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Protein

Malonyl-CoA decarboxylase, mitochondrial

Gene

MLYCD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.4 Publications

Catalytic activityi

Malonyl-CoA = acetyl-CoA + CO2.5 Publications

Enzyme regulationi

Malonyl-CoA decarboxylase activity does not require any cofactors or divalent metal ions. Formation of interchain disulfide bonds leads to positive cooperativity between active sites and increases the affinity for malonyl-CoA and the catalytic efficiency (in vitro).2 Publications

Kineticsi

kcat is 19 sec(-1) with malonyl-CoA for malonyl-CoA decarboxylase mitochondrial form, PubMed:15003260. kcat is 28 sec(-1) with malonyl-CoA for Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form, PubMed:15003260. The catalytic efficiency for malonyl-CoA is at least 1.09-fold higher with the malonyl-CoA decarboxylase cytoplasmic+peroxisomal form, PubMed:15003260.

  1. KM=0.36 mM for malonyl-CoA (Malonyl-CoA decarboxylase mitochondrial form), PubMed:150032603 Publications
  2. KM=0.83 mM for malonyl-CoA (Malonyl-CoA decarboxylase mitochondrial form), PubMed:234825653 Publications
  3. KM=0.22 mM for malonyl-CoA (Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form), PubMed:104551073 Publications
  4. KM=0.33 mM for malonyl-CoA (Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form), PubMed:150032603 Publications

    Pathway:iacetyl-CoA biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes acetyl-CoA from malonyl-CoA.
    Proteins known to be involved in this subpathway in this organism are:
    1. Malonyl-CoA decarboxylase, mitochondrial (MLYCD)
    This subpathway is part of the pathway acetyl-CoA biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from malonyl-CoA, the pathway acetyl-CoA biosynthesis and in Metabolic intermediate biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei211 – 2111Essential for catalytic activityBy similarity
    Active sitei329 – 3291Proton acceptor1 Publication
    Binding sitei329 – 3291Malonyl-CoACurated
    Active sitei423 – 4231Proton donor1 Publication
    Binding sitei423 – 4231Malonyl-CoACurated

    GO - Molecular functioni

    • malonyl-CoA decarboxylase activity Source: UniProtKB
    • receptor binding Source: UniProtKB

    GO - Biological processi

    • acetyl-CoA biosynthetic process Source: UniProtKB
    • cellular lipid metabolic process Source: Reactome
    • fatty acid biosynthetic process Source: UniProtKB
    • malonyl-CoA catabolic process Source: UniProtKB
    • positive regulation of fatty acid oxidation Source: UniProtKB
    • regulation of glucose metabolic process Source: UniProtKB
    • response to ischemia Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BRENDAi4.1.1.9. 2681.
    ReactomeiREACT_16957. Peroxisomal lipid metabolism.
    SABIO-RKO95822.
    UniPathwayiUPA00340; UER00710.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malonyl-CoA decarboxylase, mitochondrial (EC:4.1.1.9)
    Short name:
    MCD
    Gene namesi
    Name:MLYCD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:7150. MLYCD.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • mitochondrial matrix Source: UniProtKB
    • mitochondrion Source: UniProtKB
    • peroxisomal matrix Source: UniProtKB
    • peroxisome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    Malonyl-CoA decarboxylase deficiency (MLYCD deficiency)

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionAutosomal recessive disease characterized by abdominal pain, chronic constipation, episodic vomiting, metabolic acidosis and malonic aciduria.

    See also OMIM:248360

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi206 – 2061C → S: Abolishes formation of disulfide-linked homotetramers. Abolishes the cooperative enzyme kinetics that are seen under oxidative conditions. 1 Publication
    Mutagenesisi243 – 2431C → S: Does not abolish formation of disulfide-linked homotetramers. No effect on development of cooperative enzyme kinetics in response to oxidative conditions. 1 Publication
    Mutagenesisi290 – 2901S → F: 2-fold reduction in catalytic activity. 1 Publication
    Mutagenesisi302 – 3021E → G: Decreases catalytic activity. Increases affinity for malonyl-CoA. 1 Publication
    Mutagenesisi329 – 3291S → A: 110-fold reduction in catalytic activity. 1 Publication
    Mutagenesisi423 – 4231H → N: 7-fold reduction in catalytic activity. 1 Publication
    Mutagenesisi456 – 4561Y → S: 3.5-fold reduction in catalytic activity. 1 Publication

    Organism-specific databases

    MIMi248360. phenotype.
    Orphaneti943. Malonic aciduria.
    PharmGKBiPA30861.

    Polymorphism and mutation databases

    BioMutaiMLYCD.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939MitochondrionSequence AnalysisAdd
    BLAST
    Chaini40 – 493454Malonyl-CoA decarboxylase, mitochondrialPRO_0000021088Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591N6-acetyllysineBy similarity
    Modified residuei168 – 1681N6-acetyllysine; alternateBy similarity
    Modified residuei168 – 1681N6-succinyllysine; alternateBy similarity
    Disulfide bondi206 – 206InterchainSequence Analysis
    Modified residuei211 – 2111N6-acetyllysineBy similarity
    Modified residuei222 – 2221N6-succinyllysineBy similarity
    Modified residuei389 – 3891N6-acetyllysineBy similarity
    Modified residuei472 – 4721N6-acetyllysineBy similarity

    Post-translational modificationi

    Acetylation at Lys-472 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-472 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

    MaxQBiO95822.
    PaxDbiO95822.
    PRIDEiO95822.

    PTM databases

    PhosphoSiteiO95822.

    Expressioni

    Tissue specificityi

    Expressed in fibroblasts and hepatoblastoma cells (at protein level). Expressed strongly in heart, liver, skeletal muscle, kidney and pancreas. Expressed in myotubes. Expressed weakly in brain, placenta, spleen, thymus, testis, ovary and small intestine.2 Publications

    Gene expression databases

    BgeeiO95822.
    CleanExiHS_MLYCD.
    GenevisibleiO95822. HS.

    Organism-specific databases

    HPAiHPA031625.

    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 PEX5.2 Publications

    Protein-protein interaction databases

    BioGridi116989. 4 interactions.
    DIPiDIP-60405N.
    IntActiO95822. 1 interaction.
    STRINGi9606.ENSP00000262430.

    Structurei

    Secondary structure

    1
    493
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 478Combined sources
    Helixi54 – 563Combined sources
    Helixi67 – 7610Combined sources
    Helixi81 – 9414Combined sources
    Helixi99 – 11214Combined sources
    Turni114 – 1163Combined sources
    Helixi119 – 13214Combined sources
    Helixi138 – 1458Combined sources
    Beta strandi147 – 1493Combined sources
    Helixi150 – 16617Combined sources
    Helixi173 – 18917Combined sources
    Helixi192 – 1943Combined sources
    Beta strandi195 – 2006Combined sources
    Helixi206 – 2149Combined sources
    Helixi224 – 2307Combined sources
    Beta strandi235 – 2428Combined sources
    Beta strandi250 – 26011Combined sources
    Helixi266 – 2694Combined sources
    Beta strandi285 – 29410Combined sources
    Helixi296 – 2983Combined sources
    Turni299 – 3013Combined sources
    Helixi303 – 31816Combined sources
    Beta strandi324 – 3274Combined sources
    Helixi334 – 3418Combined sources
    Beta strandi348 – 3503Combined sources
    Helixi357 – 36711Combined sources
    Helixi374 – 3796Combined sources
    Turni380 – 3823Combined sources
    Helixi383 – 3864Combined sources
    Helixi388 – 3936Combined sources
    Helixi395 – 40713Combined sources
    Beta strandi414 – 4174Combined sources
    Helixi418 – 4258Combined sources
    Beta strandi429 – 4346Combined sources
    Helixi441 – 4477Combined sources
    Beta strandi451 – 4555Combined sources
    Helixi458 – 4603Combined sources
    Helixi461 – 47111Combined sources
    Helixi478 – 4869Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YGWX-ray2.80A/B40-490[»]
    4F0XX-ray3.29A/B/C/D/E/F/G/H39-493[»]
    ProteinModelPortaliO95822.
    SMRiO95822. Positions 39-493.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 190151Alpha-helical domainAdd
    BLAST
    Regioni191 – 493303Catalytic domainAdd
    BLAST
    Regioni299 – 3057Malonyl-CoA bindingCurated

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi491 – 4933Microbody targeting signalSequence Analysis

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1593.
    GeneTreeiENSGT00390000005410.
    HOGENOMiHOG000141409.
    HOVERGENiHBG000825.
    InParanoidiO95822.
    KOiK01578.
    OMAiLDEGREQ.
    OrthoDBiEOG76X5ZZ.
    PhylomeDBiO95822.
    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. AlignAdd to basket

    Note: A single transcription start site has been demonstrated in Rat.

