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Q920F5

- DCMC_RAT

UniProt

Q920F5 - DCMC_RAT

Protein

Malonyl-CoA decarboxylase, mitochondrial

Gene

Mlycd

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation.3 Publications

    Catalytic activityi

    Malonyl-CoA = acetyl-CoA + CO2.3 Publications

    Enzyme regulationi

    Malonyl-CoA decarboxylase activity does not require any cofactors or divalent metal ions.By similarity

    Kineticsi

    1. KM=0.36 mM for malonyl-CoA1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei210 – 2101Essential for catalytic activity
    Active sitei328 – 3281Proton acceptorBy similarity
    Binding sitei328 – 3281Malonyl-CoABy similarity
    Active sitei422 – 4221Proton donorBy similarity
    Binding sitei422 – 4221Malonyl-CoABy similarity

    GO - Molecular functioni

    1. malonyl-CoA decarboxylase activity Source: RGD

    GO - Biological processi

    1. acetyl-CoA biosynthetic process Source: RGD
    2. fatty acid biosynthetic process Source: UniProtKB
    3. fatty acid oxidation Source: RGD
    4. malonyl-CoA catabolic process Source: UniProtKB
    5. positive regulation of fatty acid oxidation Source: UniProtKB
    6. regulation of fatty acid beta-oxidation Source: RGD
    7. regulation of fatty acid oxidation Source: RGD
    8. regulation of glucose metabolic process Source: UniProtKB
    9. response to ischemia Source: UniProtKB

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Enzyme and pathway databases

    SABIO-RKQ920F5.
    UniPathwayiUPA00340; UER00710.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malonyl-CoA decarboxylase, mitochondrial (EC:4.1.1.9)
    Short name:
    MCD
    Gene namesi
    Name:Mlycd
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 19

    Organism-specific databases

    RGDi620234. Mlycd.

    Subcellular locationi

    Cytoplasm 1 Publication. Mitochondrion matrix 1 Publication. Peroxisome By similarity. Peroxisome matrix 1 Publication
    Note: Enzymatically active in all three subcellular compartments.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: RGD
    3. mitochondrial matrix Source: UniProtKB
    4. mitochondrion Source: RGD
    5. peroxisomal matrix Source: UniProtKB
    6. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Peroxisome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi210 – 2101K → M: Abolishes catalytic activity. 1 Publication
    Mutagenesisi308 – 3081K → M: 40% reduction in catalytic activity. 1 Publication
    Mutagenesisi388 – 3881K → M: 40% reduction in catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3838MitochondrionSequence AnalysisAdd
    BLAST
    Chaini39 – 492454Malonyl-CoA decarboxylase, mitochondrialPRO_0000021092Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581N6-acetyllysine1 Publication
    Modified residuei167 – 1671N6-acetyllysine; alternateBy similarity
    Modified residuei167 – 1671N6-succinyllysine; alternateBy similarity
    Disulfide bondi205 – 205InterchainSequence Analysis
    Modified residuei210 – 2101N6-acetyllysine1 Publication
    Modified residuei221 – 2211N6-succinyllysineBy similarity
    Modified residuei316 – 3161N6-acetyllysine1 Publication
    Modified residuei385 – 3851N6-acetyllysine; alternateBy similarity
    Modified residuei385 – 3851N6-succinyllysine; alternateBy similarity
    Modified residuei388 – 3881N6-acetyllysine1 Publication
    Modified residuei441 – 4411N6-acetyllysine1 Publication
    Modified residuei471 – 4711N6-acetyllysineBy similarity

    Post-translational modificationi

    Acetylation at Lys-471 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-471 by SIRT4 represses activity, leading to promote lipogenesis By similarity.By similarity
    Interchain disulfide bonds may form in peroxisomes Potential. Interchain disulfide bonds are not expected to form in the reducing environment of the cytoplasm and mitochondria.Curated

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    PaxDbiQ920F5.
    PRIDEiQ920F5.

    PTM databases

    PhosphoSiteiQ920F5.

    Expressioni

    Tissue specificityi

    Expressed in liver, heart, skeletal muscles and adipose tissues (at protein level). Ubiquitous. Strongly expressed in liver, kidney, heart, skeletal muscle and adipose tissues. Weakly expressed in brain.4 Publications

    Gene expression databases

    GenevestigatoriQ920F5.

