O95822 (DCMC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malonyl-CoA decarboxylase, mitochondrial
Short name=MCD
EC=4.1.1.9

Gene names

Name:

MLYCD

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	493 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. 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.
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.
Involvement in disease	Defects in MLYCD are the cause of malonyl-CoA decarboxylase deficiency (MLYCD deficiency) [MIM:248360]. MLYCD deficiency is an autosomal recessive disease characterized by abdominal pain, chronic constipation, episodic vomiting, metabolic acidosis and malonic aciduria.
Sequence caution	The sequence AAD16177.2 differs from that shown. Reason: Frameshift at positions 23, 28, 297 and 308. The sequence AAD34631.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm Mitochondrion Peroxisome
Domain	Transit peptide
Molecular function	Decarboxylase Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	malonyl-CoA decarboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion
	Chain	? – 493		Malonyl-CoA decarboxylase, mitochondrial		PRO_0000021088
Regions
	Motif	491 – 493	3	Microbody targeting signal Potential
Amino acid modifications
	Modified residue	387	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	82	1	A → D in AAD16177. Ref.5
	Sequence conflict	119	1	A → S in AAD48994. Ref.1
	Sequence conflict	127	1	D → V in AAD48994. Ref.1
	Sequence conflict	192	1	S → P in AAD34631. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O95822 [UniParc]. Last modified December 1, 2000. Version 3. Checksum: 8F061CA38908E8FC	FASTA	493	55,003
	10 20 30 40 50 60 MRGFGPGLTA RRLLPLRLPP RPPGPRLASG QAAGALERAM DELLRRAVPP TPAYELREKT 70 80 90 100 110 120 PAPAEGQCAD FVSFYGGLAE TAQRAELLGR LARGFGVDHG QVAEQSAGVL HLRQQQREAA 130 140 150 160 170 180 VLLQAEDRLR YALVPRYRGL FHHISKLDGG VRFLVQLRAD LLEAQALKLV EGPDVREMNG 190 200 210 220 230 240 VLKGMLSEWF SSGFLNLERV TWHSPCEVLQ KISEAEAVHP VKNWMDMKRR VGPYRRCYFF 250 260 270 280 290 300 SHCSTPGEPL VVLHVALTGD ISSNIQAIVK EHPPSETEEK NKITAAIFYS ISLTQQGLQG 310 320 330 340 350 360 VELGTFLIKR VVKELQREFP HLGVFSSLSP IPGFTKWLLG LLNSQTKEHG RNELFTDSEC 370 380 390 400 410 420 KEISEITGGP INETLKLLLS SSEWVQSEKL VRALQTPLMR LCAWYLYGEK HRGYALNPVA 430 440 450 460 470 480 NFHLQNGAVL WRINWMADVS LRGITGSCGL MANYRYFLEE TGPNSTSYLG SKIIKASEQV 490 LSLVAQFQKN SKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and mutational analysis of human malonyl-coenzyme A decarboxylase." Gao J., Waber L., Bennett M.J., Gibson K.M., Cohen J.C. J. Lipid Res. 40:178-182(1999) [PubMed: 9869665] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA decarboxylase and is mutated in malonyl-CoA decarboxylase deficiency." Sacksteder K.A., Morrell J.C., Wanders R.J.A., Matalon R., Gould S.J. J. Biol. Chem. 274:24461-24468(1999) [PubMed: 10455107] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-493.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-493. Tissue: Eye and Lung.
[5]	"The molecular basis of malonyl-CoA decarboxylase deficiency." FitzPatrick D.R., Hill A., Tolmie J.L., Thorburn D.R., Christodoulou J. Am. J. Hum. Genet. 65:318-326(1999) [PubMed: 10417274] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-493.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF090834 mRNA. Translation: AAD48994.1. BC000286 mRNA. Translation: AAH00286.1. BC052592 mRNA. Translation: AAH52592.1. AF153679 mRNA. Translation: AAD34631.1. Different initiation. AF097832 mRNA. Translation: AAD16177.2. Frameshift.
IPI	IPI00000663. IPI00759655.
RefSeq	NP_036345.2. NM_012213.2.
UniGene	Hs.644610.
3D structure databases
ProteinModelPortal	O95822.
ModBase	Search...
Protein-protein interaction databases
STRING	O95822.
PTM databases
PhosphoSite	O95822.
Proteomic databases
PRIDE	O95822.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262430; ENSP00000262430; ENSG00000103150.
GeneID	23417.
KEGG	hsa:23417.
UCSC	uc002fgz.1. human.
Organism-specific databases
CTD	23417.
GeneCards	GC16P083932.
H-InvDB	HIX0013284.
HGNC	HGNC:7150. MLYCD.
HPA	HPA031625.
MIM	248360. phenotype. 606761. gene.
neXtProt	NX_O95822.
Orphanet	943. Malonic aciduria.
PharmGKB	PA30861.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11770.
GeneTree	ENSGT00390000005410.
HOGENOM	HBG602644.
HOVERGEN	HBG000825.
InParanoid	O95822.
OMA	GRNELFT.
OrthoDB	EOG4RBQJF.
PhylomeDB	O95822.
Gene expression databases
ArrayExpress	O95822.
Bgee	O95822.
CleanEx	HS_MLYCD.
Genevestigator	O95822.
GermOnline	ENSG00000103150. Homo sapiens.
Family and domain databases
InterPro	IPR007956. Malonyl_CoA_deC. [Graphical view]
KO	K01578.
Pfam	PF05292. MCD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	45627.
SOURCE	Search...

Entry information

Entry name

DCMC_HUMAN

Accession

Primary (citable) accession number: O95822
Secondary accession number(s): Q9UNU5, Q9Y3F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.