Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q920F5 (DCMC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malonyl-CoA decarboxylase, mitochondrial

Short name=MCD
EC=4.1.1.9
Gene names
Name:Mlycd
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

Malonyl-CoA = acetyl-CoA + CO2.

Pathway

Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from malonyl-CoA: step 1/1.

Subunit structure

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) By similarity.

Subcellular location

Mitochondrion. Cytoplasm. Peroxisome.

Post-translational modification

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.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Mitochondrial (identifier: Q920F5-1)

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: Q920F5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 492Malonyl-CoA decarboxylase, mitochondrialPRO_0000021092

Regions

Region298 – 3047Malonyl-CoA binding By similarity
Motif490 – 4923Microbody targeting signal Potential

Sites

Binding site3281Malonyl-CoA By similarity
Binding site4221Malonyl-CoA By similarity

Amino acid modifications

Disulfide bond205Interchain Potential

Natural variations

Alternative sequence1 – 3838Missing in isoform Cytoplasmic+peroxisomal.
VSP_018818

Experimental info

Sequence conflict2131E → D in CAB46681. Ref.1
Sequence conflict2181H → Q in CAB46681. Ref.1
Sequence conflict3011E → G in CAB46681. Ref.1
Sequence conflict4121Missing in CAB46681. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Mitochondrial [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: D1FB65533B5A582E

FASTA49254,762
        10         20         30         40         50         60 
MRGLGPSLRA RRLLPLRYPP RPPGPRGPRL CSGLTASAMD ELLRRAVPPT PAYELREKTP 

        70         80         90        100        110        120 
APAEGQCADF VSFYGGLAEA AQRAELLGRL AQGFGVDHGQ VAEQSAGVLQ LRQQSREAAV 

       130        140        150        160        170        180 
LLQAEDRLRY ALVPRYRGLF HHISKLDGGV RFLVQLRADL LEAQALKLVE GPHVREMNGV 

       190        200        210        220        230        240 
LKSMLSEWFS SGFLNLERVT WHSPCEVLQK ISECEAVHPV KNWMDMKRRV GPYRRCYFFS 

       250        260        270        280        290        300 
HCSTPGDPLV VLHVALTGDI SNNIQSIVKE CPPSETEEKN RIAAAVFYSI SLTQQGLQGV 

       310        320        330        340        350        360 
ELGTFLIKRV VKELQKEFPH LGAFSSLSPI PGFTKWLLGL LNVQGKEYGR NELFTDSECK 

       370        380        390        400        410        420 
EIAEVTGDPV HESLKGLLSS GEWAKSEKLA QALQGPLMRL CAWYLYGEKH RGYALNPVAN 

       430        440        450        460        470        480 
FHLQNGAVMW RINWMADSSL KGLTSSCGLM VNYRYYLEET GPNSISYLGS KNIKASEQIL 

       490 
SLVAQFQSNS KL 

« Hide

Isoform Cytoplasmic+peroxisomal [UniParc].

Checksum: 92D3679A358E332B
Show »

FASTA45450,685

References

« Hide 'large scale' references
[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].
[2]Lee G.-Y., Kim Y.-S.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[3]"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].
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007704 mRNA. Translation: CAB46681.1.
AF304865 mRNA. Translation: AAL09352.1.
BC061845 mRNA. Translation: AAH61845.1.
IPIIPI00200489.
IPI00760151.
RefSeqNP_445929.1. NM_053477.1.
UniGeneRn.13468.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000019923.

PTM databases

PhosphoSiteQ920F5.

Proteomic databases

PaxDbQ920F5.
PRIDEQ920F5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019923; ENSRNOP00000019923; ENSRNOG00000014522.
GeneID85239.
KEGGrno:85239.
UCSCRGD:620234. rat.

Organism-specific databases

CTD23417.
RGD620234. Mlycd.

Phylogenomic databases

eggNOGCOG1593.
GeneTreeENSGT00390000005410.
HOGENOMHOG000141409.
HOVERGENHBG000825.
InParanoidQ920F5.
KOK01578.
OMAAPADRRC.
OrthoDBEOG4RBQJF.

Enzyme and pathway databases

SABIO-RKQ920F5.
UniPathwayUPA00340; UER00710.

Gene expression databases

ArrayExpressQ920F5.
GenevestigatorQ920F5.
GermOnlineENSRNOG00000014522. Rattus norvegicus.

Family and domain databases

InterProIPR007956. Malonyl_CoA_deC.
[Graphical view]
PfamPF05292. MCD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio617288.

Entry information

Entry nameDCMC_RAT
AccessionPrimary (citable) accession number: Q920F5
Secondary accession number(s): Q9WUY2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 1, 2001
Last modified: May 29, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways