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Q99J39 (DCMC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Subcellular location

Mitochondrion. Cytoplasm. Peroxisome.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Mitochondrial (identifier: Q99J39-1)

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: Q99J39-2)

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_0000021090

Regions

Motif490 – 4923Microbody targeting signal Potential

Natural variations

Alternative sequence1 – 3838Missing in isoform Cytoplasmic+peroxisomal.
VSP_018817

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: CEBDA62714A21DC1

FASTA49254,736
        10         20         30         40         50         60 
MRGLGPGLRA RRLLPLRSPP RPPGPRGRRL CGGLAASAMD ELLRRAVPPT PAYELREKTP 

        70         80         90        100        110        120 
APAEGQCADF VSFYGGLAEA SQRAELLGRL AQGFGVDHGQ VAEQSAGVLQ LRQQAREAAV 

       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 
HCSTPGEPLV VLHVALTGDI SNNIQGIVKE CPPTETEERN RIAAAIFYSI SLTQQGLQGV 

       310        320        330        340        350        360 
ELGTFLIKRV VKELQKEFPQ LGAFSSLSPI PGFTKWLLGL LNVQGKEHGR NELFTDSECQ 

       370        380        390        400        410        420 
EISAVTGNPV HESLKGFLSS GEWVKSEKLT QALQGPLMRL CAWYLYGEKH RGYALNPVAN 

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

       490 
SLVAQFQNNS KL 

« Hide

Isoform Cytoplasmic+peroxisomal [UniParc].

Checksum: 233693B9C1BF74CA
Show »

FASTA45450,766

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum.
[2]"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].
Strain: 129, C57BL/6J and FVB/N.
Tissue: Mammary tumor.
[3]"Mouse malonyl-CoA decarboxylase: genome structure, cDNA cloning, expression and promoter study."
Kim N.H., Lee G.Y., Kim Y.S.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-175.
Strain: 129S6/SvEvTac.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK082479 mRNA. Translation: BAC38505.1.
BC004764 mRNA. Translation: AAH04764.1.
AY331094 Genomic DNA. Translation: AAP93335.2.
IPIIPI00114866.
IPI00759857.
RefSeqNP_064350.2. NM_019966.2.
UniGeneMm.423037.

3D structure databases

ProteinModelPortalQ99J39.
SMRQ99J39. Positions 38-486.
ModBaseSearch...

PTM databases

PhosphoSiteQ99J39.

Proteomic databases

PaxDbQ99J39.
PRIDEQ99J39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000098367; ENSMUSP00000095970; ENSMUSG00000074064.
GeneID56690.
KEGGmmu:56690.
UCSCuc009npn.1. mouse.

Organism-specific databases

CTD23417.
MGIMGI:1928485. Mlycd.

Phylogenomic databases

eggNOGCOG1593.
GeneTreeENSGT00390000005410.
HOGENOMHOG000141409.
HOVERGENHBG000825.
InParanoidQ99J39.
KOK01578.
OMAAPADRRC.
OrthoDBEOG4RBQJF.

Enzyme and pathway databases

UniPathwayUPA00340; UER00710.

Gene expression databases

BgeeQ99J39.
CleanExMM_MLYCD.
GenevestigatorQ99J39.
GermOnlineENSMUSG00000074064. Mus musculus.

Family and domain databases

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

Other

BindingDBQ99J39.
ChEMBLCHEMBL1255162.
NextBio313103.
SOURCESearch...

Entry information

Entry nameDCMC_MOUSE
AccessionPrimary (citable) accession number: Q99J39
Secondary accession number(s): Q7TNL6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2001
Last modified: April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways