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Q99J39

- DCMC_MOUSE

UniProt

Q99J39 - DCMC_MOUSE

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Protein

Malonyl-CoA decarboxylase, mitochondrial

Gene
Mlycd
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. Plays a role in controlling the extent of ischemic injury by promoting glucose oxidation.2 Publications

Catalytic activityi

Malonyl-CoA = acetyl-CoA + CO2.1 Publication

Enzyme regulationi

Malonyl-CoA decarboxylase activity does not require any cofactors or divalent metal ions By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei328 – 3281Malonyl-CoA By similarity
Binding sitei422 – 4221Malonyl-CoA By similarity

GO - Molecular functioni

  1. malonyl-CoA decarboxylase activity Source: UniProtKB
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. acetyl-CoA biosynthetic process Source: UniProtKB
  2. fatty acid biosynthetic process Source: UniProtKB
  3. fatty acid oxidation Source: Ensembl
  4. malonyl-CoA catabolic process Source: UniProtKB
  5. positive regulation of fatty acid oxidation Source: UniProtKB
  6. regulation of fatty acid beta-oxidation Source: Ensembl
  7. regulation of glucose metabolic process Source: UniProtKB
  8. response to ischemia Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00340; UER00710.

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl-CoA decarboxylase, mitochondrial (EC:4.1.1.9)
Short name:
MCD
Gene namesi
Name:Mlycd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1928485. Mlycd.

Subcellular locationi

Cytoplasm By similarity. Mitochondrion matrix. Peroxisome By similarity. Peroxisome matrix By similarity
Note: Enzymatically active in all three subcellular compartments By similarity.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Ensembl
  3. mitochondrial matrix Source: UniProtKB
  4. mitochondrion Source: MGI
  5. peroxisomal matrix Source: UniProtKB
  6. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

Pathology & Biotechi

Disruption phenotypei

Mice show an increased expression of genes regulating fatty acid utilization and likely contributes to the absence of changes in energy metabolism in the aerobic heart. Display a preference for glucose utilization after ischemia and improve functional recovery of the heart.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi471 – 4711K → Q: Mimicks constitutive acetylation, leading to increased malonyl-CoA decarboxylase activity. 1 Publication
Mutagenesisi471 – 4711K → R: Decreased acetylation, leading to reduced malonyl-CoA decarboxylase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 492Malonyl-CoA decarboxylase, mitochondrialPRO_0000021090
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581N6-acetyllysine1 Publication
Modified residuei167 – 1671N6-acetyllysine; alternate1 Publication
Modified residuei167 – 1671N6-succinyllysine; alternate1 Publication
Disulfide bondi205 – 205Interchain Reviewed prediction
Modified residuei210 – 2101N6-acetyllysine1 Publication
Modified residuei221 – 2211N6-succinyllysine1 Publication
Modified residuei316 – 3161N6-acetyllysine1 Publication
Modified residuei385 – 3851N6-acetyllysine; alternate1 Publication
Modified residuei385 – 3851N6-succinyllysine; alternate1 Publication
Modified residuei388 – 3881N6-acetyllysine1 Publication
Modified residuei441 – 4411N6-acetyllysine1 Publication
Modified residuei471 – 4711N6-acetyllysine1 Publication

Post-translational modificationi

Interchain disulfide bonds may form in peroxisomes Reviewed prediction. Interchain disulfide bonds are not expected to form in the reducing environment of the cytoplasm and mitochondria.
Acetylation at Lys-471 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-471 by SIRT4 represses activity, leading to promote lipogenesis.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiQ99J39.
PaxDbiQ99J39.
PRIDEiQ99J39.

PTM databases

PhosphoSiteiQ99J39.

Expressioni

Gene expression databases

BgeeiQ99J39.
CleanExiMM_MLYCD.
GenevestigatoriQ99J39.

Interactioni

Subunit structurei

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). Associates with the peroxisomal targeting signal receptor PEX5 By similarity.

Protein-protein interaction databases

MINTiMINT-1861916.

Structurei

3D structure databases

ProteinModelPortaliQ99J39.
SMRiQ99J39. Positions 38-492.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni298 – 3047Malonyl-CoA binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi490 – 4923Microbody targeting signal Reviewed prediction

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1593.
GeneTreeiENSGT00390000005410.
HOGENOMiHOG000141409.
HOVERGENiHBG000825.
InParanoidiQ99J39.
KOiK01578.
OMAiLDEGREQ.
OrthoDBiEOG76X5ZZ.
PhylomeDBiQ99J39.
TreeFamiTF312959.

Family and domain databases

InterProiIPR007956. Malonyl_CoA_deC.
[Graphical view]
PfamiPF05292. MCD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Note: A single transcription start site has been demonstrated in Rat.

