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Entry version 182 (23 Feb 2022)
Sequence version 3 (01 Dec 2000)
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Protein

Malonyl-CoA decarboxylase, mitochondrial

Gene

MLYCD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation.

4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Malonyl-CoA decarboxylase activity does not require any cofactors or divalent metal ions. Formation of interchain disulfide bonds leads to positive cooperativity between active sites and increases the affinity for malonyl-CoA and the catalytic efficiency (in vitro).2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 19 sec(-1) with malonyl-CoA for malonyl-CoA decarboxylase mitochondrial form (PubMed:15003260). kcat is 28 sec(-1) with malonyl-CoA for Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form (PubMed:15003260). The catalytic efficiency for malonyl-CoA is at least 1.09-fold higher with the malonyl-CoA decarboxylase cytoplasmic+peroxisomal form (PubMed:15003260).1 Publication
  1. KM=0.36 mM for malonyl-CoA (Malonyl-CoA decarboxylase mitochondrial form)1 Publication
  2. KM=0.83 mM for malonyl-CoA (Malonyl-CoA decarboxylase mitochondrial form)1 Publication
  3. KM=0.22 mM for malonyl-CoA (Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form)1 Publication
  4. KM=0.33 mM for malonyl-CoA (Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: acetyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes acetyl-CoA from malonyl-CoA. This subpathway is part of the pathway acetyl-CoA biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from malonyl-CoA, the pathway acetyl-CoA biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei211Essential for catalytic activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei329Proton acceptor1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei329Malonyl-CoACurated1
Active sitei423Proton donor1 Publication1
Binding sitei423Malonyl-CoACurated1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.1.9, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
O95822

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-390247, Beta-oxidation of very long chain fatty acids [O95822-2]
R-HSA-9033241, Peroxisomal protein import [O95822-2]

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O95822

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
O95822

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00340;UER00710

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000251

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Malonyl-CoA decarboxylase, mitochondrialCurated (EC:4.1.1.95 Publications)
Short name:
MCD
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MLYCDImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:7150, MLYCD

Online Mendelian Inheritance in Man (OMIM)

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MIMi
606761, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O95822

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000103150

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Malonyl-CoA decarboxylase deficiency (MLYCD deficiency)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAutosomal recessive disease characterized by abdominal pain, chronic constipation, episodic vomiting, metabolic acidosis and malonic aciduria.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi206C → S: Abolishes formation of disulfide-linked homotetramers. Abolishes the cooperative enzyme kinetics that are seen under oxidative conditions. 1 Publication1
Mutagenesisi243C → S: Does not abolish formation of disulfide-linked homotetramers. No effect on development of cooperative enzyme kinetics in response to oxidative conditions. 1 Publication1
Mutagenesisi290S → F: 2-fold reduction in catalytic activity. 1 Publication1
Mutagenesisi302E → G: Decreases catalytic activity. Increases affinity for malonyl-CoA. 1 Publication1
Mutagenesisi329S → A: 110-fold reduction in catalytic activity. 1 Publication1
Mutagenesisi423H → N: 7-fold reduction in catalytic activity. 1 Publication1
Mutagenesisi456Y → S: 3.5-fold reduction in catalytic activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
23417

MalaCards human disease database

More...
MalaCardsi
MLYCD
MIMi248360, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000103150

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
943, Malonic aciduria

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA30861

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
O95822, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4698

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1275

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
MLYCD

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 39MitochondrionSequence analysisAdd BLAST39
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002108840 – 493Malonyl-CoA decarboxylase, mitochondrialAdd BLAST454

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei59N6-acetyllysineBy similarity1
Modified residuei168N6-acetyllysine; alternateBy similarity1
Modified residuei168N6-succinyllysine; alternateBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi206InterchainSequence analysis
Modified residuei211N6-acetyllysineBy similarity1
Modified residuei222N6-succinyllysineBy similarity1
Modified residuei389N6-acetyllysineBy similarity1
Modified residuei472N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylation at Lys-472 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-472 by SIRT4 represses activity, leading to promote lipogenesis (By similarity).By similarity
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.Curated

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O95822

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O95822

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
O95822

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O95822

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O95822

PeptideAtlas

More...
PeptideAtlasi
O95822

PRoteomics IDEntifications database

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PRIDEi
O95822

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
51071 [O95822-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O95822

