ACSF3_HUMAN
ID ACSF3_HUMAN Reviewed; 576 AA.
AC Q4G176; A8K4J8; C9JQL6; Q6INA0; Q8N2F7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Malonate--CoA ligase ACSF3, mitochondrial {ECO:0000305};
DE EC=6.2.1.n3 {ECO:0000269|PubMed:21846720};
DE AltName: Full=Acyl-CoA synthetase family member 3;
DE Flags: Precursor;
GN Name=ACSF3 {ECO:0000312|HGNC:HGNC:27288}; ORFNames=PSEC0197;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-2; PRO-17 AND
RP MET-372.
RC TISSUE=Brain;
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 [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17762044; DOI=10.1194/jlr.m700378-jlr200;
RA Watkins P.A., Maiguel D., Jia Z., Pevsner J.;
RT "Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human
RT genome.";
RL J. Lipid Res. 48:2736-2750(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF ARG-354.
RX PubMed=21846720; DOI=10.1074/jbc.m111.291591;
RA Witkowski A., Thweatt J., Smith S.;
RT "Mammalian ACSF3 protein is a malonyl-CoA synthetase that supplies the
RT chain extender units for mitochondrial fatty acid synthesis.";
RL J. Biol. Chem. 286:33729-33736(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP VARIANTS CMAMMA ARG-198; LEU-243; ILE-358; LYS-359; THR-462;
RP 465-GLN--GLY-470 DEL; GLN-471; TRP-471; SER-480 AND TRP-558, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21841779; DOI=10.1038/ng.908;
RA Sloan J.L., Johnston J.J., Manoli I., Chandler R.J., Krause C.,
RA Carrillo-Carrasco N., Chandrasekaran S.D., Sysol J.R., O'Brien K.,
RA Hauser N.S., Sapp J.C., Dorward H.M., Huizing M., Barshop B.A., Berry S.A.,
RA James P.M., Champaigne N.L., de Lonlay P., Valayannopoulos V.,
RA Geschwind M.D., Gavrilov D.K., Nyhan W.L., Biesecker L.G., Venditti C.P.;
RT "Exome sequencing identifies ACSF3 as a cause of combined malonic and
RT methylmalonic aciduria.";
RL Nat. Genet. 43:883-886(2011).
CC -!- FUNCTION: Catalyzes the initial reaction in intramitochondrial fatty
CC acid synthesis, by activating malonate and methylmalonate, but not
CC acetate, into their respective CoA thioester (PubMed:21846720,
CC PubMed:21841779). May have some preference toward very-long-chain
CC substrates (PubMed:17762044). {ECO:0000269|PubMed:17762044,
CC ECO:0000269|PubMed:21841779, ECO:0000269|PubMed:21846720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:17762044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000269|PubMed:17762044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + malonate = AMP + diphosphate + malonyl-CoA;
CC Xref=Rhea:RHEA:32139, ChEBI:CHEBI:15792, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:456215; EC=6.2.1.n3;
CC Evidence={ECO:0000269|PubMed:21846720};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32140;
CC Evidence={ECO:0000269|PubMed:21846720};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36.8 uM for malonate {ECO:0000269|PubMed:21846720};
CC -!- INTERACTION:
CC Q4G176; Q6A162: KRT40; NbExp=3; IntAct=EBI-10714818, EBI-10171697;
CC Q4G176; O95460-2: MATN4; NbExp=3; IntAct=EBI-10714818, EBI-12072296;
CC Q4G176; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-10714818, EBI-1105153;
CC Q4G176; P51157: RAB28; NbExp=3; IntAct=EBI-10714818, EBI-11898753;
CC Q4G176; P14373: TRIM27; NbExp=3; IntAct=EBI-10714818, EBI-719493;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21841779,
CC ECO:0000269|PubMed:21846720}.
CC -!- DISEASE: Combined malonic and methylmalonic aciduria (CMAMMA)
CC [MIM:614265]: A metabolic disease characterized by malonic and
CC methylmalonic aciduria, with urinary excretion of much larger amounts
CC of methylmalonic acid than malonic acid, in the presence of normal
CC malonyl-CoA decarboxylase activity. Clinical features include coma,
CC ketoacidosis, hypoglycemia, failure to thrive, microcephaly, dystonia,
CC axial hypotonia and/or developmental delay, and neurologic
CC manifestations including seizures, psychiatric disease and/or cognitive
CC decline. {ECO:0000269|PubMed:21841779}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72391.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AK075499; BAC11654.1; -; mRNA.
DR EMBL; AK290963; BAF83652.1; -; mRNA.
DR EMBL; AC009113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471184; EAW66744.1; -; Genomic_DNA.
DR EMBL; BC028399; AAH28399.1; -; mRNA.
DR EMBL; BC072391; AAH72391.1; ALT_SEQ; mRNA.
DR CCDS; CCDS10974.1; -.
DR RefSeq; NP_001120686.1; NM_001127214.3.
DR RefSeq; NP_001230208.1; NM_001243279.2.
DR RefSeq; NP_777577.2; NM_174917.4.
DR AlphaFoldDB; Q4G176; -.
DR SMR; Q4G176; -.
DR BioGRID; 128248; 80.
DR IntAct; Q4G176; 17.
DR STRING; 9606.ENSP00000479130; -.
DR ChEMBL; CHEMBL4523315; -.
DR SwissLipids; SLP:000000541; -.
DR GlyGen; Q4G176; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q4G176; -.
DR PhosphoSitePlus; Q4G176; -.
DR BioMuta; ACSF3; -.
DR DMDM; 296439438; -.
DR EPD; Q4G176; -.
DR jPOST; Q4G176; -.
DR MassIVE; Q4G176; -.
DR MaxQB; Q4G176; -.
DR PaxDb; Q4G176; -.
DR PeptideAtlas; Q4G176; -.
DR PRIDE; Q4G176; -.
DR ProteomicsDB; 62157; -.
DR Antibodypedia; 2033; 114 antibodies from 19 providers.
DR DNASU; 197322; -.
DR Ensembl; ENST00000317447.9; ENSP00000320646.4; ENSG00000176715.17.
DR Ensembl; ENST00000406948.7; ENSP00000384627.3; ENSG00000176715.17.
DR Ensembl; ENST00000614302.5; ENSP00000479130.1; ENSG00000176715.17.
DR GeneID; 197322; -.
DR KEGG; hsa:197322; -.
DR MANE-Select; ENST00000614302.5; ENSP00000479130.1; NM_001243279.3; NP_001230208.1.
DR UCSC; uc002fmp.5; human.
DR CTD; 197322; -.
DR DisGeNET; 197322; -.
DR GeneCards; ACSF3; -.
DR HGNC; HGNC:27288; ACSF3.
DR HPA; ENSG00000176715; Low tissue specificity.
DR MalaCards; ACSF3; -.
DR MIM; 614245; gene.
DR MIM; 614265; phenotype.
DR neXtProt; NX_Q4G176; -.
DR OpenTargets; ENSG00000176715; -.
DR Orphanet; 289504; Combined malonic and methylmalonic acidemia.
DR PharmGKB; PA162375375; -.
DR VEuPathDB; HostDB:ENSG00000176715; -.
DR eggNOG; KOG1176; Eukaryota.
DR GeneTree; ENSGT00940000157000; -.
DR InParanoid; Q4G176; -.
DR OMA; VHDHERI; -.
DR OrthoDB; 533939at2759; -.
DR PhylomeDB; Q4G176; -.
DR TreeFam; TF312995; -.
DR PathwayCommons; Q4G176; -.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SignaLink; Q4G176; -.
DR BioGRID-ORCS; 197322; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; ACSF3; human.
DR GeneWiki; ACSF3; -.
DR GenomeRNAi; 197322; -.
DR Pharos; Q4G176; Tbio.
DR PRO; PR:Q4G176; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q4G176; protein.
DR Bgee; ENSG00000176715; Expressed in mucosa of transverse colon and 104 other tissues.
DR ExpressionAtlas; Q4G176; baseline and differential.
