuei81 – 811N6-acetyllysine; alternateBy similarity
Modified residuei81 – 811N6-succinyllysine; alternateBy similarity
Modified residuei92 – 921N6-acetyllysineBy similarity
Modified residuei95 – 951N6-acetyllysineBy similarity
Modified residuei165 – 1651N6-succinyllysineBy similarity
Modified residuei240 – 2401N6-succinyllysineBy similarity
Modified residuei254 – 2541N6-acetyllysine; alternateBy similarity
Modified residuei254 – 2541N6-succinyllysine; alternateBy similarity
Modified residuei279 – 2791N6-acetyllysine; alternateBy similarity
Modified residuei279 – 2791N6-succinyllysine; alternateBy similarity
Modified residuei318 – 3181N6-acetyllysineBy similarity
Modified residuei322 – 3221N6-acetyllysine; alternateBy similarity
Modified residuei322 – 3221N6-succinyllysine; alternateBy similarity
Modified residuei358 – 3581N6-acetyllysineBy similarity

Post-translational modificationi

Acetylation at Lys-318 and Lys-322 in proximity of the cofactor-binding sites strongly reduces catalytic activity. These sites are deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP28330.
PaxDbiP28330.
PRIDEiP28330.

PTM databases

PhosphoSiteiP28330.

Expressioni

Gene expression databases

BgeeiP28330.
CleanExiHS_ACADL.
ExpressionAtlasiP28330. baseline and differential.
GenevestigatoriP28330.

Organism-specific databases

HPAiHPA010611.
HPA011990.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi106551. 4 interactions.
STRINGi9606.ENSP00000233710.

Structurei

3D structure databases

ProteinModelPortaliP28330.
SMRiP28330. Positions 51-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG104903.
InParanoidiP28330.
KOiK00255.
OMAiYMWEYPV.
OrthoDBiEOG77126W.
PhylomeDBiP28330.
TreeFamiTF105054.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28330-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAARLLRGSL RVLGGHRAPR QLPAARCSHS GGEERLETPS AKKLTDIGIR
60 70 80 90 100
RIFSPEHDIF RKSVRKFFQE EVIPHHSEWE KAGEVSREVW EKAGKQGLLG
110 120 130 140 150
VNIAEHLGGI GGDLYSAAIV WEEQAYSNCS GPGFSIHSGI VMSYITNHGS
160 170 180 190 200
EEQIKHFIPQ MTAGKCIGAI AMTEPGAGSD LQGIKTNAKK DGSDWILNGS
210 220 230 240 250
KVFISNGSLS DVVIVVAVTN HEAPSPAHGI SLFLVENGMK GFIKGRKLHK
260 270 280 290 300
MGLKAQDTAE LFFEDIRLPA SALLGEENKG FYYIMKELPQ ERLLIADVAI
310 320 330 340 350
SASEFMFEET RNYVKQRKAF GKTVAHLQTV QHKLAELKTH ICVTRAFVDN
360 370 380 390 400
CLQLHEAKRL DSATACMAKY WASELQNSVA YDCVQLHGGW GYMWEYPIAK
410 420 430
AYVDARVQPI YGGTNEIMKE LIAREIVFDK
Length:430
Mass (Da):47,656
Last modified:February 10, 2009 - v2
Checksum:i72F9803685406DF9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031S → T.1 Publication
Corresponds to variant rs1801204 [ dbSNP | Ensembl ].
VAR_000328
Natural varianti333 – 3331K → Q.2 Publications
Corresponds to variant rs2286963 [ dbSNP | Ensembl ].
VAR_000329

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2389.1.
PIRiA40559.
RefSeqiNP_001599.1. NM_001608.3.
UniGeneiHs.471277.

Genome annotation databases

EnsembliENST00000233710; ENSP00000233710; ENSG00000115361.
GeneIDi33.
KEGGihsa:33.
UCSCiuc002vdz.4. human.

Polymorphism databases

DMDMi223590148.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS2389.1.
PIRi A40559.
RefSeqi NP_001599.1. NM_001608.3.
UniGenei Hs.471277.

3D structure databases

ProteinModelPortali P28330.
SMRi P28330. Positions 51-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106551. 4 interactions.
STRINGi 9606.ENSP00000233710.

PTM databases

PhosphoSitei P28330.

Polymorphism databases

DMDMi 223590148.

Proteomic databases

MaxQBi P28330.
PaxDbi P28330.
PRIDEi P28330.

Protocols and materials databases

DNASUi 33.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233710 ; ENSP00000233710 ; ENSG00000115361 .
GeneIDi 33.
KEGGi hsa:33.
UCSCi uc002vdz.4. human.

Organism-specific databases

CTDi 33.
GeneCardsi GC02M211052.
HGNCi HGNC:88. ACADL.
HPAi HPA010611.
HPA011990.
MIMi 201475. phenotype.
609576. gene.
neXtProti NX_P28330.
Orphaneti 99900. Long chain acyl-CoA dehydrogenase deficiency.
PharmGKBi PA24424.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1960.
GeneTreei ENSGT00760000119007.
HOGENOMi HOG000131659.
HOVERGENi HBG104903.
InParanoidi P28330.
KOi K00255.
OMAi YMWEYPV.
OrthoDBi EOG77126W.
PhylomeDBi P28330.
TreeFami TF105054.

Enzyme and pathway databases

UniPathwayi UPA00660 .
BioCyci MetaCyc:HS03876-MONOMER.
Reactomei REACT_2108. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
SABIO-RK P28330.

Miscellaneous databases

ChiTaRSi ACADL. human.
GenomeRNAii 33.
NextBioi 127.
PROi P28330.
SOURCEi Search...

Gene expression databases

Bgeei P28330.
CleanExi HS_ACADL.
ExpressionAtlasi P28330. baseline and differential.
Genevestigatori P28330.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view ]
Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-333.
    Tissue: Brain.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Colon.
  6. "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.

Entry informationi

Entry nameiACADL_HUMAN
AccessioniPrimary (citable) accession number: P28330
Secondary accession number(s): B2R8T3, Q8IUN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 10, 2009
Last modified: November 26, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3