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O95822

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in fibroblasts and hepatoblastoma cells (at protein level). Expressed strongly in heart, liver, skeletal muscle, kidney and pancreas. Expressed in myotubes. Expressed weakly in brain, placenta, spleen, thymus, testis, ovary and small intestine.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000103150, Expressed in heart left ventricle and 201 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O95822, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O95822, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000103150, Tissue enhanced (tongue)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
116989, 26 interactors

Database of interacting proteins

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DIPi
DIP-60405N

Protein interaction database and analysis system

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IntActi
O95822, 17 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000262430

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O95822

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
O95822, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O95822

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni40 – 190Alpha-helical domainAdd BLAST151
Regioni191 – 493Catalytic domainAdd BLAST303
Regioni299 – 305Malonyl-CoA bindingCurated7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi491 – 493Microbody targeting signalSequence analysis3

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3018, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00390000005410

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_023433_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O95822

Identification of Orthologs from Complete Genome Data

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OMAi
PIDWSTP

Database of Orthologous Groups

More...
OrthoDBi
1436590at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O95822

TreeFam database of animal gene trees

More...
TreeFami
TF312959

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.140.90, 1 hit
3.40.630.150, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR038917, Malonyl_CoA_deC
IPR007956, Malonyl_CoA_deC_C
IPR042303, Malonyl_CoA_deC_C_sf
IPR035372, MCD_N
IPR038351, MCD_N_sf

The PANTHER Classification System

More...
PANTHERi
PTHR28641, PTHR28641, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05292, MCD, 1 hit
PF17408, MCD_N, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Note: A single transcription start site has been demonstrated in Rat.

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform Mitochondrial (identifier: O95822-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
        10         20         30         40         50
MRGFGPGLTA RRLLPLRLPP RPPGPRLASG QAAGALERAM DELLRRAVPP
60 70 80 90 100
TPAYELREKT PAPAEGQCAD FVSFYGGLAE TAQRAELLGR LARGFGVDHG
110 120 130 140 150
QVAEQSAGVL HLRQQQREAA VLLQAEDRLR YALVPRYRGL FHHISKLDGG
160 170 180 190 200
VRFLVQLRAD LLEAQALKLV EGPDVREMNG VLKGMLSEWF SSGFLNLERV
210 220 230 240 250
TWHSPCEVLQ KISEAEAVHP VKNWMDMKRR VGPYRRCYFF SHCSTPGEPL
260 270 280 290 300
VVLHVALTGD ISSNIQAIVK EHPPSETEEK NKITAAIFYS ISLTQQGLQG
310 320 330 340 350
VELGTFLIKR VVKELQREFP HLGVFSSLSP IPGFTKWLLG LLNSQTKEHG
360 370 380 390 400
RNELFTDSEC KEISEITGGP INETLKLLLS SSEWVQSEKL VRALQTPLMR
410 420 430 440 450
LCAWYLYGEK HRGYALNPVA NFHLQNGAVL WRINWMADVS LRGITGSCGL
460 470 480 490
MANYRYFLEE TGPNSTSYLG SKIIKASEQV LSLVAQFQKN SKL
Length:493
Mass (Da):55,003
Last modified:December 1, 2000 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8F061CA38908E8FC
GO
Isoform Cytoplasmic+peroxisomal (identifier: O95822-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.

Note: May be produced by alternative initiation at Met-40 of isoform mitochondrial. Alternatively, represents a proteolytic processed form of the mitochondrial form.Curated
Show »
Length:454
Mass (Da):50,946
Checksum:i41C79B2AC6DB3554
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087X1B8A0A087X1B8_HUMAN
Malonyl-CoA decarboxylase, mitochon...
MLYCD
175Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
V9GY18V9GY18_HUMAN
Malonyl-CoA decarboxylase, mitochon...
MLYCD
98Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
V9GYW3V9GYW3_HUMAN
Malonyl-CoA decarboxylase, mitochon...
MLYCD
91Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD16177 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti82A → D in AAD16177 (PubMed:10417274).Curated1
Sequence conflicti119A → S in AAD48994 (PubMed:9869665).Curated1
Sequence conflicti127D → V in AAD48994 (PubMed:9869665).Curated1
Sequence conflicti192S → P in AAD34631 (PubMed:10455107).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0476491 – 39Missing in isoform Cytoplasmic+peroxisomal. 3 PublicationsAdd BLAST39

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF097832 mRNA Translation: AAD16177.2 Frameshift.
AF153679 mRNA Translation: AAD34631.1
AF090834 mRNA Translation: AAD48994.1
AC009119 Genomic DNA No translation available.
BC000286 mRNA Translation: AAH00286.1
BC052592 mRNA Translation: AAH52592.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS42206.1 [O95822-1]

