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Q8R3F5 (FABD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malonyl-CoA-acyl carrier protein transacylase, mitochondrial

Short name=MCT
EC=2.3.1.39
Alternative name(s):
Mitochondrial malonyltransferase
[Acyl-carrier-protein] malonyltransferase
Gene names
Name:Mcat
Synonyms:Mt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondrias By similarity.

Catalytic activity

Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the type II malonyltransferase family.

Sequence caution

The sequence AAH25519.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   Molecular_function[acyl-carrier-protein] S-malonyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 381Malonyl-CoA-acyl carrier protein transacylase, mitochondrialPRO_0000042239

Sites

Active site1511 By similarity
Active site2681 By similarity

Amino acid modifications

Modified residue3121N6-succinyllysine Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8R3F5 [UniParc].

Last modified October 11, 2005. Version 3.
Checksum: 7024C1EBAF95B1EE

FASTA38141,928
        10         20         30         40         50         60 
MSARVARAGW AWRSWGRRAA SSLREPPPDA VDVAELLRDS SVAEEGAQEA VARRRPPSQC 

        70         80         90        100        110        120 
SVLLFPGQGC QAVGMGSGLL HLPRVRQLYE AAHRVLGYDL LELCLRGPQE DLDRTVHCQP 

       130        140        150        160        170        180 
AVFVASLAAV EKLHHLQPAV IDNCVAAAGF SVGEFAALVF AGAMDFSEGL YAVKARAEAM 

       190        200        210        220        230        240 
QEASEAVPSG MLSVLGQRQS NFSFACLEAQ EHCKSLGIEN PVCQVSNYLF PDCRVISGHL 

       250        260        270        280        290        300 
EALQFLRRNS AKYHFRRTKM LPVSGGFHTC LMEPAVDPLM KVLGSINIKK PLVAVHSNVS 

       310        320        330        340        350        360 
GQKYTHPQHI RKLLGQQVVS PVKWEQTMHS IYERKKGMEF PSTYEVGPGQ QLGSILKCCN 

       370        380 
RQAWKSYSHV DVMQNIMDPD P 

« Hide

References

[1]"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: Thyroid.
[2]"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-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC099494 mRNA. Translation: AAH99494.1.
BC025519 mRNA. Translation: AAH25519.1. Different initiation.
RefSeqNP_001025185.1. NM_001030014.2.
UniGeneMm.37560.

3D structure databases

ProteinModelPortalQ8R3F5.
SMRQ8R3F5. Positions 3-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8R3F5. 1 interaction.
MINTMINT-4094897.

PTM databases

PhosphoSiteQ8R3F5.

Proteomic databases

PaxDbQ8R3F5.
PRIDEQ8R3F5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000061882; ENSMUSP00000051569; ENSMUSG00000048755.
GeneID223722.
KEGGmmu:223722.
UCSCuc007xbf.1. mouse.

Organism-specific databases

CTD27349.
MGIMGI:2388651. Mcat.

Phylogenomic databases

eggNOGCOG0331.
GeneTreeENSGT00390000013715.
HOGENOMHOG000036504.
HOVERGENHBG051540.
InParanoidQ8R3F5.
KOK00645.
OMALEMSVAS.
OrthoDBEOG7D85X6.
PhylomeDBQ8R3F5.
TreeFamTF313401.

Enzyme and pathway databases

UniPathwayUPA00094.

Gene expression databases

BgeeQ8R3F5.
CleanExMM_MCAT.
GenevestigatorQ8R3F5.

Family and domain databases

Gene3D3.40.366.10. 2 hits.
InterProIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMCAT. mouse.
NextBio376844.
PROQ8R3F5.
SOURCESearch...

Entry information

Entry nameFABD_MOUSE
AccessionPrimary (citable) accession number: Q8R3F5
Secondary accession number(s): Q4FZH0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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