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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

Acyl-CoA dehydrogenase specific for acyl chain lengths of 4 to 16 that catalyzes the initial step of fatty acid beta-oxidation. Utilizes the electron transfer flavoprotein (ETF) as an electron acceptor to transfer electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).1 Publication

Miscellaneous

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

<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

FAD1 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.
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 ‘Function’ 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
Binding sitei216Substrate1
<p>This subsection of the ‘Function’ 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 acceptor1
Binding sitei402Substrate; via amide nitrogen1
Binding sitei413Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 – 167FAD1 Publication10
Nucleotide bindingi191 – 193FAD1 Publication3
Nucleotide bindingi306 – 308FAD1 Publication3
Nucleotide bindingi316 – 317FAD1 Publication2
Nucleotide bindingi374 – 378FAD1 Publication5
Nucleotide bindingi403 – 405FAD1 Publication3

<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

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BioCyci
MetaCyc:HS04089-MONOMER

Reactome - a knowledgebase of biological pathways and processes

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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

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SABIO-RKi
P11310

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

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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_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:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.7)
Short name:
MCAD
<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:ACADM
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000117054.13

Human Gene Nomenclature Database

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HGNCi
HGNC:89 ACADM

Online Mendelian Inheritance in Man (OMIM)

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MIMi
607008 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P11310

<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; 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 mutations 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.
See also OMIM:201450
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 Publication1
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; most common variant. 6 PublicationsCorresponds to variant dbSNP:rs77931234Ensembl.1
Natural variantiVAR_000326336S → R in ACADMD. 1 Publication1
Natural variantiVAR_015959352Y → C in ACADMD. 1 Publication1
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_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>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
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

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
34

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

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GeneReviewsi
ACADM

MalaCards human disease database

More...
MalaCardsi
ACADM
MIMi201450 phenotype

Open Targets

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OpenTargetsi
ENSG00000117054

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

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Orphaneti
42 Medium chain acyl-CoA dehydrogenase deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24425

Chemistry databases

Drug and drug target database

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DrugBanki
DB03415 3-Thiaoctanoyl-Coenzyme A
DB03147 Flavin adenine dinucleotide
DB02910 Octanoyl-Coenzyme A

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ACADM

Domain mapping of disease mutations (DMDM)

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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 – 25MitochondrionAdd BLAST25
<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_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_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-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity (By similarity). These sites are deacetylated by SIRT3.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P11310

MaxQB - The MaxQuant DataBase

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MaxQBi
P11310

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

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PaxDbi
P11310

PeptideAtlas

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PeptideAtlasi
P11310

PRoteomics IDEntifications database

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PRIDEi
P11310

ProteomicsDB human proteome resource

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ProteomicsDBi
52743
52744 [P11310-2]

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00005040

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P11310

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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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

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Bgeei
ENSG00000117054 Expressed in 237 organ(s), highest expression level in skeletal muscle tissue of rectus abdominis

CleanEx database of gene expression profiles

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CleanExi
HS_ACADM

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P11310 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P11310 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA006198
HPA026542

<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. Interacts with the heterodimeric electron transfer flavoprotein ETF.3 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
106552, 50 interactors

Database of interacting proteins

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DIPi
DIP-34281N

Protein interaction database and analysis system

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IntActi
P11310, 14 interactors

Molecular INTeraction database

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MINTi
P11310

STRING: functional protein association networks

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STRINGi
9606.ENSP00000409612

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P11310

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

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SMRi
P11310

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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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 binding4

<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

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eggNOGi
KOG0140 Eukaryota
COG1960 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158429

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000131659

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000224

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P11310

KEGG Orthology (KO)

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KOi
K00249

Database for complete collections of gene phylogenies

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PhylomeDBi
P11310

TreeFam database of animal gene trees

More...
TreeFami
TF105020

Family and domain databases

Conserved Domains Database

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CDDi
cd01157 MCAD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.540.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_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.

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.<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 'canonical' 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
Acyl-Coenzyme A dehydrogenase, C-4 ...
ACADM hCG_22915
454Annotation score:

Annotation score:3 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:2 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>
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>
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 Publication1
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; most common variant. 6 PublicationsCorresponds to variant dbSNP:rs77931234Ensembl.1
Natural variantiVAR_000326336S → R in ACADMD. 1 Publication1
Natural variantiVAR_015959352Y → C in ACADMD. 1 Publication1
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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<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
, M91421, M91422, M91423, M91425, M91426, M91427, M91428, M91429, M91430, 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]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.445040

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, Polymorphism

<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
, M91421, M91422, M91423, M91425, M91426, M91427, M91428, M91429, M91430, 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]
UniGeneiHs.445040

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[»]
ProteinModelPortaliP11310
SMRiP11310
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106552, 50 interactors
DIPiDIP-34281N
IntActiP11310, 14 interactors
MINTiP11310
STRINGi9606.ENSP00000409612

Chemistry databases

DrugBankiDB03415 3-Thiaoctanoyl-Coenzyme A
DB03147 Flavin adenine dinucleotide
DB02910 Octanoyl-Coenzyme A
SwissLipidsiSLP:000001334

PTM databases

iPTMnetiP11310
PhosphoSitePlusiP11310
SwissPalmiP11310

Polymorphism and mutation databases

BioMutaiACADM
DMDMi113017

2D gel databases

REPRODUCTION-2DPAGEiIPI00005040
UCD-2DPAGEiP11310

Proteomic databases

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

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
34
Structural Biology KnowledgebaseSearch...

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
EuPathDBiHostDB:ENSG00000117054.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ACADM
GeneReviewsiACADM
HGNCiHGNC:89 ACADM
HPAiHPA006198
HPA026542
MalaCardsiACADM
MIMi201450 phenotype
607008 gene
neXtProtiNX_P11310
OpenTargetsiENSG00000117054
Orphaneti42 Medium chain acyl-CoA dehydrogenase deficiency
PharmGKBiPA24425

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0140 Eukaryota
COG1960 LUCA
GeneTreeiENSGT00940000158429
HOGENOMiHOG000131659
HOVERGENiHBG000224
InParanoidiP11310
KOiK00249
PhylomeDBiP11310
TreeFamiTF105020

Enzyme and pathway databases

UniPathwayi
UPA00660

BioCyciMetaCyc:HS04089-MONOMER
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

Miscellaneous databases

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

Protein Ontology

More...
PROi
PR:P11310

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000117054 Expressed in 237 organ(s), highest expression level in skeletal muscle tissue of rectus abdominis
CleanExiHS_ACADM
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...

<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_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: July 1, 1989
Last sequence update: July 1, 1989
Last modified: December 5, 2018
This is version 210 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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