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Entry version 225 (10 Feb 2021)
Sequence version 1 (01 Jul 1989)
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Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADM

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

Medium-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:1970566, PubMed:8823175, PubMed:21237683, PubMed:2251268). 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:2251268). Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (PubMed:25416781, PubMed:15159392). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains (PubMed:1970566, PubMed:8823175, PubMed:21237683, PubMed:2251268).6 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

FAD4 Publications

<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=175 µM for butyryl-CoA1 Publication
  2. KM=15 µM for hexanoyl-CoA1 Publication
  3. KM=3.4 µM for octanoyl-CoA1 Publication
  4. KM=2.5 µM for decanoyl-CoA1 Publication
  5. KM=2.5 µM for dodecanoyl-CoA1 Publication
  6. KM=2.3 µM for tetradecanoyl-CoA1 Publication
  7. KM=1.6 µM for hexadecanoyl-CoA1 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 sitei167Substrate; via carbonyl oxygen1 Publication1
    Binding sitei216Substrate1 Publication1
    Binding sitei351SubstrateBy 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 sitei401Proton acceptor2 Publications1
    Binding sitei413SubstrateBy 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 bindingi158 – 167FADCombined sources4 Publications10
    Nucleotide bindingi191 – 193FADCombined sources4 Publications3
    Nucleotide bindingi306 – 308FAD; shared with dimeric partnerCombined sources4 Publications3
    Nucleotide bindingi316 – 317FADCombined sources4 Publications2
    Nucleotide bindingi374 – 378FAD; shared with dimeric partnerCombined sources4 Publications5
    Nucleotide bindingi401 – 405FADCombined sources4 Publications5

    <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:HS04089-MONOMER

    Pathway Commons web resource for biological pathway data

    More...
    PathwayCommonsi
    P11310

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-1989781, PPARA activates gene expression
    R-HSA-77288, mitochondrial fatty acid beta-oxidation of unsaturated fatty acids
    R-HSA-77346, Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
    R-HSA-77348, Beta oxidation of octanoyl-CoA to hexanoyl-CoA

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P11310

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P11310

    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:000001334

    <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:
    Medium-chain specific acyl-CoA dehydrogenase, mitochondrial1 Publication (EC:1.3.8.73 Publications)
    Short name:
    MCAD1 Publication
    Alternative name(s):
    Medium chain acyl-CoA dehydrogenase1 Publication
    Short name:
    MCADH1 Publication
    <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:ACADMImported
    <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>OrganismiHomo sapiens (Human)
    <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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <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
    • UP000005640 <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 1

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:89, ACADM

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    607008, gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P11310

