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Q99J39

- DCMC_MOUSE

UniProt

Q99J39 - DCMC_MOUSE

Protein

Malonyl-CoA decarboxylase, mitochondrial

Gene

Mlycd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jun 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. Plays a role in controlling the extent of ischemic injury by promoting glucose oxidation.2 Publications

    Catalytic activityi

    Malonyl-CoA = acetyl-CoA + CO2.1 Publication

    Enzyme regulationi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei210 – 2101Essential for catalytic activityBy similarity
    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: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

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

    UniPathwayiUPA00340; UER00710.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malonyl-CoA decarboxylase, mitochondrial (EC:4.1.1.9)
    Short name:
    MCD
    Gene namesi
    Name:Mlycd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1928485. Mlycd.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Peroxisome

    Pathology & Biotechi

    Disruption phenotypei

    Mice show an increased expression of genes regulating fatty acid utilization and likely contributes to the absence of changes in energy metabolism in the aerobic heart. Display a preference for glucose utilization after ischemia and improve functional recovery of the heart.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi471 – 4711K → Q: Mimicks constitutive acetylation, leading to increased malonyl-CoA decarboxylase activity. 1 Publication
    Mutagenesisi471 – 4711K → R: Decreased acetylation, leading to reduced malonyl-CoA decarboxylase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3838MitochondrionSequence AnalysisAdd
    BLAST
    Chaini39 – 492454Malonyl-CoA decarboxylase, mitochondrialPRO_0000021090Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581N6-acetyllysine1 Publication
    Modified residuei167 – 1671N6-acetyllysine; alternate1 Publication
    Modified residuei167 – 1671N6-succinyllysine; alternate1 Publication
    Disulfide bondi205 – 205InterchainSequence Analysis
    Modified residuei210 – 2101N6-acetyllysine1 Publication
    Modified residuei221 – 2211N6-succinyllysine1 Publication
    Modified residuei316 – 3161N6-acetyllysine1 Publication
    Modified residuei385 – 3851N6-acetyllysine; alternate1 Publication
    Modified residuei385 – 3851N6-succinyllysine; alternate1 Publication
    Modified residuei388 – 3881N6-acetyllysine1 Publication
    Modified residuei441 – 4411N6-acetyllysine1 Publication
    Modified residuei471 – 4711N6-acetyllysine1 Publication

    Post-translational modificationi

    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
    Acetylation at Lys-471 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-471 by SIRT4 represses activity, leading to promote lipogenesis.2 Publications

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiQ99J39.
    PaxDbiQ99J39.
    PRIDEiQ99J39.

    PTM databases

    PhosphoSiteiQ99J39.

    Expressioni

    Gene expression databases

    BgeeiQ99J39.
    CleanExiMM_MLYCD.
    GenevestigatoriQ99J39.

    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

    MINTiMINT-1861916.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99J39.
    SMRiQ99J39. Positions 38-492.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    InParanoidiQ99J39.
    KOiK01578.
    OMAiLDEGREQ.
    OrthoDBiEOG76X5ZZ.
    PhylomeDBiQ99J39.
    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: A single transcription start site has been demonstrated in Rat.

    Isoform Mitochondrial (identifier: Q99J39-1) [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

    MRGLGPGLRA RRLLPLRSPP RPPGPRGRRL CGGLAASAMD ELLRRAVPPT    50
    PAYELREKTP APAEGQCADF VSFYGGLAEA SQRAELLGRL AQGFGVDHGQ 100
    VAEQSAGVLQ LRQQAREAAV LLQAEDRLRY ALVPRYRGLF HHISKLDGGV 150
    RFLVQLRADL LEAQALKLVE GPHVREMNGV LKSMLSEWFS SGFLNLERVT 200
    WHSPCEVLQK ISECEAVHPV KNWMDMKRRV GPYRRCYFFS HCSTPGEPLV 250
    VLHVALTGDI SNNIQGIVKE CPPTETEERN RIAAAIFYSI SLTQQGLQGV 300
    ELGTFLIKRV VKELQKEFPQ LGAFSSLSPI PGFTKWLLGL LNVQGKEHGR 350
    NELFTDSECQ EISAVTGNPV HESLKGFLSS GEWVKSEKLT QALQGPLMRL 400
    CAWYLYGEKH RGYALNPVAN FHLQNGAVMW RINWMADSSL KGLTSSCGLM 450
    VNYRYYLEET GPNSISYLGS KNIKASEQIL SLVAQFQNNS KL 492
    Length:492
    Mass (Da):54,736
    Last modified:June 1, 2001 - v1
    Checksum:iCEBDA62714A21DC1
    GO
    Isoform Cytoplasmic+peroxisomal (identifier: Q99J39-2) [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.

    Show »
    Length:454
    Mass (Da):50,766
    Checksum:i233693B9C1BF74CA
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3838Missing in isoform Cytoplasmic+peroxisomal. CuratedVSP_018817Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK082479 mRNA. Translation: BAC38505.1.
    BC004764 mRNA. Translation: AAH04764.1.
    AY331094 Genomic DNA. Translation: AAP93335.2.
    CCDSiCCDS22703.1. [Q99J39-1]
    RefSeqiNP_064350.2. NM_019966.2. [Q99J39-1]
    UniGeneiMm.423037.

    Genome annotation databases

    EnsembliENSMUST00000098367; ENSMUSP00000095970; ENSMUSG00000074064. [Q99J39-1]
    GeneIDi56690.
    KEGGimmu:56690.
    UCSCiuc009npn.1. mouse. [Q99J39-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK082479 mRNA. Translation: BAC38505.1 .
    BC004764 mRNA. Translation: AAH04764.1 .
    AY331094 Genomic DNA. Translation: AAP93335.2 .
    CCDSi CCDS22703.1. [Q99J39-1 ]
    RefSeqi NP_064350.2. NM_019966.2. [Q99J39-1 ]
    UniGenei Mm.423037.

    3D structure databases

    ProteinModelPortali Q99J39.
    SMRi Q99J39. Positions 38-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1861916.

    Chemistry

    BindingDBi Q99J39.
    ChEMBLi CHEMBL1255162.

    PTM databases

    PhosphoSitei Q99J39.

    Proteomic databases

    MaxQBi Q99J39.
    PaxDbi Q99J39.
    PRIDEi Q99J39.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000098367 ; ENSMUSP00000095970 ; ENSMUSG00000074064 . [Q99J39-1 ]
    GeneIDi 56690.
    KEGGi mmu:56690.
    UCSCi uc009npn.1. mouse. [Q99J39-1 ]

    Organism-specific databases

    CTDi 23417.
    MGIi MGI:1928485. Mlycd.

    Phylogenomic databases

    eggNOGi COG1593.
    GeneTreei ENSGT00390000005410.
    HOGENOMi HOG000141409.
    HOVERGENi HBG000825.
    InParanoidi Q99J39.
    KOi K01578.
    OMAi LDEGREQ.
    OrthoDBi EOG76X5ZZ.
    PhylomeDBi Q99J39.
    TreeFami TF312959.

    Enzyme and pathway databases

    UniPathwayi UPA00340 ; UER00710 .

    Miscellaneous databases

    NextBioi 313103.
    PROi Q99J39.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99J39.
    CleanExi MM_MLYCD.
    Genevestigatori Q99J39.

    Family and domain databases

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

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Cerebellum.
    2. "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].
      Strain: 129, C57BL/6J and FVB/N.
      Tissue: Mammary tumor.
    3. "Mouse malonyl-CoA decarboxylase: genome structure, cDNA cloning, expression and promoter study."
      Kim N.H., Lee G.Y., Kim Y.S.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-175.
      Strain: 129S6/SvEvTac.
    4. "Absence of malonyl coenzyme A decarboxylase in mice increases cardiac glucose oxidation and protects the heart from ischemic injury."
      Dyck J.R., Hopkins T.A., Bonnet S., Michelakis E.D., Young M.E., Watanabe M., Kawase Y., Jishage K., Lopaschuk G.D.
      Circulation 114:1721-1728(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
    5. Cited for: FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-58; LYS-167; LYS-210; LYS-316; LYS-388; LYS-441 AND LYS-471, MUTAGENESIS OF LYS-471.
    6. "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-167; LYS-221 AND LYS-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "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-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiDCMC_MOUSE
    AccessioniPrimary (citable) accession number: Q99J39
    Secondary accession number(s): Q7TNL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 98 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, 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

    External Data

    Dasty 3