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Entry version 195 (29 Sep 2021)
Sequence version 2 (10 Feb 2009)
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Protein

Long-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity).

The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity).

Among the different mitochondrial acyl-CoA dehydrogenases, long-chain specific acyl-CoA dehydrogenase can act on saturated and unsaturated acyl-CoAs with 6 to 24 carbons with a preference for 8 to 18 carbons long primary chains (PubMed:8823175, PubMed:21237683).

By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FADBy similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=29 µM for hexanoyl-CoA1 Publication
  2. KM=8 µM for octanoyl-CoA1 Publication
  3. KM=10 µM for decanoyl-CoA1 Publication
  4. KM=7 µM for dodecanoyl-CoA1 Publication
  5. KM=10 µM for tetradecanoyl-CoA1 Publication
  6. KM=14 µM for hexadecanoyl-CoA1 Publication
  7. KM=8 µM for octadecanoyl-CoA1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: mitochondrial fatty acid beta-oxidation

This protein is involved in the pathway mitochondrial fatty acid beta-oxidation, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway mitochondrial fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei179Substrate; via carbonyl oxygenBy similarity1
Binding sitei282SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei291Proton acceptor1 Publication1
Binding sitei317FADBy similarity1
Binding sitei328FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi170 – 179FADBy similarity10
Nucleotide bindingi203 – 205FADBy similarity3
Nucleotide bindingi385 – 389FADBy similarity5
Nucleotide bindingi414 – 416FADBy similarity3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS03876-MONOMER

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
P28330

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-77285, Beta oxidation of myristoyl-CoA to lauroyl-CoA
R-HSA-77288, mitochondrial fatty acid beta-oxidation of unsaturated fatty acids
R-HSA-77310, Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P28330

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00660

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001327

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Long-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.83 Publications)
Short name:
LCAD
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ACADLImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:88, ACADL

Online Mendelian Inheritance in Man (OMIM)

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MIMi
609576, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P28330

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000115361

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Mitochondrion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi291E → Q: Loss of long-chain-acyl-CoA dehydrogenase activity. No effect on protein abundance. No effect on solubility. No effect on substrate binding. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
33

MalaCards human disease database

More...
MalaCardsi
ACADL

Open Targets

More...
OpenTargetsi
ENSG00000115361

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24424

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P28330, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ACADL

Domain mapping of disease mutations (DMDM)

More...
DMDMi
223590148

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 30MitochondrionBy similarityAdd BLAST30
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000050931 – 430Long-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei42N6-acetyllysineBy similarity1
Modified residuei54PhosphoserineBy similarity1
Modified residuei66N6-acetyllysine; alternateBy similarity1
Modified residuei66N6-succinyllysine; alternateBy similarity1
Modified residuei81N6-acetyllysine; alternateBy similarity1
Modified residuei81N6-succinyllysine; alternateBy similarity1
Modified residuei92N6-acetyllysineBy similarity1
Modified residuei95N6-acetyllysineBy similarity1
Modified residuei165N6-succinyllysineBy similarity1
Modified residuei240N6-succinyllysineBy similarity1
Modified residuei254N6-acetyllysine; alternateBy similarity1
Modified residuei254N6-succinyllysine; alternateBy similarity1
Modified residuei279N6-acetyllysine; alternateBy similarity1
Modified residuei279N6-succinyllysine; alternateBy similarity1
Modified residuei318N6-acetyllysineBy similarity1
Modified residuei322N6-acetyllysine; alternateBy similarity1
Modified residuei322N6-succinyllysine; alternateBy similarity1
Modified residuei358N6-acetyllysineBy similarity1
Modified residuei362PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P28330

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P28330

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P28330

PeptideAtlas

More...
PeptideAtlasi
P28330

PRoteomics IDEntifications database

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PRIDEi
P28330

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
54469

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P28330

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P28330

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P28330

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000115361, Expressed in left lobe of thyroid gland and 164 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P28330, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000115361, Tissue enhanced (lung, thyroid gland)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
106551, 11 interactors

Protein interaction database and analysis system

More...
IntActi
P28330, 8 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000233710

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P28330, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P28330

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni227 – 228Substrate bindingBy similarity2
Regioni289 – 292Substrate bindingBy similarity4
Regioni412 – 413Substrate bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0141, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157652

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_018204_0_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P28330

Identification of Orthologs from Complete Genome Data

More...
OMAi
QNRVATQ

Database of Orthologous Groups

More...
OrthoDBi
589058at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P28330