    Eukaryotic Pathogen, Vector and Host Database Resources

    More...
    VEuPathDBi
    HostDB:ENSG00000117054.13

    <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

    <p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD)16 Publications
    The disease is caused by variants affecting the gene represented in this entry.
    Disease descriptionAn inborn error of mitochondrial fatty acid beta-oxidation which causes fasting hypoglycemia, hepatic dysfunction and encephalopathy, often resulting in death in infancy.
    Related information in OMIM
    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_00031753R → C in ACADMD. Corresponds to variant dbSNP:rs398123072EnsemblClinVar.1
    Natural variantiVAR_01369867Y → H in ACADMD; mild. 1 PublicationCorresponds to variant dbSNP:rs121434280EnsemblClinVar.1
    Natural variantiVAR_01595478I → T in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs398123074EnsemblClinVar.1
    Natural variantiVAR_000318115 – 116Missing in ACADMD. 1 Publication2
    Natural variantiVAR_015955116C → Y in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs875989859EnsemblClinVar.1
    Natural variantiVAR_015956121T → I in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434283EnsemblClinVar.1
    Natural variantiVAR_000319149M → I in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434277EnsemblClinVar.1
    Natural variantiVAR_000320193T → A in ACADMD; the thermostability is markedly decreased. 2 PublicationsCorresponds to variant dbSNP:rs121434279EnsemblClinVar.1
    Natural variantiVAR_000321195G → R in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434278EnsemblClinVar.1
    Natural variantiVAR_015957206R → L in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs200724875EnsemblClinVar.1
    Natural variantiVAR_000322244C → R in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434276EnsemblClinVar.1
    Natural variantiVAR_013699245S → L in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434281EnsemblClinVar.1
    Natural variantiVAR_000323267G → R in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434274EnsemblClinVar.1
    Natural variantiVAR_013700281R → T in ACADMD; mild or benign clinical phenotype. 1 PublicationCorresponds to variant dbSNP:rs121434282EnsemblClinVar.1
    Natural variantiVAR_015958310G → R in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs747268471EnsemblClinVar.1
    Natural variantiVAR_000324326M → T in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs786204631EnsemblClinVar.1
    Natural variantiVAR_000325329K → E in ACADMD; may alter splicing; decreased fatty acid beta-oxidation. 6 PublicationsCorresponds to variant dbSNP:rs77931234EnsemblClinVar.1
    Natural variantiVAR_000326336S → R in ACADMD. 1 Publication1
    Natural variantiVAR_015959352Y → C in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs1227800781EnsemblClinVar.1
    Natural variantiVAR_000327375I → T in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434275EnsemblClinVar.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi86L → M: Strongly reduced rate of electron transfer to ETF. 1 Publication1
    Mutagenesisi98L → W: Strongly reduced rate of electron transfer to ETF. 1 Publication1
    Mutagenesisi100L → Y: Strongly reduced rate of electron transfer to ETF. 1 Publication1
    Mutagenesisi108I → M: Strongly reduced rate of electron transfer to ETF. 1 Publication1
    Mutagenesisi191W → A: Loss of electron transfer to ETF. 1 Publication1
    Mutagenesisi191W → F: Reduces rate of electron transfer to ETF about six-fold. 1 Publication1
    Mutagenesisi237E → A: Strongly reduced rate of electron transfer to ETF. 2 Publications1
    Mutagenesisi280T → E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410. 1 Publication1
    Mutagenesisi384E → A: Reduces rate of electron transfer to ETF three-fold. 2 Publications1
    Mutagenesisi384E → Q: Reduces rate of electron transfer to ETF two-fold. 2 Publications1
    Mutagenesisi401E → G: Changed substrate specificity towards longer acyl chains; when associated with E-280. 1 Publication1
    Mutagenesisi401E → Q: Loss of acyl-CoA dehydrogenase activity. 1 Publication1
    Mutagenesisi401E → T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280. 1 Publication1

    Keywords - Diseasei

    Disease variant

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    34

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...
    GeneReviewsi
    ACADM

    MalaCards human disease database

    More...
    MalaCardsi
    ACADM
    MIMi201450, phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000117054

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    42, Medium chain acyl-CoA dehydrogenase deficiency

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA24425

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    P11310, Tbio

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4295713

    Drug and drug target database

    More...
    DrugBanki
    DB03415, 3-thiaoctanoyl-CoA
    DB03147, Flavin adenine dinucleotide
    DB02910, Octanoyl-Coenzyme A

    Genetic variation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    ACADM

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    113017

    <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 – 25Mitochondrion1 PublicationAdd BLAST25
    <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_000000050226 – 421Medium-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST396

    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 residuei69N6-acetyllysine; alternateBy similarity1
    Modified residuei69N6-succinyllysine; alternateBy similarity1
    Modified residuei179N6-succinyllysineBy similarity1
    Modified residuei212N6-acetyllysine; alternateBy similarity1
    Modified residuei212N6-succinyllysine; alternateBy similarity1
    Modified residuei217N6-acetyllysine; alternateBy similarity1
    Modified residuei217N6-succinyllysine; alternateBy similarity1
    Modified residuei259N6-acetyllysine; alternateBy similarity1
    Modified residuei259N6-succinyllysine; alternateBy similarity1
    Modified residuei271N6-acetyllysine; alternateBy similarity1
    Modified residuei271N6-succinyllysine; alternateBy similarity1
    Modified residuei279N6-acetyllysineCombined sources1
    Modified residuei301N6-acetyllysineCombined sources1
    Modified residuei351PhosphothreonineBy 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