Isoform Mitochondrial (identifier: Q99J39-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MRGLGPGLRA RRLLPLRSPP RPPGPRGRRL CGGLAASAMD ELLRRAVPPT    50
PAYELREKTP APAEGQCADF VSFYGGLAEA SQRAELLGRL AQGFGVDHGQ 100
VAEQSAGVLQ LRQQAREAAV LLQAEDRLRY ALVPRYRGLF HHISKLDGGV 150
RFLVQLRADL LEAQALKLVE GPHVREMNGV LKSMLSEWFS SGFLNLERVT 200
WHSPCEVLQK ISECEAVHPV KNWMDMKRRV GPYRRCYFFS HCSTPGEPLV 250
VLHVALTGDI SNNIQGIVKE CPPTETEERN RIAAAIFYSI SLTQQGLQGV 300
ELGTFLIKRV VKELQKEFPQ LGAFSSLSPI PGFTKWLLGL LNVQGKEHGR 350
NELFTDSECQ EISAVTGNPV HESLKGFLSS GEWVKSEKLT QALQGPLMRL 400
CAWYLYGEKH RGYALNPVAN FHLQNGAVMW RINWMADSSL KGLTSSCGLM 450
VNYRYYLEET GPNSISYLGS KNIKASEQIL SLVAQFQNNS KL 492
Length:492
Mass (Da):54,736
Last modified:June 1, 2001 - v1
Checksum:iCEBDA62714A21DC1
GO
Isoform Cytoplasmic+peroxisomal (identifier: Q99J39-2) [UniParc]FASTAAdd to Basket

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

Note: May be produced by alternative initiation at Met-39 of isoform mitochondrial. Alternatively, represents a proteolytic processed form of the mitochondrial form.

Show »
Length:454
Mass (Da):50,766
Checksum:i233693B9C1BF74CA
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838Missing in isoform Cytoplasmic+peroxisomal. VSP_018817Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK082479 mRNA. Translation: BAC38505.1.
BC004764 mRNA. Translation: AAH04764.1.
AY331094 Genomic DNA. Translation: AAP93335.2.
CCDSiCCDS22703.1. [Q99J39-1]
RefSeqiNP_064350.2. NM_019966.2. [Q99J39-1]
UniGeneiMm.423037.

Genome annotation databases

EnsembliENSMUST00000098367; ENSMUSP00000095970; ENSMUSG00000074064. [Q99J39-1]
GeneIDi56690.
KEGGimmu:56690.
UCSCiuc009npn.1. mouse. [Q99J39-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK082479 mRNA. Translation: BAC38505.1 .
BC004764 mRNA. Translation: AAH04764.1 .
AY331094 Genomic DNA. Translation: AAP93335.2 .
CCDSi CCDS22703.1. [Q99J39-1 ]
RefSeqi NP_064350.2. NM_019966.2. [Q99J39-1 ]
UniGenei Mm.423037.

3D structure databases

ProteinModelPortali Q99J39.
SMRi Q99J39. Positions 38-492.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1861916.

Chemistry

BindingDBi Q99J39.
ChEMBLi CHEMBL1255162.

PTM databases

PhosphoSitei Q99J39.

Proteomic databases

MaxQBi Q99J39.
PaxDbi Q99J39.
PRIDEi Q99J39.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000098367 ; ENSMUSP00000095970 ; ENSMUSG00000074064 . [Q99J39-1 ]
GeneIDi 56690.
KEGGi mmu:56690.
UCSCi uc009npn.1. mouse. [Q99J39-1 ]

Organism-specific databases

CTDi 23417.
MGIi MGI:1928485. Mlycd.

Phylogenomic databases

eggNOGi COG1593.
GeneTreei ENSGT00390000005410.
HOGENOMi HOG000141409.
HOVERGENi HBG000825.
InParanoidi Q99J39.
KOi K01578.
OMAi LDEGREQ.
OrthoDBi EOG76X5ZZ.
PhylomeDBi Q99J39.
TreeFami TF312959.

Enzyme and pathway databases

UniPathwayi UPA00340 ; UER00710 .

Miscellaneous databases

NextBioi 313103.
PROi Q99J39.
SOURCEi Search...

Gene expression databases

Bgeei Q99J39.
CleanExi MM_MLYCD.
Genevestigatori Q99J39.

Family and domain databases

InterProi IPR007956. Malonyl_CoA_deC.
[Graphical view ]
Pfami PF05292. MCD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
  4. "Absence of malonyl coenzyme A decarboxylase in mice increases cardiac glucose oxidation and protects the heart from ischemic injury."
    Dyck J.R., Hopkins T.A., Bonnet S., Michelakis E.D., Young M.E., Watanabe M., Kawase Y., Jishage K., Lopaschuk G.D.
    Circulation 114:1721-1728(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
  5. Cited for: FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-58; LYS-167; LYS-210; LYS-316; LYS-388; LYS-441 AND LYS-471, MUTAGENESIS OF LYS-471.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-167; LYS-221 AND LYS-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDCMC_MOUSE
AccessioniPrimary (citable) accession number: Q99J39
Secondary accession number(s): Q7TNL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

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