P12617 (DCMC_ANSAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 67.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Malonyl-CoA decarboxylase, mitochondrial Short name=MCD EC=4.1.1.9 | ||
| Gene names |
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| Organism | Anser anser anser (Western graylag goose) | ||
| Taxonomic identifier | 8844 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anser ›  |
Protein attributes
| Sequence length | 504 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. |
| Catalytic activity | Malonyl-CoA = acetyl-CoA + CO2. |
| Pathway | Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from malonyl-CoA: step 1/1. |
| Subcellular location | Mitochondrion. Cytoplasm. Peroxisome. Note: Mitochondrial in liver. Cytoplasmic in uropygial gland. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism |
| Cellular component | Cytoplasm Mitochondrion Peroxisome |
| Coding sequence diversity | Alternative initiation |
| Domain | Transit peptide |
| Molecular function | Decarboxylase Lyase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | acetyl-CoA biosynthetic process Inferred from sequence or structural similarity PubMed 9869665. Source: UniProtKB fatty acid biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisomeInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | malonyl-CoA decarboxylase activity Inferred from sequence or structural similarity PubMed 10455107PubMed 9869665. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative initiation. [Align] [Select] | ||||||
| Isoform Mitochondrial (identifier: P12617-1) 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. | ||||||
| Isoform Cytoplasmic+peroxisomal (identifier: P12617-2) The sequence of this isoform differs from the canonical sequence as follows: 1-50: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 504 | Malonyl-CoA decarboxylase, mitochondrial | PRO_0000021086 | ||||||
Regions | |||||||||
| Motif | 502 – 504 | 3 | Microbody targeting signal Potential | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 50 | 50 | Missing in isoform Cytoplasmic+peroxisomal. | VSP_018815 | |||||
Experimental info | |||||||||
| Sequence conflict | 124 – 136 | 13 | Missing AA sequence Ref.2 | ||||||
| Sequence conflict | 140 | 1 | V → L in AAA49317. Ref.2 | ||||||
Sequences
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References
| [1] | "Cytoplasmic accumulation of a normally mitochondrial malonyl-CoA decarboxylase by the use of an alternate transcription start site." Courchesne-Smith C., Jang S.-H., Shi Q., Dewille J., Sasaki G., Kolattukudy P.E. Arch. Biochem. Biophys. 298:576-586(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Uropygial gland. |
| [2] | "Molecular cloning, nucleotide sequence, and tissue distribution of malonyl-CoA decarboxylase." Jang S.-H., Cheesbrough T.M., Kolattukudy P.E. J. Biol. Chem. 264:3500-3505(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-504, PARTIAL PROTEIN SEQUENCE. Tissue: Uropygial gland. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L21171 mRNA. Translation: AAA49317.1. Sequence problems. |
| PIR | A33313. S27113. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG000825. |
Enzyme and pathway databases | |
| UniPathway | UPA00340; UER00710. |
Family and domain databases | |
| InterPro | IPR007956. Malonyl_CoA_deC. [Graphical view] |
| Pfam | PF05292. MCD. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DCMC_ANSAN | ||||||||
| Accession | Primary (citable) accession number: P12617 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |