ID ACS2L_HUMAN Reviewed; 689 AA. AC Q9NUB1; B3KXL2; B4DJZ3; D3DW48; F5H6F4; F8W7Y1; Q5TF42; Q8IV99; Q8N234; AC Q96JI1; Q96JX6; Q9NU28; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-APR-2003, sequence version 2. DT 24-JAN-2024, entry version 181. DE RecName: Full=Acetyl-coenzyme A synthetase 2-like, mitochondrial; DE EC=6.2.1.1 {ECO:0000269|PubMed:16788062}; DE AltName: Full=Acetate--CoA ligase 2; DE AltName: Full=Acetyl-CoA synthetase 2 {ECO:0000303|PubMed:16788062}; DE Short=AceCS2 {ECO:0000303|PubMed:16788062}; DE AltName: Full=Acyl-CoA synthetase short-chain family member 1; DE AltName: Full=Propionate--CoA ligase; DE EC=6.2.1.17 {ECO:0000250|UniProtKB:Q99NB1}; DE Flags: Precursor; GN Name=ACSS1; Synonyms=ACAS2L, KIAA1846; 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] (ISOFORMS 3 AND 4), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 169-689 (ISOFORM 1), AND VARIANT MET-488. RC TISSUE=Placenta, Thalamus, and Tongue; 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 GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP MET-488. RC TISSUE=Brain, and Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 336-689 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [6] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [7] RP ACETYLATION AT LYS-642, MUTAGENESIS OF LYS-642, FUNCTION, CATALYTIC RP ACTIVITY, INTERACTION WITH SIRT3, ACTIVITY REGULATION, PROTEIN SEQUENCE OF RP N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=16788062; DOI=10.1073/pnas.0603968103; RA Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., Verdin E.; RT "Reversible lysine acetylation controls the activity of the mitochondrial RT enzyme acetyl-CoA synthetase 2."; RL Proc. Natl. Acad. Sci. U.S.A. 103:10224-10229(2006). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [9] 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 [10] 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 [11] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 638-649 IN COMPLEX WITH SIRT3. RX PubMed=19535340; DOI=10.1074/jbc.m109.014928; RA Jin L., Wei W., Jiang Y., Peng H., Cai J., Mao C., Dai H., Choy W., RA Bemis J.E., Jirousek M.R., Milne J.C., Westphal C.H., Perni R.B.; RT "Crystal structures of human SIRT3 displaying substrate-induced RT conformational changes."; RL J. Biol. Chem. 284:24394-24405(2009). CC -!- FUNCTION: Catalyzes the synthesis of acetyl-CoA from short-chain fatty CC acids (PubMed:16788062). Acetate is the preferred substrate CC (PubMed:16788062). Can also utilize propionate with a much lower CC affinity (By similarity). Provides acetyl-CoA that is utilized mainly CC for oxidation under ketogenic conditions (By similarity). Involved in CC thermogenesis under ketogenic conditions, using acetate as a vital fuel CC when carbohydrate availability is insufficient (By similarity). CC {ECO:0000250|UniProtKB:Q99NB1, ECO:0000269|PubMed:16788062}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:456215; EC=6.2.1.1; CC Evidence={ECO:0000269|PubMed:16788062}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177; CC Evidence={ECO:0000305|PubMed:16788062}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA; CC Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, CC ChEBI:CHEBI:456215; EC=6.2.1.17; CC Evidence={ECO:0000250|UniProtKB:Q99NB1}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374; CC Evidence={ECO:0000250|UniProtKB:Q99NB1}; CC -!- ACTIVITY REGULATION: Inhibited by acetylation at Lys-642 and activated CC by deacetylation mediated by the deacetylase SIRT3. CC {ECO:0000269|PubMed:16788062}. CC -!- SUBUNIT: Interacts with SIRT3. {ECO:0000269|PubMed:16788062, CC ECO:0000269|PubMed:19535340}. CC -!- INTERACTION: CC Q9NUB1; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10313831, EBI-16439278; CC Q9NUB1; Q08AM6: VAC14; NbExp=6; IntAct=EBI-10313831, EBI-2107455; CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000269|PubMed:16788062}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9NUB1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NUB1-2; Sequence=VSP_007249; CC Name=3; CC IsoId=Q9NUB1-3; Sequence=VSP_044693, VSP_044694; CC Name=4; CC IsoId=Q9NUB1-4; Sequence=VSP_045546, VSP_045547; CC -!