    Isoform Mitochondrial (identifier: O95822-1) [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
    MRGFGPGLTA RRLLPLRLPP RPPGPRLASG QAAGALERAM DELLRRAVPP
    60 70 80 90 100
    TPAYELREKT PAPAEGQCAD FVSFYGGLAE TAQRAELLGR LARGFGVDHG
    110 120 130 140 150
    QVAEQSAGVL HLRQQQREAA VLLQAEDRLR YALVPRYRGL FHHISKLDGG
    160 170 180 190 200
    VRFLVQLRAD LLEAQALKLV EGPDVREMNG VLKGMLSEWF SSGFLNLERV
    210 220 230 240 250
    TWHSPCEVLQ KISEAEAVHP VKNWMDMKRR VGPYRRCYFF SHCSTPGEPL
    260 270 280 290 300
    VVLHVALTGD ISSNIQAIVK EHPPSETEEK NKITAAIFYS ISLTQQGLQG
    310 320 330 340 350
    VELGTFLIKR VVKELQREFP HLGVFSSLSP IPGFTKWLLG LLNSQTKEHG
    360 370 380 390 400
    RNELFTDSEC KEISEITGGP INETLKLLLS SSEWVQSEKL VRALQTPLMR
    410 420 430 440 450
    LCAWYLYGEK HRGYALNPVA NFHLQNGAVL WRINWMADVS LRGITGSCGL
    460 470 480 490
    MANYRYFLEE TGPNSTSYLG SKIIKASEQV LSLVAQFQKN SKL
    Length:493
    Mass (Da):55,003
    Last modified:December 1, 2000 - v3
    Checksum:i8F061CA38908E8FC
    GO
    Isoform Cytoplasmic+peroxisomal (identifier: O95822-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.

    Note: May be produced by alternative initiation at Met-40 of isoform mitochondrial. Alternatively, represents a proteolytic processed form of the mitochondrial form.
    Show »
    Length:454
    Mass (Da):50,946
    Checksum:i41C79B2AC6DB3554
    GO

    Sequence cautioni

    The sequence AAD16177.2 differs from that shown. Reason: Frameshift at positions 23, 28, 297 and 308. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821A → D in AAD16177 (PubMed:10417274).Curated
    Sequence conflicti119 – 1191A → S in AAD48994 (PubMed:9869665).Curated
    Sequence conflicti127 – 1271D → V in AAD48994 (PubMed:9869665).Curated
    Sequence conflicti192 – 1921S → P in AAD34631 (PubMed:10455107).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3939Missing in isoform Cytoplasmic+peroxisomal. 3 PublicationsVSP_047649Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF097832 mRNA. Translation: AAD16177.2. Frameshift.
    AF153679 mRNA. Translation: AAD34631.1.
    AF090834 mRNA. Translation: AAD48994.1.
    AC009119 Genomic DNA. No translation available.
    BC000286 mRNA. Translation: AAH00286.1.
    BC052592 mRNA. Translation: AAH52592.1.
    CCDSiCCDS42206.1. [O95822-1]
    RefSeqiNP_036345.2. NM_012213.2. [O95822-1]
    UniGeneiHs.644610.