NCBI Reference Sequences

More...
RefSeqi
NP_036345.2, NM_012213.2 [O95822-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000262430; ENSP00000262430; ENSG00000103150

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
23417

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:23417

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...
MANE-Selecti
ENST00000262430.6; ENSP00000262430.4; NM_012213.3; NP_036345.2

UCSC genome browser

More...
UCSCi
uc002fgz.4, human [O95822-1]

Keywords - Coding sequence diversityi

Alternative initiation

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF097832 mRNA Translation: AAD16177.2 Frameshift.
AF153679 mRNA Translation: AAD34631.1
AF090834 mRNA Translation: AAD48994.1
AC009119 Genomic DNA No translation available.
BC000286 mRNA Translation: AAH00286.1
BC052592 mRNA Translation: AAH52592.1
CCDSiCCDS42206.1 [O95822-1]
RefSeqiNP_036345.2, NM_012213.2 [O95822-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YGWX-ray2.80A/B40-490[»]
4F0XX-ray3.29A/B/C/D/E/F/G/H39-493[»]
SMRiO95822
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi116989, 26 interactors
DIPiDIP-60405N
IntActiO95822, 17 interactors
STRINGi9606.ENSP00000262430

Chemistry databases

BindingDBiO95822
ChEMBLiCHEMBL4698
GuidetoPHARMACOLOGYi1275
SwissLipidsiSLP:000000251

PTM databases

iPTMnetiO95822
PhosphoSitePlusiO95822

Genetic variation databases

BioMutaiMLYCD

Proteomic databases

EPDiO95822
jPOSTiO95822
MassIVEiO95822
MaxQBiO95822
PaxDbiO95822
PeptideAtlasiO95822
PRIDEiO95822
ProteomicsDBi51071 [O95822-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
30519, 111 antibodies from 22 providers

The DNASU plasmid repository

More...
DNASUi
23417

Genome annotation databases

EnsembliENST00000262430; ENSP00000262430; ENSG00000103150
GeneIDi23417
KEGGihsa:23417
MANE-SelectiENST00000262430.6; ENSP00000262430.4; NM_012213.3; NP_036345.2
UCSCiuc002fgz.4, human [O95822-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
23417
DisGeNETi23417

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MLYCD
HGNCiHGNC:7150, MLYCD
HPAiENSG00000103150, Tissue enhanced (tongue)
MalaCardsiMLYCD
MIMi248360, phenotype
606761, gene
neXtProtiNX_O95822
OpenTargetsiENSG00000103150
Orphaneti943, Malonic aciduria
PharmGKBiPA30861
VEuPathDBiHostDB:ENSG00000103150

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3018, Eukaryota
GeneTreeiENSGT00390000005410
HOGENOMiCLU_023433_0_0_1
InParanoidiO95822
OMAiPIDWSTP
OrthoDBi1436590at2759
PhylomeDBiO95822
TreeFamiTF312959

Enzyme and pathway databases

UniPathwayiUPA00340;UER00710
BRENDAi4.1.1.9, 2681
PathwayCommonsiO95822
ReactomeiR-HSA-390247, Beta-oxidation of very long chain fatty acids [O95822-2]
R-HSA-9033241, Peroxisomal protein import [O95822-2]
SABIO-RKiO95822
SignaLinkiO95822

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
23417, 5 hits in 1047 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
MLYCD, human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
23417
PharosiO95822, Tchem

Protein Ontology

More...
PROi
PR:O95822
RNActiO95822, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000103150, Expressed in heart left ventricle and 201 other tissues
ExpressionAtlasiO95822, baseline and differential
GenevisibleiO95822, HS

Family and domain databases

Gene3Di1.20.140.90, 1 hit
3.40.630.150, 1 hit
InterProiView protein in InterPro
IPR038917, Malonyl_CoA_deC
IPR007956, Malonyl_CoA_deC_C
IPR042303, Malonyl_CoA_deC_C_sf
IPR035372, MCD_N
IPR038351, MCD_N_sf
PANTHERiPTHR28641, PTHR28641, 1 hit
PfamiView protein in Pfam
PF05292, MCD, 1 hit
PF17408, MCD_N, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDCMC_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O95822
Secondary accession number(s): Q9UNU5, Q9Y3F2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: February 23, 2022
This is version 182 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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