ACSF3_MOUSE
ID ACSF3_MOUSE Reviewed; 583 AA.
AC Q3URE1; Q78IW2; Q8VC75;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Malonate--CoA ligase ACSF3, mitochondrial {ECO:0000305};
DE EC=6.2.1.n3 {ECO:0000250|UniProtKB:Q4G176};
DE AltName: Full=Acyl-CoA synthetase family member 3;
DE Flags: Precursor;
GN Name=Acsf3 {ECO:0000312|MGI:MGI:2182591};
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 193-583 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Spleen;
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).
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. May have some preference
CC toward very-long-chain substrates. {ECO:0000250|UniProtKB:Q4G176}.
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:0000250|UniProtKB:Q4G176};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000250|UniProtKB:Q4G176};
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:0000250|UniProtKB:Q4G176};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32140;
CC Evidence={ECO:0000250|UniProtKB:Q4G176};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q4G176}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3URE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3URE1-2; Sequence=VSP_030705, VSP_030706;
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22709.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK141579; BAE24747.1; -; mRNA.
DR EMBL; BC022709; AAH22709.3; ALT_INIT; mRNA.
DR CCDS; CCDS40505.1; -. [Q3URE1-1]
DR RefSeq; NP_659181.2; NM_144932.4. [Q3URE1-1]
DR RefSeq; XP_006531093.1; XM_006531030.1. [Q3URE1-1]
DR RefSeq; XP_006531094.1; XM_006531031.1.
DR RefSeq; XP_006531095.1; XM_006531032.2. [Q3URE1-1]
DR AlphaFoldDB; Q3URE1; -.
DR SMR; Q3URE1; -.
DR STRING; 10090.ENSMUSP00000015160; -.
DR iPTMnet; Q3URE1; -.
DR PhosphoSitePlus; Q3URE1; -.
DR EPD; Q3URE1; -.
DR jPOST; Q3URE1; -.
DR MaxQB; Q3URE1; -.
DR PaxDb; Q3URE1; -.
DR PeptideAtlas; Q3URE1; -.
DR PRIDE; Q3URE1; -.
DR ProteomicsDB; 285847; -. [Q3URE1-1]
DR ProteomicsDB; 285848; -. [Q3URE1-2]
DR Antibodypedia; 2033; 114 antibodies from 19 providers.
DR DNASU; 257633; -.
DR Ensembl; ENSMUST00000015160; ENSMUSP00000015160; ENSMUSG00000015016. [Q3URE1-1]
DR Ensembl; ENSMUST00000212790; ENSMUSP00000148762; ENSMUSG00000015016. [Q3URE1-1]
DR GeneID; 257633; -.
DR KEGG; mmu:257633; -.
DR UCSC; uc009ntr.1; mouse. [Q3URE1-2]
DR UCSC; uc009nts.1; mouse. [Q3URE1-1]
DR CTD; 197322; -.
DR MGI; MGI:2182591; Acsf3.
DR VEuPathDB; HostDB:ENSMUSG00000015016; -.
DR eggNOG; KOG1176; Eukaryota.
DR GeneTree; ENSGT00940000157000; -.
DR HOGENOM; CLU_000022_59_11_1; -.
DR InParanoid; Q3URE1; -.
DR OMA; VHDHERI; -.
DR OrthoDB; 533939at2759; -.
DR PhylomeDB; Q3URE1; -.
DR TreeFam; TF312995; -.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR BioGRID-ORCS; 257633; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Acsf3; mouse.
DR PRO; PR:Q3URE1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3URE1; protein.
DR Bgee; ENSMUSG00000015016; Expressed in ileal epithelium and 181 other tissues.
DR ExpressionAtlas; Q3URE1; baseline and differential.
DR Genevisible; Q3URE1; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016878; F:acid-thiol ligase activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; ISO:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
DR GO; GO:0090410; P:malonate catabolic process; ISO:MGI.
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 Alternative splicing; ATP-binding; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..583
FT /note="Malonate--CoA ligase ACSF3, mitochondrial"
FT /id="PRO_0000315801"
FT BINDING 202..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 327..367
FT /note="LMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNP -> FCGDPIA
FT RSGSTHHLRKPAEGFPLHHPCRGKREGDKGEVIV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030705"
FT VAR_SEQ 368..583
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030706"
SQ SEQUENCE 583 AA; 65077 MW; BA1D80C18F91D27D CRC64;
MPPHLALPFR RLFWSLASSQ LIPRRHRGHS LLPTTPEAHT DGSVPVFIRA LAFGDRIALI
DKYGHHTYRE LYDRSLCLAQ EICRLQGCKV GDLQEERVSF LCSNDVSYVV AQWASWMSGG
VAVPLYWKHP EAQLEYFIQD SRSSLVVVGQ EYLERLSPLA QRLGVPLLPL TPAVYHGATE
KPTEQPVEES GWRDRGAMIF YTSGTTGRPK GALSTHRNLA AVVTGLVHSW AWTKNDVILH
VLPLHHVHGV VNKLLCPLWV GATCVMLPEF SAQQVWEKFL SSEAPQITVF MAVPTVYSKL
LDYYDKHFTQ PHVQDFVRAV CKERIRLMVS GSAALPVPLL EKWRSATGHT LLERYGMTEI
GMALSNPLTE ARVPGSVGTP LPGVEVRIIS ENPQKGSPYI IHAEGNERGT KVTPGFEEKE
GELLVRGPSV FREYWDKPEE TKSAFTSDGW FRTGDTAVFK DARYWIRGRT SVDIIKTGGY
KVSALEIERH LLAHPSITDV AVIGVPDMTW GQRVTAVVAL QEGHSLSHGD LKEWARGVLA
PYAVPSELLL VEEIPRNQMG KVNKKELLKQ LYPSGQRSQP GQG