    Genome annotation databases

    EnsembliENST00000262430; ENSP00000262430; ENSG00000103150.
    GeneIDi23417.
    KEGGihsa:23417.
    UCSCiuc002fgz.3. human. [O95822-1]

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF097832 mRNA. Translation: AAD16177.2. Frameshift.
    AF153679 mRNA. Translation: AAD34631.1.
    AF090834 mRNA. Translation: AAD48994.1.
    AC009119 Genomic DNA. No translation available.
    BC000286 mRNA. Translation: AAH00286.1.
    BC052592 mRNA. Translation: AAH52592.1.
    CCDSiCCDS42206.1. [O95822-1]
    RefSeqiNP_036345.2. NM_012213.2. [O95822-1]
    UniGeneiHs.644610.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YGWX-ray2.80A/B40-490[»]
    4F0XX-ray3.29A/B/C/D/E/F/G/H39-493[»]
    ProteinModelPortaliO95822.
    SMRiO95822. Positions 39-493.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116989. 4 interactions.
    DIPiDIP-60405N.
    IntActiO95822. 1 interaction.
    STRINGi9606.ENSP00000262430.

    Chemistry

    BindingDBiO95822.
    ChEMBLiCHEMBL4698.

    PTM databases

    PhosphoSiteiO95822.

    Polymorphism and mutation databases

    BioMutaiMLYCD.

    Proteomic databases

    MaxQBiO95822.
    PaxDbiO95822.
    PRIDEiO95822.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000262430; ENSP00000262430; ENSG00000103150.
    GeneIDi23417.
    KEGGihsa:23417.
    UCSCiuc002fgz.3. human. [O95822-1]

    Organism-specific databases

    CTDi23417.
    GeneCardsiGC16P083932.
    H-InvDBHIX0173296.
    HGNCiHGNC:7150. MLYCD.
    HPAiHPA031625.
    MIMi248360. phenotype.
    606761. gene.
    neXtProtiNX_O95822.
    Orphaneti943. Malonic aciduria.
    PharmGKBiPA30861.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1593.
    GeneTreeiENSGT00390000005410.
    HOGENOMiHOG000141409.
    HOVERGENiHBG000825.
    InParanoidiO95822.
    KOiK01578.
    OMAiLDEGREQ.
    OrthoDBiEOG76X5ZZ.
    PhylomeDBiO95822.
    TreeFamiTF312959.

    Enzyme and pathway databases

    UniPathwayiUPA00340; UER00710.
    BRENDAi4.1.1.9. 2681.
    ReactomeiREACT_16957. Peroxisomal lipid metabolism.
    SABIO-RKO95822.

    Miscellaneous databases

    ChiTaRSiMLYCD. human.
    GenomeRNAii23417.
    NextBioi45627.
    PROiO95822.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO95822.
    CleanExiHS_MLYCD.
    GenevisibleiO95822. HS.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Tissue: Heart.
    3. "Cloning and mutational analysis of human malonyl-coenzyme A decarboxylase."
      Gao J., Waber L., Bennett M.J., Gibson K.M., Cohen J.C.
      J. Lipid Res. 40:178-182(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), CATALYTIC ACTIVITY.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS MITOCHONDRIAL AND CYTOPLASMIC+PEROXISOMAL).
      Tissue: Eye and Lung.
    6. Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "Malonyl CoenzymeA decarboxylase regulates lipid and glucose metabolism in human skeletal muscle."
      Bouzakri K., Austin R., Rune A., Lassman M.E., Garcia-Roves P.M., Berger J.P., Krook A., Chibalin A.V., Zhang B.B., Zierath J.R.
      Diabetes 57:1508-1516(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. "A proteome-wide perspective on peroxisome targeting signal 1(PTS1)-Pex5p affinities."
      Ghosh D., Berg J.M.
      J. Am. Chem. Soc. 132:3973-3979(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH PEX5.
    9. "Structural asymmetry and disulphide bridges among subunits modulate the activity of human Malonyl-CoA Decarboxylase."
      Aparicio D., Perez R., Carpena X., Diaz M., Ferrer J.C., Loewen P.C., Fita I.
      J. Biol. Chem. 288:11907-11919(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 39-493 IN COMPLEX WITH LIGAND REPRESENTING COENZYME A, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-206; CYS-243 AND GLU-302, IDENTIFICATION BY MASS SPECTROMETRY.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 40-490, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-290; SER-329; HIS-423 AND TYR-456.

    Entry informationi

    Entry nameiDCMC_HUMAN
    AccessioniPrimary (citable) accession number: O95822
    Secondary accession number(s): Q9UNU5, Q9Y3F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 1, 2000
    Last modified: July 22, 2015
    This is version 137 of the entry and version 3 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.