    Acetylated. Could occur at proximity of the cofactor-binding sites and reduce the catalytic activity. Could be deacetylated by SIRT3.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P11310

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P11310

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P11310

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P11310

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

    More...
    PaxDbi
    P11310

    PeptideAtlas

    More...
    PeptideAtlasi
    P11310

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P11310

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    52743 [P11310-1]
    52744 [P11310-2]

    2D gel databases

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    IPI00005040

    University College Dublin 2-DE Proteome Database

    More...
    UCD-2DPAGEi
    P11310

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P11310

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

    More...
    PhosphoSitePlusi
    P11310

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P11310

    <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
    ENSG00000117054, Expressed in skeletal muscle tissue of rectus abdominis and 250 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P11310, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P11310, HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    ENSG00000117054, Tissue enhanced (liver, skeletal muscle)

    <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 (PubMed:8823176, Ref. 23).

    Interacts with the heterodimeric electron transfer flavoprotein ETF.

    4 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    106552, 79 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-34281N

    Protein interaction database and analysis system

    More...
    IntActi
    P11310, 24 interactors

    Molecular INTeraction database

    More...
    MINTi
    P11310

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000359871

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P11310, 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

    Secondary structure

    1421
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    P11310

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P11310

    <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>Regioni278 – 281Substrate binding1 Publication4

    <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
    KOG0140, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000158429

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P11310

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P11310

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF105020

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01157, MCAD, 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
    IPR034180, MCAD

    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>Sequences (2+)i

    <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.

    This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P11310-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MAAGFGRCCR VLRSISRFHW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA
    60 70 80 90 100
    TARKFAREEI IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL
    110 120 130 140 150
    GTFDACLISE ELAYGCTGVQ TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT
    160 170 180 190 200
    EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG DEYIINGQKM WITNGGKANW
    210 220 230 240 250
    YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM GQRCSDTRGI
    260 270 280 290 300
    VFEDVKVPKE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT
    310 320 330 340 350
    KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN
    360 370 380 390 400
    TYYASIAKAF AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY
    410 420
    EGTSQIQRLI VAREHIDKYK N
    Length:421
    Mass (Da):46,588
    Last modified:July 1, 1989 - 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:i7CD0B5832410581B
    GO
    Isoform 2 (identifier: P11310-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         10-10: R → RCSLQ

    Show »
    Length:425
    Mass (Da):47,020
    Checksum:iC6A133404E1B6E70
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    Q5T4U5Q5T4U5_HUMAN
    Medium-chain specific acyl-CoA dehy...
    ACADM hCG_22915
    454Annotation 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>
    B7Z9I1B7Z9I1_HUMAN
    Medium-chain specific acyl-CoA dehy...
    ACADM
    385Annotation score:

    Annotation score:4 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>
    E9PJM9E9PJM9_HUMAN
    Medium-chain-specific acyl-CoA dehy...
    ACADM
    104Annotation score:

    Annotation score:1 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>
    E9PRX4E9PRX4_HUMAN
    Medium-chain-specific acyl-CoA dehy...
    ACADM
    76Annotation score:

    Annotation score:1 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>
    H0YDT5H0YDT5_HUMAN
    Medium-chain-specific acyl-CoA dehy...
    ACADM
    67Annotation score:

    Annotation score:1 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>
    E9PQA8E9PQA8_HUMAN
    Medium-chain-specific acyl-CoA dehy...
    ACADM
    45Annotation score:

    Annotation score:1 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>
    E9PLN7E9PLN7_HUMAN
    Medium-chain-specific acyl-CoA dehy...
    ACADM
    50Annotation score:

    Annotation score:1 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>
    E9PIX8E9PIX8_HUMAN
    Acyl-CoA dehydrogenase C-4 to C-12 ...
    ACADM
    47Annotation score:

