Tag | Content |
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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 |
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145 | GLFHHISKLDGGVRF | acetylation | [1] | 167 | LLEAQALKLVEGPHV | acetylation | [1] | 312 | FLIKRVVKELQKEFP | acetylation | [1] | 385 | LSSGEWAKSEKLAQA | acetylation | [1] | 471 | SISYLGSKNIKASEQ | acetylation | [1] |
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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. |
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