TreeFam database of animal gene trees

More...
TreeFami
TF105054

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01160, LCAD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.540.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006089, Acyl-CoA_DH_CS
IPR006091, Acyl-CoA_Oxase/DH_cen-dom
IPR036250, AcylCo_DH-like_C
IPR009075, AcylCo_DH/oxidase_C
IPR013786, AcylCoA_DH/ox_N
IPR037069, AcylCoA_DH/ox_N_sf
IPR009100, AcylCoA_DH/oxidase_NM_dom
IPR034179, LCAD

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00441, Acyl-CoA_dh_1, 1 hit
PF02770, Acyl-CoA_dh_M, 1 hit
PF02771, Acyl-CoA_dh_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47203, SSF47203, 1 hit
SSF56645, SSF56645, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00072, ACYL_COA_DH_1, 1 hit
PS00073, ACYL_COA_DH_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i72F9803685406DF9
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000328303S → T1 PublicationCorresponds to variant dbSNP:rs1801204Ensembl.1
Natural variantiVAR_000329333K → Q2 PublicationsCorresponds to variant dbSNP:rs2286963EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2389.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A40559

NCBI Reference Sequences

More...
RefSeqi
NP_001599.1, NM_001608.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000233710; ENSP00000233710; ENSG00000115361

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
33

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:33

UCSC genome browser

More...
UCSCi
uc002vdz.5, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
CCDSiCCDS2389.1
PIRiA40559
RefSeqiNP_001599.1, NM_001608.3

3D structure databases

SMRiP28330
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi106551, 11 interactors
IntActiP28330, 8 interactors
STRINGi9606.ENSP00000233710

Chemistry databases

SwissLipidsiSLP:000001327

PTM databases

iPTMnetiP28330
PhosphoSitePlusiP28330
SwissPalmiP28330

Genetic variation databases

BioMutaiACADL
DMDMi223590148

Proteomic databases

MassIVEiP28330
MaxQBiP28330
PaxDbiP28330
PeptideAtlasiP28330
PRIDEiP28330
ProteomicsDBi54469

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
1641, 323 antibodies

The DNASU plasmid repository

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DNASUi
33

Genome annotation databases

EnsembliENST00000233710; ENSP00000233710; ENSG00000115361
GeneIDi33
KEGGihsa:33
UCSCiuc002vdz.5, human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
33
DisGeNETi33

GeneCards: human genes, protein and diseases

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GeneCardsi
ACADL
HGNCiHGNC:88, ACADL
HPAiENSG00000115361, Tissue enhanced (lung, thyroid gland)
MalaCardsiACADL
MIMi609576, gene
neXtProtiNX_P28330
OpenTargetsiENSG00000115361
PharmGKBiPA24424
VEuPathDBiHostDB:ENSG00000115361

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG0141, Eukaryota
GeneTreeiENSGT00940000157652
HOGENOMiCLU_018204_0_3_1
InParanoidiP28330
OMAiQNRVATQ
OrthoDBi589058at2759
PhylomeDBiP28330
TreeFamiTF105054

Enzyme and pathway databases

UniPathwayiUPA00660
BioCyciMetaCyc:HS03876-MONOMER
PathwayCommonsiP28330
ReactomeiR-HSA-77285, Beta oxidation of myristoyl-CoA to lauroyl-CoA
R-HSA-77288, mitochondrial fatty acid beta-oxidation of unsaturated fatty acids
R-HSA-77310, Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
SABIO-RKiP28330

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
33, 9 hits in 1008 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
ACADL, human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
33
PharosiP28330, Tbio

Protein Ontology

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PROi
PR:P28330
RNActiP28330, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000115361, Expressed in left lobe of thyroid gland and 164 other tissues
GenevisibleiP28330, HS

Family and domain databases

CDDicd01160, LCAD, 1 hit
Gene3Di1.10.540.10, 1 hit
InterProiView protein in InterPro
IPR006089, Acyl-CoA_DH_CS
IPR006091, Acyl-CoA_Oxase/DH_cen-dom
IPR036250, AcylCo_DH-like_C
IPR009075, AcylCo_DH/oxidase_C
IPR013786, AcylCoA_DH/ox_N
IPR037069, AcylCoA_DH/ox_N_sf
IPR009100, AcylCoA_DH/oxidase_NM_dom
IPR034179, LCAD
PfamiView protein in Pfam
PF00441, Acyl-CoA_dh_1, 1 hit
PF02770, Acyl-CoA_dh_M, 1 hit
PF02771, Acyl-CoA_dh_N, 1 hit
SUPFAMiSSF47203, SSF47203, 1 hit
SSF56645, SSF56645, 1 hit
PROSITEiView protein in PROSITE
PS00072, ACYL_COA_DH_1, 1 hit
PS00073, ACYL_COA_DH_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACADL_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P28330
Secondary accession number(s): B2R8T3, Q8IUN8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 10, 2009
Last modified: September 29, 2021
This is version 195 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
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