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P45952

- ACADM_MOUSE

UniProt

P45952 - ACADM_MOUSE

Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadm

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    This enzyme is specific for acyl chain lengths of 4 to 16.

    Catalytic activityi

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

    Cofactori

    FAD.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei167 – 1671Substrate; via carbonyl oxygenBy similarity
    Active sitei401 – 4011Proton acceptorBy similarity
    Binding sitei402 – 4021Substrate; via amide nitrogenBy similarity
    Binding sitei413 – 4131SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi158 – 16710FADBy similarity
    Nucleotide bindingi191 – 1933FADBy similarity
    Nucleotide bindingi306 – 3083FADBy similarity
    Nucleotide bindingi316 – 3172FADBy similarity
    Nucleotide bindingi374 – 3785FADBy similarity
    Nucleotide bindingi403 – 4053FADBy similarity

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: InterPro
    3. medium-chain-acyl-CoA dehydrogenase activity Source: BHF-UCL

    GO - Biological processi

    1. cardiac muscle cell differentiation Source: MGI
    2. carnitine biosynthetic process Source: Ensembl
    3. carnitine metabolic process Source: MGI
    4. carnitine metabolic process, CoA-linked Source: BHF-UCL
    5. fatty acid beta-oxidation Source: UniProtKB
    6. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: BHF-UCL
    7. glycogen biosynthetic process Source: BHF-UCL
    8. heart development Source: MGI
    9. liver development Source: MGI
    10. medium-chain fatty acid catabolic process Source: Ensembl
    11. medium-chain fatty acid metabolic process Source: BHF-UCL
    12. organic acid metabolic process Source: MGI
    13. post-embryonic development Source: MGI
    14. regulation of gluconeogenesis Source: BHF-UCL
    15. response to cold Source: MGI
    16. response to starvation Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_198602. PPARA activates gene expression.
    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:87867. Acadm.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2525MitochondrionBy similarityAdd
    BLAST
    Chaini26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000504Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei30 – 301N6-acetyllysine; alternate1 Publication
    Modified residuei30 – 301N6-succinyllysine; alternate1 Publication
    Modified residuei69 – 691N6-acetyllysine; alternate1 Publication
    Modified residuei69 – 691N6-succinyllysine; alternate1 Publication
    Modified residuei79 – 791N6-acetyllysine1 Publication
    Modified residuei179 – 1791N6-succinyllysine1 Publication
    Modified residuei212 – 2121N6-acetyllysine; alternate1 Publication
    Modified residuei212 – 2121N6-succinyllysine; alternate1 Publication
    Modified residuei217 – 2171N6-acetyllysine; alternate1 Publication
    Modified residuei217 – 2171N6-succinyllysine; alternate1 Publication
    Modified residuei235 – 2351N6-acetyllysine; alternate1 Publication
    Modified residuei235 – 2351N6-succinyllysine; alternate1 Publication
    Modified residuei259 – 2591N6-acetyllysine; alternate1 Publication
    Modified residuei259 – 2591N6-succinyllysine; alternate1 Publication
    Modified residuei271 – 2711N6-acetyllysine; alternate1 Publication
    Modified residuei271 – 2711N6-succinyllysine; alternate1 Publication
    Modified residuei301 – 3011N6-acetyllysine1 Publication

    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

    Proteomic databases

    MaxQBiP45952.
    PaxDbiP45952.
    PRIDEiP45952.

    2D gel databases

    SWISS-2DPAGEP45952.

    PTM databases

    PhosphoSiteiP45952.

    Expressioni

    Gene expression databases

    ArrayExpressiP45952.
    BgeeiP45952.
    CleanExiMM_ACADM.
    GenevestigatoriP45952.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    IntActiP45952. 2 interactions.
    MINTiMINT-1860219.

    Structurei

    3D structure databases

    ProteinModelPortaliP45952.
    SMRiP45952. Positions 35-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni278 – 2814Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1960.
    GeneTreeiENSGT00750000117417.
    HOGENOMiHOG000131659.
    HOVERGENiHBG000224.
    InParanoidiP45952.
    KOiK00249.
    OMAiSAWEVDQ.
    OrthoDBiEOG74FF0S.
    PhylomeDBiP45952.
    TreeFamiTF105020.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProiIPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P45952-1 [UniParc]FASTAAdd to Basket

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    MAAAFRRGCR VLRSVSHFEC RTQHSKAAHK QEPGLGFSFE LTEQQKEFQA    50
    TARKFAREEI IPVAPEYDKS GEYPFPLIKR AWELGLINAH IPESCGGLGL 100
    GTFDACLITE ELAYGCTGVQ TAIEANSLGQ MPVILAGNDQ QKKKYLGRMT 150
    EQPMMCAYCV TEPSAGSDVA AIKTKAEKKG DEYVINGQKM WITNGGKANW 200
    YFLLARSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM GQRCSDTRGI 250
    AFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT 300
    KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN 350
    TYYASIAKAF AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY 400
    EGTAQIQRLI IAREHIEKYK N 421
    Length:421
    Mass (Da):46,481
    Last modified:November 1, 1995 - v1
    Checksum:i36976704E3E48CBB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351L → I in S48759. (PubMed:1438358)Curated
    Sequence conflicti184 – 1841V → A in S48761. (PubMed:1438358)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07159 mRNA. Translation: AAA76733.1 .
    S48761 Genomic DNA. No translation available.
    S48759 Genomic DNA. No translation available.
    CCDSi CCDS17924.1.
    PIRi A55724.
    RefSeqi NP_031408.1. NM_007382.5.
    UniGenei Mm.10530.

    3D structure databases

    ProteinModelPortali P45952.
    SMRi P45952. Positions 35-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P45952. 2 interactions.
    MINTi MINT-1860219.

    PTM databases

    PhosphoSitei P45952.

    2D gel databases

    SWISS-2DPAGE P45952.

    Proteomic databases

    MaxQBi P45952.
    PaxDbi P45952.
    PRIDEi P45952.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000072697 ; ENSMUSP00000072483 ; ENSMUSG00000062908 .
    GeneIDi 11364.
    KEGGi mmu:11364.
    UCSCi uc008ruj.1. mouse.

    Organism-specific databases

    CTDi 34.
    MGIi MGI:87867. Acadm.

    Phylogenomic databases

    eggNOGi COG1960.
    GeneTreei ENSGT00750000117417.
    HOGENOMi HOG000131659.
    HOVERGENi HBG000224.
    InParanoidi P45952.
    KOi K00249.
    OMAi SAWEVDQ.
    OrthoDBi EOG74FF0S.
    PhylomeDBi P45952.
    TreeFami TF105020.

    Enzyme and pathway databases

    UniPathwayi UPA00660 .
    Reactomei REACT_198602. PPARA activates gene expression.

    Miscellaneous databases

    NextBioi 278640.
    PROi P45952.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P45952.
    Bgeei P45952.
    CleanExi MM_ACADM.
    Genevestigatori P45952.

    Family and domain databases

    Gene3Di 1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProi IPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view ]
    Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of the mouse medium-chain acyl-CoA dehydrogenase cDNA."
      Tolwani R.J., Farmer S.C., Wood P.A.
      Genomics 23:247-249(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    2. "Molecular studies of mouse medium and long-chain acyl-CoA dehydrogenase genes for site-directed mutagenesis of embryonic stem cells."
      Wood P.A., Farmer S.C., Tolwani R.J., Warren J.R., Steinkampf M.P., Johnson L.W., Mountz J.D., Kelly D.P.
      Prog. Clin. Biol. Res. 375:151-160(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-193.
    3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-69; LYS-179; LYS-212; LYS-217; LYS-235; LYS-259 AND LYS-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-69; LYS-79; LYS-212; LYS-217; LYS-235; LYS-259; LYS-271 AND LYS-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiACADM_MOUSE
    AccessioniPrimary (citable) accession number: P45952
    Secondary accession number(s): Q64235
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    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

    External Data

    Dasty 3