DR Genevisible; Q4G176; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016878; F:acid-thiol ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0090409; F:malonyl-CoA synthetase activity; IDA:UniProtKB.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:FlyBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0090410; P:malonate catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..83
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 84..576
FT /note="Malonate--CoA ligase ACSF3, mitochondrial"
FT /id="PRO_0000315800"
FT BINDING 202..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VARIANT 2
FT /note="L -> P (in dbSNP:rs7188200)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038306"
FT VARIANT 17
FT /note="A -> P (in dbSNP:rs11547019)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038307"
FT VARIANT 198
FT /note="M -> R (in CMAMMA; dbSNP:rs387907121)"
FT /evidence="ECO:0000269|PubMed:21841779"
FT /id="VAR_066504"
FT VARIANT 243
FT /note="P -> L (in CMAMMA; dbSNP:rs140986055)"
FT /evidence="ECO:0000269|PubMed:21841779"
FT /id="VAR_066505"
FT VARIANT 358
FT /note="T -> I (in CMAMMA; dbSNP:rs387907120)"
FT /evidence="ECO:0000269|PubMed:21841779"
FT /id="VAR_066506"
FT VARIANT 359
FT /note="E -> K (in CMAMMA; dbSNP:rs150487794)"
FT /evidence="ECO:0000269|PubMed:21841779"
FT /id="VAR_066507"
FT VARIANT 372
FT /note="V -> M (in dbSNP:rs3743979)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038308"
FT VARIANT 462
FT /note="K -> T (in CMAMMA; dbSNP:rs1362504214)"
FT /evidence="ECO:0000269|PubMed:21841779"
FT /id="VAR_066508"
FT VARIANT 465..470
FT /note="Missing (in CMAMMA)"
FT /evidence="ECO:0000269|PubMed:21841779"
FT /id="VAR_066509"
FT VARIANT 471
FT /note="R -> Q (in CMAMMA; dbSNP:rs387907119)"
FT /evidence="ECO:0000269|PubMed:21841779"
FT /id="VAR_066510"
FT VARIANT 471
FT /note="R -> W (in CMAMMA; dbSNP:rs138680796)"
FT /evidence="ECO:0000269|PubMed:21841779"
FT /id="VAR_066511"
FT VARIANT 480
FT /note="G -> S (in CMAMMA)"
FT /evidence="ECO:0000269|PubMed:21841779"
FT /id="VAR_066512"
FT VARIANT 558
FT /note="R -> W (in CMAMMA; dbSNP:rs141090143)"
FT /evidence="ECO:0000269|PubMed:21841779"
FT /id="VAR_066513"
FT MUTAGEN 354
FT /note="R->A: Impairs malonyl-CoA synthase activity."
FT /evidence="ECO:0000269|PubMed:21846720"
FT MUTAGEN 354
FT /note="R->L: Impairs malonyl-CoA synthase activity."
FT /evidence="ECO:0000269|PubMed:21846720"
FT CONFLICT 148
FT /note="A -> V (in Ref. 5; AAH28399)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="K -> E (in Ref. 2; BAC11654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 64130 MW; 60F0D5020817EF70 CRC64;
MLPHVVLTFR RLGCALASCR LAPARHRGSG LLHTAPVARS DRSAPVFTRA LAFGDRIALV
DQHGRHTYRE LYSRSLRLSQ EICRLCGCVG GDLREERVSF LCANDASYVV AQWASWMSGG
VAVPLYRKHP AAQLEYVICD SQSSVVLASQ EYLELLSPVV RKLGVPLLPL TPAIYTGAVE
EPAEVPVPEQ GWRNKGAMII YTSGTTGRPK GVLSTHQNIR AVVTGLVHKW AWTKDDVILH
VLPLHHVHGV VNALLCPLWV GATCVMMPEF SPQQVWEKFL SSETPRINVF MAVPTIYTKL
MEYYDRHFTQ PHAQDFLRAV CEEKIRLMVS GSAALPLPVL EKWKNITGHT LLERYGMTEI
GMALSGPLTT AVRLPGSVGT PLPGVQVRIV SENPQREACS YTIHAEGDER GTKVTPGFEE
KEGELLVRGP SVFREYWNKP EETKSAFTLD GWFKTGDTVV FKDGQYWIRG RTSVDIIKTG
GYKVSALEVE WHLLAHPSIT DVAVIGVPDM TWGQRVTAVV TLREGHSLSH RELKEWARNV
LAPYAVPSEL VLVEEIPRNQ MGKIDKKALI RHFHPS
