ACS2L_HUMAN
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 03-AUG-2022, entry version 173.
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};
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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; 19.
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 BioMuta; ACSS1; -.
DR DMDM; 30172968; -.
DR EPD; Q9NUB1; -.
DR jPOST; Q9NUB1; -.
DR MassIVE; Q9NUB1; -.
DR MaxQB; Q9NUB1; -.
DR PaxDb; Q9NUB1; -.
DR PeptideAtlas; Q9NUB1; -.
DR PRIDE; Q9NUB1; -.
DR ProteomicsDB; 27173; -.
DR ProteomicsDB; 30036; -.
DR ProteomicsDB; 82660; -. [Q9NUB1-1]
DR ProteomicsDB; 82661; -. [Q9NUB1-2]
DR Antibodypedia; 24959; 141 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 CTD; 84532; -.
DR DisGeNET; 84532; -.
DR GeneCards; ACSS1; -.
DR HGNC; HGNC:16091; ACSS1.
DR HPA; ENSG00000154930; Low tissue specificity.
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; 288915at2759; -.
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 BioGRID-ORCS; 84532; 9 hits in 1073 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 173 other tissues.
DR ExpressionAtlas; Q9NUB1; baseline and differential.
DR Genevisible; Q9NUB1; HS.
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 Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
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
