ACSF2_MOUSE
ID ACSF2_MOUSE Reviewed; 615 AA.
AC Q8VCW8; Q3TDU9; Q3U5G9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Medium-chain acyl-CoA ligase ACSF2, mitochondrial {ECO:0000305};
DE EC=6.2.1.2 {ECO:0000250|UniProtKB:Q96CM8};
DE Flags: Precursor;
GN Name=Acsf2 {ECO:0000312|MGI:MGI:2388287};
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 STRAIN=C57BL/6J, and NOD; TISSUE=Diencephalon, and Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-182, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-182; LYS-478; LYS-544; LYS-570 AND LYS-599, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-182; LYS-199; LYS-340;
RP LYS-398; LYS-510; LYS-544 AND LYS-570, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Acyl-CoA synthases catalyze the initial reaction in fatty
CC acid metabolism, by forming a thioester with CoA. Has some preference
CC toward medium-chain substrates. Plays a role in adipocyte
CC differentiation. {ECO:0000250|UniProtKB:Q96CM8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q96CM8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q96CM8};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AK034209; BAC28632.1; -; mRNA.
DR EMBL; AK153582; BAE32109.1; -; mRNA.
DR EMBL; AK169987; BAE41499.1; -; mRNA.
DR EMBL; AL645764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018371; AAH18371.1; -; mRNA.
DR EMBL; BC063269; AAH63269.1; -; mRNA.
DR CCDS; CCDS25259.1; -.
DR RefSeq; NP_722502.1; NM_153807.2.
DR AlphaFoldDB; Q8VCW8; -.
DR SMR; Q8VCW8; -.
DR BioGRID; 234459; 3.
DR STRING; 10090.ENSMUSP00000099453; -.
DR iPTMnet; Q8VCW8; -.
DR PhosphoSitePlus; Q8VCW8; -.
DR SwissPalm; Q8VCW8; -.
DR EPD; Q8VCW8; -.
DR jPOST; Q8VCW8; -.
DR MaxQB; Q8VCW8; -.
DR PaxDb; Q8VCW8; -.
DR PeptideAtlas; Q8VCW8; -.
DR PRIDE; Q8VCW8; -.
DR ProteomicsDB; 285846; -.
DR Antibodypedia; 30532; 140 antibodies from 24 providers.
DR DNASU; 264895; -.
DR Ensembl; ENSMUST00000103164; ENSMUSP00000099453; ENSMUSG00000076435.
DR GeneID; 264895; -.
DR KEGG; mmu:264895; -.
DR UCSC; uc007kzc.1; mouse.
DR CTD; 80221; -.
DR MGI; MGI:2388287; Acsf2.
DR VEuPathDB; HostDB:ENSMUSG00000076435; -.
DR eggNOG; KOG1177; Eukaryota.
DR GeneTree; ENSGT00940000156830; -.
DR HOGENOM; CLU_000022_59_7_1; -.
DR InParanoid; Q8VCW8; -.
DR OMA; KQSDMKA; -.
DR OrthoDB; 386992at2759; -.
DR PhylomeDB; Q8VCW8; -.
DR TreeFam; TF313466; -.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR BioGRID-ORCS; 264895; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Acsf2; mouse.
DR PRO; PR:Q8VCW8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VCW8; protein.
DR Bgee; ENSMUSG00000076435; Expressed in adrenal gland and 61 other tissues.
DR Genevisible; Q8VCW8; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
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 Acetylation; ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..615
FT /note="Medium-chain acyl-CoA ligase ACSF2, mitochondrial"
FT /id="PRO_0000315795"
FT BINDING 263..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 182
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 182
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 340
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 398
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 478
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 510
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 544
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 544
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 570
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 570
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 599
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 176
FT /note="V -> L (in Ref. 2; BAE32109)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="A -> G (in Ref. 2; BAE32109)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="D -> Y (in Ref. 2; BAE32109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 615 AA; 67951 MW; 84AF2B6FA13D91A8 CRC64;
MAVYHGMLRF GRLCIASLGA RGPRTLLSRP RPNSKLQSVR ALSSGMVNCT NPLPIGGLSY
IQGHTDSHLV NTTVGECLDA TAQRFPDREA LVILHENIRL NFAQLKEEVD KAASGLLSIG
LRKGDRLGMW GPNSYAWVLI QLATAQAGII LVSVNPAYQS SELEYVLRKV GCKGIVFPKQ
FKTQQYYDIL KQVCPELEKA QPGALKSERL PDLTTVISVD APLPGTLLLD DIVAAGGKEQ
NLAQLRYNQR FLSCYDPINI QFTSGTTGNP KGATLSHHNI VNNSMLIGQR LKMPTKTAEE
LRLVLPSPLY HCLGSVGGTM VSMMHGATLL LSSPSFNGKK ALEAISREKG TLLYGTPTMF
VDILNQPDFS SYDFTSIRGG VIAGSPAPPE LIRAIINKMN MKELVVVYGT TENSPVTFMN
FPEDTLEQKA GSVGRIMPHT EAQIVNVETG ELTNLNVPGE LYIRGYCVMQ GYWGEPQKTF
ETVGQDKWYR TGDIALMDEQ GFCKIVGRSK DMIIRGGENI YPAELEDFFL KHPQVQEAQV
VGVKDERMGE EICACIRLKS GETTTAEEIK AFCKGKISHF KIPRYIVFVE GYPLTISGKI
QKFKLREQME QHLKL