    Interactioni

    Subunit structurei

    Homotetramer. Dimer of dimers. The two subunits within a dimer display conformational differences suggesting that at any given moment, only one of the two subunits is competent for malonyl-CoA binding and catalytic activity. Under oxidizing conditions, can form disulfide-linked homotetramers (in vitro). Associates with the peroxisomal targeting signal receptor PEX5 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000019923.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni39 – 189151Alpha-helical domainBy similarityAdd
    BLAST
    Regioni190 – 492303Catalytic domainBy similarityAdd
    BLAST
    Regioni298 – 3047Malonyl-CoA bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi490 – 4923Microbody targeting signalSequence Analysis

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1593.
    GeneTreeiENSGT00390000005410.
    HOGENOMiHOG000141409.
    HOVERGENiHBG000825.
    InParanoidiQ920F5.
    KOiK01578.
    OMAiLDEGREQ.
    OrthoDBiEOG76X5ZZ.
    PhylomeDBiQ920F5.
    TreeFamiTF312959.

    Family and domain databases

    InterProiIPR007956. Malonyl_CoA_deC.
    [Graphical view]
    PfamiPF05292. MCD. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Note: According to PubMed:10229677, a single transcription start site has been demonstrated.

    Isoform Mitochondrial (identifier: Q920F5-1) [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

    MRGLGPSLRA RRLLPLRYPP RPPGPRGPRL CSGLTASAMD ELLRRAVPPT    50
    PAYELREKTP APAEGQCADF VSFYGGLAEA AQRAELLGRL AQGFGVDHGQ 100
    VAEQSAGVLQ LRQQSREAAV LLQAEDRLRY ALVPRYRGLF HHISKLDGGV 150
    RFLVQLRADL LEAQALKLVE GPHVREMNGV LKSMLSEWFS SGFLNLERVT 200
    WHSPCEVLQK ISECEAVHPV KNWMDMKRRV GPYRRCYFFS HCSTPGDPLV 250
    VLHVALTGDI SNNIQSIVKE CPPSETEEKN RIAAAVFYSI SLTQQGLQGV 300
    ELGTFLIKRV VKELQKEFPH LGAFSSLSPI PGFTKWLLGL LNVQGKEYGR 350
    NELFTDSECK EIAEVTGDPV HESLKGLLSS GEWAKSEKLA QALQGPLMRL 400
    CAWYLYGEKH RGYALNPVAN FHLQNGAVMW RINWMADSSL KGLTSSCGLM 450
    VNYRYYLEET GPNSISYLGS KNIKASEQIL SLVAQFQSNS KL 492
    Length:492
    Mass (Da):54,762
    Last modified:December 1, 2001 - v1
    Checksum:iD1FB65533B5A582E
    GO
    Isoform Cytoplasmic+peroxisomal (identifier: Q920F5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-38: Missing.

    Note: May be produced by alternative initiation at Met-39 of isoform mitochondrial. Alternatively, represents a proteolytic processed form of the mitochondrial form (PubMed:10947976).1 Publication

    Show »
    Length:454
    Mass (Da):50,685
    Checksum:i92D3679A358E332B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti213 – 2131E → D in CAB46681. (PubMed:10229677)Curated
    Sequence conflicti218 – 2181H → Q in CAB46681. (PubMed:10229677)Curated
    Sequence conflicti301 – 3011E → G in CAB46681. (PubMed:10229677)Curated
    Sequence conflicti412 – 4121Missing in CAB46681. (PubMed:10229677)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3838Missing in isoform Cytoplasmic+peroxisomal. CuratedVSP_018818Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007704 mRNA. Translation: CAB46681.1.
    AF304865 mRNA. Translation: AAL09352.1.
    BC061845 mRNA. Translation: AAH61845.1.
    RefSeqiNP_445929.1. NM_053477.1.
    UniGeneiRn.13468.

    Genome annotation databases

    EnsembliENSRNOT00000019923; ENSRNOP00000019923; ENSRNOG00000014522. [Q920F5-1]
    GeneIDi85239.
    KEGGirno:85239.
    UCSCiRGD:620234. rat. [Q920F5-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007704 mRNA. Translation: CAB46681.1 .
    AF304865 mRNA. Translation: AAL09352.1 .
    BC061845 mRNA. Translation: AAH61845.1 .
    RefSeqi NP_445929.1. NM_053477.1.
    UniGenei Rn.13468.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000019923.

