Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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).By similarity

Miscellaneous

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

Catalytic activityi

A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

Cofactori

FADBy similarity

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
Binding sitei167Substrate; via carbonyl oxygenBy similarity1
Active sitei401Proton acceptorBy similarity1
Binding sitei402Substrate; via amide nitrogenBy similarity1
Binding sitei413SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi158 – 167FADBy similarity10
Nucleotide bindingi191 – 193FADBy similarity3
Nucleotide bindingi306 – 308FADBy similarity3
Nucleotide bindingi316 – 317FADBy similarity2
Nucleotide bindingi374 – 378FADBy similarity5
Nucleotide bindingi403 – 405FADBy similarity3

GO - Molecular functioni

GO - Biological processi

  • cardiac muscle cell differentiation Source: MGI
  • carnitine biosynthetic process Source: MGI
  • carnitine metabolic process Source: MGI
  • carnitine metabolic process, CoA-linked Source: BHF-UCL
  • fatty acid beta-oxidation Source: UniProtKB
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: BHF-UCL
  • glycogen biosynthetic process Source: BHF-UCL
  • heart development Source: MGI
  • liver development Source: MGI
  • medium-chain fatty acid catabolic process Source: MGI
  • medium-chain fatty acid metabolic process Source: BHF-UCL
  • organic acid metabolic process Source: MGI
  • oxidation-reduction process Source: MGI
  • post-embryonic development Source: MGI
  • protein homotetramerization Source: MGI
  • regulation of gluconeogenesis Source: BHF-UCL
  • response to cold Source: MGI
  • response to starvation Source: MGI

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-77288 mitochondrial fatty acid beta-oxidation of unsaturated fatty acids
R-MMU-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
R-MMU-77348 Beta oxidation of octanoyl-CoA to hexanoyl-CoA
UniPathwayiUPA00660

Names & Taxonomyi

Protein namesi
Recommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.7)
Short name:
MCAD
Gene namesi
Name:Acadm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:87867 Acadm

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 25MitochondrionBy similarityAdd BLAST25
ChainiPRO_000000050426 – 421Medium-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei30N6-acetyllysine; alternateCombined sources1
Modified residuei30N6-succinyllysine; alternateCombined sources1
Modified residuei69N6-acetyllysine; alternateCombined sources1
Modified residuei69N6-succinyllysine; alternateCombined sources1
Modified residuei79N6-acetyllysineCombined sources1
Modified residuei179N6-succinyllysineCombined sources1
Modified residuei212N6-acetyllysine; alternateCombined sources1
Modified residuei212N6-succinyllysine; alternateCombined sources1
Modified residuei217N6-acetyllysine; alternateCombined sources1
Modified residuei217N6-succinyllysine; alternateCombined sources1
Modified residuei235N6-acetyllysine; alternateCombined sources1
Modified residuei235N6-succinyllysine; alternateCombined sources1
Modified residuei259N6-acetyllysine; alternateCombined sources1
Modified residuei259N6-succinyllysine; alternateCombined sources1
Modified residuei271N6-acetyllysine; alternateCombined sources1
Modified residuei271N6-succinyllysine; alternateCombined sources1
Modified residuei301N6-acetyllysineCombined sources1
Modified residuei351PhosphothreonineCombined sources1

Post-translational modificationi

Acetylation at Lys-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity. These sites are deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP45952
MaxQBiP45952
PaxDbiP45952
PeptideAtlasiP45952
PRIDEiP45952

2D gel databases

SWISS-2DPAGEiP45952

PTM databases

iPTMnetiP45952
PhosphoSitePlusiP45952
SwissPalmiP45952

Expressioni

Gene expression databases

BgeeiENSMUSG00000062908
CleanExiMM_ACADM
ExpressionAtlasiP45952 baseline and differential
GenevisibleiP45952 MM

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi197912, 1 interactor
IntActiP45952, 3 interactors
MINTiP45952
STRINGi10090.ENSMUSP00000072483

Structurei

3D structure databases

ProteinModelPortaliP45952
SMRiP45952
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni278 – 281Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0140 Eukaryota
COG1960 LUCA
GeneTreeiENSGT00760000119007
HOGENOMiHOG000131659
HOVERGENiHBG000224
InParanoidiP45952
KOiK00249
OMAiCPPSKAF
OrthoDBiEOG091G04BS
PhylomeDBiP45952
TreeFamiTF105020

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

Sequencei

Sequence statusi: Complete.

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

P45952-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAFRRGCR VLRSVSHFEC RTQHSKAAHK QEPGLGFSFE LTEQQKEFQA
60 70 80 90 100
TARKFAREEI IPVAPEYDKS GEYPFPLIKR AWELGLINAH IPESCGGLGL
110 120 130 140 150
GTFDACLITE ELAYGCTGVQ TAIEANSLGQ MPVILAGNDQ QKKKYLGRMT
160 170 180 190 200
EQPMMCAYCV TEPSAGSDVA AIKTKAEKKG DEYVINGQKM WITNGGKANW
210 220 230 240 250
YFLLARSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM GQRCSDTRGI
260 270 280 290 300
AFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT
310 320 330 340 350
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN
360 370 380 390 400
TYYASIAKAF AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY
410 420
EGTAQIQRLI IAREHIEKYK N
Length:421
Mass (Da):46,481
Last modified:November 1, 1995 - v1
Checksum:i36976704E3E48CBB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti135L → I in S48759 (PubMed:1438358).Curated1
Sequence conflicti184V → A in S48761 (PubMed:1438358).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07159 mRNA Translation: AAA76733.1
S48761 Genomic DNA No translation available.
S48759 Genomic DNA No translation available.
CCDSiCCDS17924.1
PIRiA55724
RefSeqiNP_031408.1, NM_007382.5
UniGeneiMm.10530

Genome annotation databases

EnsembliENSMUST00000072697; ENSMUSP00000072483; ENSMUSG00000062908
GeneIDi11364
KEGGimmu:11364
UCSCiuc008ruj.2 mouse

Similar proteinsi

Entry informationi

Entry nameiACADM_MOUSE
AccessioniPrimary (citable) accession number: P45952
Secondary accession number(s): Q64235
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 20, 2018
This is version 165 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health