    Annotation score:1 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 Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti356I → T in AAF63626 (Ref. 3) Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_00031753R → C in ACADMD. Corresponds to variant dbSNP:rs398123072EnsemblClinVar.1
    Natural variantiVAR_01369867Y → H in ACADMD; mild. 1 PublicationCorresponds to variant dbSNP:rs121434280EnsemblClinVar.1
    Natural variantiVAR_01595478I → T in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs398123074EnsemblClinVar.1
    Natural variantiVAR_000318115 – 116Missing in ACADMD. 1 Publication2
    Natural variantiVAR_015955116C → Y in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs875989859EnsemblClinVar.1
    Natural variantiVAR_015956121T → I in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434283EnsemblClinVar.1
    Natural variantiVAR_035716132P → R in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs875989854EnsemblClinVar.1
    Natural variantiVAR_000319149M → I in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434277EnsemblClinVar.1
    Natural variantiVAR_000320193T → A in ACADMD; the thermostability is markedly decreased. 2 PublicationsCorresponds to variant dbSNP:rs121434279EnsemblClinVar.1
    Natural variantiVAR_000321195G → R in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434278EnsemblClinVar.1
    Natural variantiVAR_015957206R → L in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs200724875EnsemblClinVar.1
    Natural variantiVAR_000322244C → R in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434276EnsemblClinVar.1
    Natural variantiVAR_013699245S → L in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434281EnsemblClinVar.1
    Natural variantiVAR_000323267G → R in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434274EnsemblClinVar.1
    Natural variantiVAR_013700281R → T in ACADMD; mild or benign clinical phenotype. 1 PublicationCorresponds to variant dbSNP:rs121434282EnsemblClinVar.1
    Natural variantiVAR_015958310G → R in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs747268471EnsemblClinVar.1
    Natural variantiVAR_000324326M → T in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs786204631EnsemblClinVar.1
    Natural variantiVAR_000325329K → E in ACADMD; may alter splicing; decreased fatty acid beta-oxidation. 6 PublicationsCorresponds to variant dbSNP:rs77931234EnsemblClinVar.1
    Natural variantiVAR_000326336S → R in ACADMD. 1 Publication1
    Natural variantiVAR_015959352Y → C in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs1227800781EnsemblClinVar.1
    Natural variantiVAR_000327375I → T in ACADMD. 1 PublicationCorresponds to variant dbSNP:rs121434275EnsemblClinVar.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_03842010R → RCSLQ in isoform 2. 1 Publication1

    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
    M16827 mRNA Translation: AAA51566.1
    M91432 M91431 Genomic DNA Translation: AAA59567.1
    AF251043 mRNA Translation: AAF63626.1
    AK312629 mRNA Translation: BAG35514.1
    AL357314 Genomic DNA No translation available.
    CH471059 Genomic DNA Translation: EAX06401.1
    BC005377 mRNA Translation: AAH05377.1
    M60505 Genomic DNA Translation: AAB59625.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS44165.1 [P11310-2]
    CCDS668.1 [P11310-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A29031, DEHUCM

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_000007.1, NM_000016.5 [P11310-1]
    NP_001120800.1, NM_001127328.2 [P11310-2]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000370841; ENSP00000359878; ENSG00000117054 [P11310-1]
    ENST00000420607; ENSP00000409612; ENSG00000117054 [P11310-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    34

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:34

    UCSC genome browser

    More...
    UCSCi
    uc001dgw.6, human [P11310-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <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
    M16827 mRNA Translation: AAA51566.1
    M91432 M91431 Genomic DNA Translation: AAA59567.1
    AF251043 mRNA Translation: AAF63626.1
    AK312629 mRNA Translation: BAG35514.1
    AL357314 Genomic DNA No translation available.
    CH471059 Genomic DNA Translation: EAX06401.1
    BC005377 mRNA Translation: AAH05377.1
    M60505 Genomic DNA Translation: AAB59625.1
    CCDSiCCDS44165.1 [P11310-2]
    CCDS668.1 [P11310-1]
    PIRiA29031, DEHUCM
    RefSeqiNP_000007.1, NM_000016.5 [P11310-1]
    NP_001120800.1, NM_001127328.2 [P11310-2]