    PTM databases

    PhosphoSitei Q920F5.

    Proteomic databases

    PaxDbi Q920F5.
    PRIDEi Q920F5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000019923 ; ENSRNOP00000019923 ; ENSRNOG00000014522 . [Q920F5-1 ]
    GeneIDi 85239.
    KEGGi rno:85239.
    UCSCi RGD:620234. rat. [Q920F5-1 ]

    Organism-specific databases

    CTDi 23417.
    RGDi 620234. Mlycd.

    Phylogenomic databases

    eggNOGi COG1593.
    GeneTreei ENSGT00390000005410.
    HOGENOMi HOG000141409.
    HOVERGENi HBG000825.
    InParanoidi Q920F5.
    KOi K01578.
    OMAi LDEGREQ.
    OrthoDBi EOG76X5ZZ.
    PhylomeDBi Q920F5.
    TreeFami TF312959.

    Enzyme and pathway databases

    UniPathwayi UPA00340 ; UER00710 .
    SABIO-RK Q920F5.

    Miscellaneous databases

    NextBioi 617288.
    PROi Q920F5.

    Gene expression databases

    Genevestigatori Q920F5.

    Family and domain databases

    InterProi IPR007956. Malonyl_CoA_deC.
    [Graphical view ]
    Pfami PF05292. MCD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of rat pancreatic beta-cell malonyl-CoA decarboxylase."
      Voilley N., Roduit R., Vicaretti R., Bonny C., Waeber G., Dyck J.R., Lopaschuk G.D., Prentki M.
      Biochem. J. 340:213-217(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    2. "Characterization of rat liver malonyl-CoA decarboxylase and the study of its role in regulating fatty acid metabolism."
      Dyck J.R., Berthiaume L.G., Thomas P.D., Kantor P.F., Barr A.J., Barr R., Singh D., Hopkins T.A., Voilley N., Prentki M., Lopaschuk G.D.
      Biochem. J. 350:599-608(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), PARTIAL PROTEIN SEQUENCE, FUNCTION, PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY.
    3. "Rat malonyl-CoA decarboxylase; cloning, expression in E. coli and its biochemical characterization."
      Lee G.Y., Bahk Y.Y., Kim Y.S.
      J. Biochem. Mol. Biol. 35:213-219(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MITOCHONDRIAL).
      Tissue: Prostate.
    5. "MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA decarboxylase and is mutated in malonyl-CoA decarboxylase deficiency."
      Sacksteder K.A., Morrell J.C., Wanders R.J.A., Matalon R., Gould S.J.
      J. Biol. Chem. 274:24461-24468(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORM CYTOPLASMIC+PEROXISOMAL), TISSUE SPECIFICITY.
    6. "Malonyl coenzyme a decarboxylase inhibition protects the ischemic heart by inhibiting fatty acid oxidation and stimulating glucose oxidation."
      Dyck J.R., Cheng J.F., Stanley W.C., Barr R., Chandler M.P., Brown S., Wallace D., Arrhenius T., Harmon C., Yang G., Nadzan A.M., Lopaschuk G.D.
      Circ. Res. 94:E78-E84(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Malonyl-CoA decarboxylase is present in the cytosolic, mitochondrial and peroxisomal compartments of rat hepatocytes."
      Joly E., Bendayan M., Roduit R., Saha A.K., Ruderman N.B., Prentki M.
      FEBS Lett. 579:6581-6586(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    8. "Mass spectrometric identification of K210 essential for rat malonyl-CoA decarboxylase catalysis."
      Nam H.W., Lee G.Y., Kim Y.S.
      J. Proteome Res. 5:1398-1406(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-58; LYS-167; LYS-210; LYS-316; LYS-388 AND LYS-441, MUTAGENESIS OF LYS-210; LYS-308 AND LYS-388.

    Entry informationi

    Entry nameiDCMC_RAT
    AccessioniPrimary (citable) accession number: Q920F5
    Secondary accession number(s): Q9WUY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways

    External Data

    Dasty 3