- PTM: Reversibly acetylated on Lys-642 (PubMed:16788062). The acetyl-CoA CC synthase activity is inhibited by acetylation and activated by CC deacetylation mediated by the deacetylase SIRT3. CC {ECO:0000269|PubMed:16788062}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB55390.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC03853.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAC03853.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK027817; BAB55390.1; ALT_INIT; mRNA. DR EMBL; AK092295; BAC03853.1; ALT_SEQ; mRNA. DR EMBL; AK127566; BAG54524.1; -; mRNA. DR EMBL; AK296306; BAG59005.1; -; mRNA. DR EMBL; AL035661; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL080312; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10106.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10109.1; -; Genomic_DNA. DR EMBL; BC039261; AAH39261.1; -; mRNA. DR EMBL; BC044588; AAH44588.1; -; mRNA. DR EMBL; AB058749; BAB47475.1; -; mRNA. DR CCDS; CCDS13167.1; -. [Q9NUB1-1] DR CCDS; CCDS58764.1; -. [Q9NUB1-3] DR CCDS; CCDS58765.1; -. [Q9NUB1-4] DR RefSeq; NP_001239604.1; NM_001252675.1. [Q9NUB1-2] DR RefSeq; NP_001239605.1; NM_001252676.1. [Q9NUB1-3] DR RefSeq; NP_001239606.1; NM_001252677.1. [Q9NUB1-4] DR RefSeq; NP_115890.2; NM_032501.3. [Q9NUB1-1] DR PDB; 3GLR; X-ray; 1.80 A; B=638-649. DR PDB; 3GLT; X-ray; 2.10 A; B=638-649. DR PDB; 3GLU; X-ray; 2.50 A; B=638-649. DR PDB; 4BVE; X-ray; 2.05 A; B=638-647. DR PDB; 4BVF; X-ray; 2.70 A; B=638-647. DR PDB; 4BVG; X-ray; 2.50 A; B=638-647. DR PDB; 4C78; X-ray; 2.00 A; C=638-647. DR PDB; 5Y4H; X-ray; 2.60 A; B=638-649. DR PDB; 5YTK; X-ray; 2.70 A; G/J/K/L=638-645. DR PDBsum; 3GLR; -. DR PDBsum; 3GLT; -. DR PDBsum; 3GLU; -. DR PDBsum; 4BVE; -. DR PDBsum; 4BVF; -. DR PDBsum; 4BVG; -. DR PDBsum; 4C78; -. DR PDBsum; 5Y4H; -. DR PDBsum; 5YTK; -. DR AlphaFoldDB; Q9NUB1; -. DR SMR; Q9NUB1; -. DR BioGRID; 124122; 20. DR DIP; DIP-61208N; -. DR IntAct; Q9NUB1; 12. DR MINT; Q9NUB1; -. DR STRING; 9606.ENSP00000316924; -. DR DrugBank; DB00171; ATP. DR SwissLipids; SLP:000000448; -. DR iPTMnet; Q9NUB1; -. DR MetOSite; Q9NUB1; -. DR PhosphoSitePlus; Q9NUB1; -. DR SwissPalm; Q9NUB1; -. DR BioMuta; ACSS1; -. DR DMDM; 30172968; -. DR EPD; Q9NUB1; -. DR jPOST; Q9NUB1; -. DR MassIVE; Q9NUB1; -. DR MaxQB; Q9NUB1; -. DR PaxDb; 9606-ENSP00000316924; -. DR PeptideAtlas; Q9NUB1; -. DR ProteomicsDB; 27173; -. DR ProteomicsDB; 30036; -. DR ProteomicsDB; 82660; -. [Q9NUB1-1] DR ProteomicsDB; 82661; -. [Q9NUB1-2] DR Pumba; Q9NUB1; -. DR Antibodypedia; 24959; 163 antibodies from 24 providers. DR DNASU; 84532; -. DR Ensembl; ENST00000323482.9; ENSP00000316924.4; ENSG00000154930.15. [Q9NUB1-1] DR Ensembl; ENST00000432802.6; ENSP00000388793.2; ENSG00000154930.15. [Q9NUB1-4] DR Ensembl; ENST00000537502.5; ENSP00000439304.2; ENSG00000154930.15. [Q9NUB1-3] DR GeneID; 84532; -. DR KEGG; hsa:84532; -. DR MANE-Select; ENST00000323482.9; ENSP00000316924.4; NM_032501.4; NP_115890.2. DR UCSC; uc002wub.4; human. [Q9NUB1-1] DR AGR; HGNC:16091; -. DR CTD; 84532; -. DR DisGeNET; 84532; -. DR GeneCards; ACSS1; -. DR HGNC; HGNC:16091; ACSS1. DR HPA; ENSG00000154930; Tissue enhanced (choroid). DR MIM; 614355; gene. DR neXtProt; NX_Q9NUB1; -. DR OpenTargets; ENSG00000154930; -. DR PharmGKB; PA24430; -. DR VEuPathDB; HostDB:ENSG00000154930; -. DR eggNOG; KOG1175; Eukaryota. DR GeneTree; ENSGT00940000158550; -. DR HOGENOM; CLU_000022_3_0_1; -. DR InParanoid; Q9NUB1; -. DR OMA; AIKASWP; -. DR OrthoDB; 144557at2759; -. DR PhylomeDB; Q9NUB1; -. DR TreeFam; TF354241; -. DR BRENDA; 6.2.1.1; 2681. DR PathwayCommons; Q9NUB1; -. DR Reactome; R-HSA-71384; Ethanol oxidation. DR SignaLink; Q9NUB1; -. DR SIGNOR; Q9NUB1; -. DR BioGRID-ORCS; 84532; 11 hits in 1152 CRISPR screens. DR ChiTaRS; ACSS1; human. DR EvolutionaryTrace; Q9NUB1; -. DR GenomeRNAi; 84532; -. DR Pharos; Q9NUB1; Tbio. DR PRO; PR:Q9NUB1; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9NUB1; Protein. DR Bgee; ENSG00000154930; Expressed in apex of heart and 174 other cell types or tissues. DR ExpressionAtlas; Q9NUB1; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:UniProtKB. DR GO; GO:0016208; F:AMP binding; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050218; F:propionate-CoA ligase activity; ISS:UniProtKB. DR GO; GO:0019413; P:acetate biosynthetic process; IEA:Ensembl. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IDA:UniProtKB. DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro. DR GO; GO:0006069; P:ethanol oxidation; TAS:Reactome. DR GO; GO:0019542; P:propionate biosynthetic process; IEA:Ensembl. DR CDD; cd05966; ACS; 1. DR Gene3D; 3.30.300.30; -; 1. DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1. DR InterPro; IPR011904; Ac_CoA_lig. DR InterPro; IPR032387; ACAS_N. 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_com. DR InterPro; IPR042099; ANL_N_sf. DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1. DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1. DR PANTHER; PTHR24095:SF110; ACETYL-COENZYME A SYNTHETASE 2-LIKE, MITOCHONDRIAL; 1. DR Pfam; PF16177; ACAS_N; 1. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF13193; AMP-binding_C; 1. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1. DR PROSITE; PS00455; AMP_BINDING; 1. DR Genevisible; Q9NUB1; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Direct protein sequencing; Ligase; Lipid metabolism; Mitochondrion; KW Nucleotide-binding; Reference proteome; Transit peptide. FT TRANSIT 1..37 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:16788062" FT CHAIN 38..689 FT /note="Acetyl-coenzyme A synthetase 2-like, mitochondrial" FT /id="PRO_0000000596" FT REGION 17..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 224..227 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250" FT BINDING 341 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250" FT BINDING 417..419 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 441..446 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 533 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 548 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 556 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250" FT BINDING 559 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT MOD_RES 396 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 642 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:16788062" FT VAR_SEQ 1..22 FT /note="MAARTLGRGVGRLLGSLRGLSG -> MRRRKERQPWDRFHFLHFAPHG (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044693" FT VAR_SEQ 23..143 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044694" FT VAR_SEQ 446..447 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007249" FT VAR_SEQ 556..575 FT /note="SGHRLGTAEIEDAIADHPAV -> LQIVGFFREAIRNSGDLLEH (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045546" FT VAR_SEQ 576..689 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045547" FT VARIANT 488 FT /note="V -> M (in dbSNP:rs6050249)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_048184" FT MUTAGEN 642 FT /note="K->Q: Loss of activity." FT /evidence="ECO:0000269|PubMed:16788062" FT CONFLICT 233 FT /note="K -> I (in Ref. 1; BAG54524)" FT /evidence="ECO:0000305" FT CONFLICT 277 FT /note="V -> M (in Ref. 4; AAH39261)" FT /evidence="ECO:0000305" SQ SEQUENCE 689 AA; 74857 MW; 66E84E39302AD08B CRC64; MAARTLGRGV GRLLGSLRGL SGQPARPPCG VSAPRRAASG PSGSAPAVAA AAAQPGSYPA LSAQAAREPA AFWGPLARDT LVWDTPYHTV WDCDFSTGKI GWFLGGQLNV SVNCLDQHVR KSPESVALIW ERDEPGTEVR ITYRELLETT CRLANTLKRH GVHRGDRVAI YMPVSPLAVA AMLACARIGA VHTVIFAGFS AESLAGRIND AKCKVVITFN QGLRGGRVVE LKKIVDEAVK HCPTVQHVLV AHRTDNKVHM GDLDVPLEQE MAKEDPVCAP ESMGSEDMLF MLYTSGSTGM PKGIVHTQAG YLLYAALTHK LVFDHQPGDI FGCVADIGWI TGHSYVVYGP LCNGATSVLF ESTPVYPNAG RYWETVERLK INQFYGAPTA VRLLLKYGDA WVKKYDRSSL RTLGSVGEPI NCEAWEWLHR VVGDSRCTLV DTWWQTETGG ICIAPRPSEE GAEILPAMAM RPFFGIVPVL MDEKGSVVEG SNVSGALCIS QAWPGMARTI YGDHQRFVDA YFKAYPGYYF TGDGAYRTEG GYYQITGRMD DVINISGHRL GTAEIEDAIA DHPAVPESAV IGYPHDIKGE AAFAFIVVKD SAGDSDVVVQ ELKSMVATKI AKYAVPDEIL VVKRLPKTRS GKVMRRLLRK IITSEAQELG DTTTLEDPSI IAEILSVYQK CKDKQAAAK //