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Q920F5

- DCMC_RAT

UniProt

Q920F5 - DCMC_RAT

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Protein
Malonyl-CoA decarboxylase, mitochondrial
Gene
Mlycd
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.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
Binding sitei328 – 3281Malonyl-CoA By similarity
Binding sitei422 – 4221Malonyl-CoA By 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
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

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. Mitochondrion matrix. Peroxisome By similarity. Peroxisome matrix
Note: Enzymatically active in all three subcellular compartments.2 Publications

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 492Malonyl-CoA decarboxylase, mitochondrialPRO_0000021092
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581N6-acetyllysine By similarity
Modified residuei167 – 1671N6-acetyllysine; alternate By similarity
Modified residuei167 – 1671N6-succinyllysine; alternate By similarity
Disulfide bondi205 – 205Interchain Reviewed prediction
Modified residuei210 – 2101N6-acetyllysine By similarity
Modified residuei221 – 2211N6-succinyllysine By similarity
Modified residuei316 – 3161N6-acetyllysine By similarity
Modified residuei385 – 3851N6-acetyllysine; alternate By similarity
Modified residuei385 – 3851N6-succinyllysine; alternate By similarity
Modified residuei388 – 3881N6-acetyllysine By similarity
Modified residuei441 – 4411N6-acetyllysine By similarity
Modified residuei471 – 4711N6-acetyllysine By 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.
Interchain disulfide bonds may form in peroxisomes Reviewed prediction. Interchain disulfide bonds are not expected to form in the reducing environment of the cytoplasm and mitochondria.

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.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019923.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni298 – 3047Malonyl-CoA binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi490 – 4923Microbody targeting signal Reviewed prediction

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).

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838Missing in isoform Cytoplasmic+peroxisomal.
VSP_018818Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131E → D in CAB46681. 1 Publication
Sequence conflicti218 – 2181H → Q in CAB46681. 1 Publication
Sequence conflicti301 – 3011E → G in CAB46681. 1 Publication
Sequence conflicti412 – 4121Missing in CAB46681. 1 Publication

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

« Hide 'large scale' publications
  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.

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: April 16, 2014
This is version 82 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

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