ID   FABD_MOUSE              Reviewed;         381 AA.
AC   Q8R3F5; Q4FZH0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 3.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Malonyl-CoA-acyl carrier protein transacylase, mitochondrial {ECO:0000305};
DE            Short=MCT;
DE            EC=2.3.1.39 {ECO:0000250|UniProtKB:Q8IVS2};
DE   AltName: Full=Mitochondrial malonyltransferase;
DE   AltName: Full=[Acyl-carrier-protein] malonyltransferase;
DE   Flags: Precursor;
GN   Name=Mcat {ECO:0000312|MGI:MGI:2388651}; Synonyms=Mt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thyroid;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-312, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Catalyzes the transfer of a malonyl moiety from malonyl-CoA
CC       to the free thiol group of the phosphopantetheine arm of the
CC       mitochondrial ACP protein (NDUFAB1). This suggests the existence of the
CC       biosynthesis of fatty acids in mitochondria.
CC       {ECO:0000250|UniProtKB:Q8IVS2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000250|UniProtKB:Q8IVS2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC         Evidence={ECO:0000250|UniProtKB:Q8IVS2};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8IVS2}.
CC   -!- SIMILARITY: Belongs to the type II malonyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25519.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC099494; AAH99494.1; -; mRNA.
DR   EMBL; BC025519; AAH25519.1; ALT_INIT; mRNA.
DR   CCDS; CCDS27704.1; -.
DR   RefSeq; NP_001025185.1; NM_001030014.2.
DR   AlphaFoldDB; Q8R3F5; -.
DR   SMR; Q8R3F5; -.
DR   STRING; 10090.ENSMUSP00000051569; -.
DR   iPTMnet; Q8R3F5; -.
DR   PhosphoSitePlus; Q8R3F5; -.
DR   SwissPalm; Q8R3F5; -.
DR   EPD; Q8R3F5; -.
DR   jPOST; Q8R3F5; -.
DR   MaxQB; Q8R3F5; -.
DR   PaxDb; 10090-ENSMUSP00000051569; -.
DR   PeptideAtlas; Q8R3F5; -.
DR   ProteomicsDB; 271546; -.
DR   Pumba; Q8R3F5; -.
DR   Antibodypedia; 27475; 254 antibodies from 23 providers.
DR   DNASU; 223722; -.
DR   Ensembl; ENSMUST00000061882.10; ENSMUSP00000051569.9; ENSMUSG00000048755.10.
DR   GeneID; 223722; -.
DR   KEGG; mmu:223722; -.
DR   UCSC; uc007xbf.1; mouse.
DR   AGR; MGI:2388651; -.
DR   CTD; 27349; -.
DR   MGI; MGI:2388651; Mcat.
DR   VEuPathDB; HostDB:ENSMUSG00000048755; -.
DR   eggNOG; KOG2926; Eukaryota.
DR   GeneTree; ENSGT00390000013715; -.
DR   HOGENOM; CLU_030558_2_1_1; -.
DR   InParanoid; Q8R3F5; -.
DR   OMA; AANYNCP; -.
DR   OrthoDB; 2265421at2759; -.
DR   PhylomeDB; Q8R3F5; -.
DR   TreeFam; TF313401; -.
DR   Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   UniPathway; UPA00094; -.
DR   BioGRID-ORCS; 223722; 24 hits in 82 CRISPR screens.
DR   ChiTaRS; Mcat; mouse.
DR   PRO; PR:Q8R3F5; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8R3F5; Protein.
DR   Bgee; ENSMUSG00000048755; Expressed in spermatocyte and 223 other cell types or tissues.
DR   ExpressionAtlas; Q8R3F5; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; ISO:MGI.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; ISO:MGI.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   PANTHER; PTHR47170; MALONYL-COA ACP TRANSACYLASE, ACP-BINDING; 1.
DR   PANTHER; PTHR47170:SF2; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   Genevisible; Q8R3F5; MM.
PE   1: Evidence at protein level;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..381
FT                   /note="Malonyl-CoA-acyl carrier protein transacylase,
FT                   mitochondrial"
FT                   /id="PRO_0000042239"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000250"
FT   MOD_RES         312
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
SQ   SEQUENCE   381 AA;  41928 MW;  7024C1EBAF95B1EE CRC64;
     MSARVARAGW AWRSWGRRAA SSLREPPPDA VDVAELLRDS SVAEEGAQEA VARRRPPSQC
     SVLLFPGQGC QAVGMGSGLL HLPRVRQLYE AAHRVLGYDL LELCLRGPQE DLDRTVHCQP
     AVFVASLAAV EKLHHLQPAV IDNCVAAAGF SVGEFAALVF AGAMDFSEGL YAVKARAEAM
     QEASEAVPSG MLSVLGQRQS NFSFACLEAQ EHCKSLGIEN PVCQVSNYLF PDCRVISGHL
     EALQFLRRNS AKYHFRRTKM LPVSGGFHTC LMEPAVDPLM KVLGSINIKK PLVAVHSNVS
     GQKYTHPQHI RKLLGQQVVS PVKWEQTMHS IYERKKGMEF PSTYEVGPGQ QLGSILKCCN
     RQAWKSYSHV DVMQNIMDPD P
//