CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018626
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Malonyl-CoA decarboxylase, mitochondrial 
Protein Synonyms/Alias
 MCD 
Gene Name
 Mlycd 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
145GLFHHISKLDGGVRFacetylation[1]
167LLEAQALKLVEGPHVacetylation[1]
312FLIKRVVKELQKEFPacetylation[1]
385LSSGEWAKSEKLAQAacetylation[1]
471SISYLGSKNIKASEQacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 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. 
Sequence Annotation
 REGION 298 304 Malonyl-CoA binding (By similarity).
 MOTIF 490 492 Microbody targeting signal (Potential).
 BINDING 328 328 Malonyl-CoA (By similarity).
 BINDING 422 422 Malonyl-CoA (By similarity).
 DISULFID 205 205 Interchain (Potential).  
Keyword
 Alternative initiation; Complete proteome; Cytoplasm; Decarboxylase; Direct protein sequencing; Disulfide bond; Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Lyase; Mitochondrion; Peroxisome; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 492 AA 
Protein Sequence
MRGLGPSLRA RRLLPLRYPP RPPGPRGPRL CSGLTASAMD ELLRRAVPPT PAYELREKTP 60
APAEGQCADF VSFYGGLAEA AQRAELLGRL AQGFGVDHGQ VAEQSAGVLQ LRQQSREAAV 120
LLQAEDRLRY ALVPRYRGLF HHISKLDGGV RFLVQLRADL LEAQALKLVE GPHVREMNGV 180
LKSMLSEWFS SGFLNLERVT WHSPCEVLQK ISECEAVHPV KNWMDMKRRV GPYRRCYFFS 240
HCSTPGDPLV VLHVALTGDI SNNIQSIVKE CPPSETEEKN RIAAAVFYSI SLTQQGLQGV 300
ELGTFLIKRV VKELQKEFPH LGAFSSLSPI PGFTKWLLGL LNVQGKEYGR NELFTDSECK 360
EIAEVTGDPV HESLKGLLSS GEWAKSEKLA QALQGPLMRL CAWYLYGEKH RGYALNPVAN 420
FHLQNGAVMW RINWMADSSL KGLTSSCGLM VNYRYYLEET GPNSISYLGS KNIKASEQIL 480
SLVAQFQSNS KL 492 
Gene Ontology
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0005739; C:mitochondrion; IDA:RGD.
 GO:0005777; C:peroxisome; IDA:RGD.
 GO:0050080; F:malonyl-CoA decarboxylase activity; IDA:RGD.
 GO:0006085; P:acetyl-CoA biosynthetic process; IDA:RGD.
 GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
 GO:0019395; P:fatty acid oxidation; IDA:RGD.
 GO:2001294; P:malonyl-CoA catabolic process; IEA:Compara.
 GO:0046321; P:positive regulation of fatty acid oxidation; IEA:Compara.
 GO:0031998; P:regulation of fatty acid beta-oxidation; IDA:RGD.
 GO:0010906; P:regulation of glucose metabolic process; IEA:Compara. 
Interpro
 IPR007956; Malonyl_CoA_deC. 
Pfam
 PF05292; MCD 
SMART
  
PROSITE
  
PRINTS