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Entry version 163 (26 Feb 2020)
Sequence version 1 (01 Apr 1990)
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Protein

Long-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadl

Organism
Rattus norvegicus (Rat)
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 (PubMed:3968063). 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 (PubMed:3968063). 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:3968063, PubMed:15466478).1 Publication2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

FAD1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by crotonyl-CoA, 2-octenoyl-CoA and 2-hexadecenoyl-CoA.1 Publication

<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=123 µM for octanoyl-CoA (at 32 degrees Celsius and pH 8.0)1 Publication
  2. KM=24.3 µM for decanoyl-CoA (at 32 degrees Celsius and pH 8.0)1 Publication
  3. KM=9 µM for dodecanoyl-CoA (at 32 degrees Celsius and pH 8.0)1 Publication
  4. KM=7.4 µM for tetradecanoyl-CoA (at 32 degrees Celsius and pH 8.0)1 Publication
  5. KM=2.5 µM for hexadecanoyl-CoA (at 32 degrees Celsius and pH 8.0)1 Publication
  6. KM=5.4 µM for octadecanoyl-CoA (at 32 degrees Celsius and pH 8.0)1 Publication
  7. KM=6.5 µM for (9Z)-octadecenoyl-CoA (at 32 degrees Celsius and pH 8.0)1 Publication
  8. KM=0.41 µM for tetradecanoyl-CoA1 Publication
  9. KM=0.4 µM for (5Z)-tetradecenoyl-CoA1 Publication
  10. KM=1.6 µM for (5E)-tetradecenoyl-CoA1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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.1 Publication
    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%5Fsection">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%5Fsection">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 acceptorBy similarity1
    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%5Fsection">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

    • acyl-CoA dehydrogenase activity Source: GO_Central
    • fatty-acyl-CoA binding Source: RGD
    • flavin adenine dinucleotide binding Source: RGD
    • identical protein binding Source: RGD
    • long-chain-acyl-CoA dehydrogenase activity Source: RGD
    • palmitoyl-CoA oxidase activity Source: RGD

    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

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-RNO-77285 Beta oxidation of myristoyl-CoA to lauroyl-CoA
    R-RNO-77310 Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P15650

    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:000001586

    <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%5Fand%5Ftaxonomy%5Fsection">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:1.3.8.82 Publications)
    Short name:
    LCAD
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 9

    Organism-specific databases

    Rat genome database

    More...
    RGDi
    2011 Acadl

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    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

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2176836

    <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 – 30Mitochondrion1 PublicationAdd BLAST30
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000051331 – 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 residuei54PhosphoserineCombined sources1
    Modified residuei55PhosphoserineCombined sources1
    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 residuei191PhosphoserineBy 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%5Fprocessing%5Fsection">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

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P15650

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

    More...
    PaxDbi
    P15650

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P15650

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P15650

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P15650

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

    More...
    PhosphoSitePlusi
    P15650

    <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
    ENSRNOG00000012966 Expressed in heart and 9 other tissues

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P15650 RN

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer.

    2 Publications

    GO - Molecular functioni

    • identical protein binding Source: RGD

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    247326, 1 interactor

    Protein interaction database and analysis system

    More...
    IntActi
    P15650, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    10116.ENSRNOP00000017686

    <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
    P15650

    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
    ENOG410XNMY LUCA

    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
    P15650

    KEGG Orthology (KO)

    More...
    KOi
    K00255

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    IVWEEQA

    Database of Orthologous Groups

    More...
    OrthoDBi
    589058at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P15650

    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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P15650-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAARLLLRSL RVLSARSATL PPPSARCSHS GAEARLETPS AKKLTDIGIR
    60 70 80 90 100
    RIFSSEHDIF RESVRKFFQE EVIPYHEEWE KAGEVSRELW EKAGKQGLLG
    110 120 130 140 150
    INIAEKHGGI GGDLLSTAVT WEEQAYSNCT GPGFSLHSDI VMPYIANYGT
    160 170 180 190 200
    KEQIEQFIPQ MTAGKCIGAI AMTEPGAGSD LQGVRTNAKR SGSDWILNGS
    210 220 230 240 250
    KVFITNGWLS DLVIVVAVTN REARSPAHGI SLFLVENGMK GFIKGKKLHK
    260 270 280 290 300
    MGMKAQDTAE LFFEDVRLPA SALLGEENKG FYYLMQELPQ ERLLIADLAI
    310 320 330 340 350
    SACEFMFEET RNYVRQRKAF GKTVAHIQTV QHKLAELKTN ICVTRAFVDS
    360 370 380 390 400
    CLQLHETKRL DSASASMAKY WASELQNTVA YQCVQLHGGW GYMWEYPIAK
    410 420 430
    AYVDARVQPI YGGTNEIMKE LIARQIVSDS
    Length:430
    Mass (Da):47,873
    Last modified:April 1, 1990 - v1
    <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:iBEE1C7E0FDD84D2E
    GO

    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
    J05029 mRNA Translation: AAA40668.1
    L11276 mRNA Translation: AAA41514.1
    BC062006 mRNA Translation: AAH62006.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A34252

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_036951.1, NM_012819.1

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSRNOT00000017686; ENSRNOP00000017686; ENSRNOG00000012966

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    25287

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    rno:25287

    UCSC genome browser

    More...
    UCSCi
    RGD:2011 rat

    <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
    J05029 mRNA Translation: AAA40668.1
    L11276 mRNA Translation: AAA41514.1
    BC062006 mRNA Translation: AAH62006.1
    PIRiA34252
    RefSeqiNP_036951.1, NM_012819.1

    3D structure databases

    SMRiP15650
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi247326, 1 interactor
    IntActiP15650, 1 interactor
    STRINGi10116.ENSRNOP00000017686

    Chemistry databases

    ChEMBLiCHEMBL2176836
    SwissLipidsiSLP:000001586

    PTM databases

    CarbonylDBiP15650
    iPTMnetiP15650
    PhosphoSitePlusiP15650

    Proteomic databases

    jPOSTiP15650
    PaxDbiP15650
    PRIDEiP15650

    Genome annotation databases

    EnsembliENSRNOT00000017686; ENSRNOP00000017686; ENSRNOG00000012966
    GeneIDi25287
    KEGGirno:25287
    UCSCiRGD:2011 rat

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    33
    RGDi2011 Acadl

    Phylogenomic databases

    eggNOGiKOG0141 Eukaryota
    ENOG410XNMY LUCA
    GeneTreeiENSGT00940000157652
    HOGENOMiCLU_018204_0_3_1
    InParanoidiP15650
    KOiK00255
    OMAiIVWEEQA
    OrthoDBi589058at2759
    PhylomeDBiP15650
    TreeFamiTF105054

    Enzyme and pathway databases

    UniPathwayiUPA00660
    ReactomeiR-RNO-77285 Beta oxidation of myristoyl-CoA to lauroyl-CoA
    R-RNO-77310 Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
    SABIO-RKiP15650

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P15650

    Gene expression databases

    BgeeiENSRNOG00000012966 Expressed in heart and 9 other tissues
    GenevisibleiP15650 RN

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <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_RAT
    <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: P15650
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: February 26, 2020
    This is version 163 of the entry and version 1 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

    <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

    Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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