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EGCX-ray2.60A/B/C/D26-421[»]
    1EGDX-ray2.40A/B/C/D26-421[»]
    1EGEX-ray2.75A/B/C/D26-421[»]
    1T9GX-ray2.90A/B/C/D26-421[»]
    2A1TX-ray2.80A/B/C/D1-421[»]
    4P13X-ray1.73A/B/C/D35-421[»]
    SMRiP11310
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi106552, 79 interactors
    DIPiDIP-34281N
    IntActiP11310, 24 interactors
    MINTiP11310
    STRINGi9606.ENSP00000359871

    Chemistry databases

    ChEMBLiCHEMBL4295713
    DrugBankiDB03415, 3-thiaoctanoyl-CoA
    DB03147, Flavin adenine dinucleotide
    DB02910, Octanoyl-Coenzyme A
    SwissLipidsiSLP:000001334

    PTM databases

    iPTMnetiP11310
    PhosphoSitePlusiP11310
    SwissPalmiP11310

    Genetic variation databases

    BioMutaiACADM
    DMDMi113017

    2D gel databases

    REPRODUCTION-2DPAGEiIPI00005040
    UCD-2DPAGEiP11310

    Proteomic databases

    EPDiP11310
    jPOSTiP11310
    MassIVEiP11310
    MaxQBiP11310
    PaxDbiP11310
    PeptideAtlasiP11310
    PRIDEiP11310
    ProteomicsDBi52743 [P11310-1]
    52744 [P11310-2]

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    1642, 438 antibodies

    The DNASU plasmid repository

    More...
    DNASUi
    34

    Genome annotation databases

    EnsembliENST00000370841; ENSP00000359878; ENSG00000117054 [P11310-1]
    ENST00000420607; ENSP00000409612; ENSG00000117054 [P11310-2]
    GeneIDi34
    KEGGihsa:34
    UCSCiuc001dgw.6, human [P11310-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    34
    DisGeNETi34

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    ACADM
    GeneReviewsiACADM
    HGNCiHGNC:89, ACADM
    HPAiENSG00000117054, Tissue enhanced (liver, skeletal muscle)
    MalaCardsiACADM
    MIMi201450, phenotype
    607008, gene
    neXtProtiNX_P11310
    OpenTargetsiENSG00000117054
    Orphaneti42, Medium chain acyl-CoA dehydrogenase deficiency
    PharmGKBiPA24425
    VEuPathDBiHostDB:ENSG00000117054.13

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0140, Eukaryota
    GeneTreeiENSGT00940000158429
    InParanoidiP11310
    PhylomeDBiP11310
    TreeFamiTF105020

    Enzyme and pathway databases

    UniPathwayiUPA00660
    BioCyciMetaCyc:HS04089-MONOMER
    PathwayCommonsiP11310
    ReactomeiR-HSA-1989781, PPARA activates gene expression
    R-HSA-77288, mitochondrial fatty acid beta-oxidation of unsaturated fatty acids
    R-HSA-77346, Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
    R-HSA-77348, Beta oxidation of octanoyl-CoA to hexanoyl-CoA
    SABIO-RKiP11310
    SIGNORiP11310

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...
    BioGRID-ORCSi
    34, 2 hits in 870 CRISPR screens

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

    More...
    ChiTaRSi
    ACADM, human
    EvolutionaryTraceiP11310

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

    More...
    GenomeRNAii
    34
    PharosiP11310, Tbio

    Protein Ontology

    More...
    PROi
    PR:P11310
    RNActiP11310, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000117054, Expressed in skeletal muscle tissue of rectus abdominis and 250 other tissues
    ExpressionAtlasiP11310, baseline and differential
    GenevisibleiP11310, HS

    Family and domain databases

    CDDicd01157, MCAD, 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
    IPR034180, MCAD
    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 nameiACADM_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: P11310
    Secondary accession number(s): Q5T4U4, Q9NYF1
    <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: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: February 10, 2021
    This is version 225 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
    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

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

    1. Human variants curated from literature reports
      Index of human variants curated from literature reports
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families
    6. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    7. Human entries with genetic variants
      List of human entries with genetic variants
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