ID ACSA_MOUSE Reviewed; 701 AA.
AC Q9QXG4; Q8BK97;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=Acetyl-coenzyme A synthetase, cytoplasmic;
DE EC=6.2.1.1 {ECO:0000269|PubMed:11150295, ECO:0000269|PubMed:16790548, ECO:0000269|PubMed:28562591};
DE AltName: Full=Acetate--CoA ligase;
DE AltName: Full=Acetyl-CoA synthetase;
DE Short=ACS;
DE Short=AceCS;
DE AltName: Full=Acetyl-CoA synthetase 1 {ECO:0000303|PubMed:11150295, ECO:0000303|PubMed:16790548};
DE Short=AceCS1 {ECO:0000303|PubMed:11150295, ECO:0000303|PubMed:16790548};
DE AltName: Full=Acyl-CoA synthetase short-chain family member 2;
DE AltName: Full=Acyl-activating enzyme;
DE AltName: Full=Propionate--CoA ligase;
DE EC=6.2.1.17 {ECO:0000269|PubMed:11150295};
GN Name=Acss2; Synonyms=Acas2, Acecs1;
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 [MRNA].
RX PubMed=12049778; DOI=10.1016/s0925-4773(02)00097-7;
RA Loikkanen I., Haghighi S., Vainio S., Pajunen A.;
RT "Expression of cytosolic acetyl-CoA synthetase gene is developmentally
RT regulated.";
RL Mech. Dev. 115:139-141(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=11150295; DOI=10.1074/jbc.m008782200;
RA Fujino T., Kondo J., Ishikawa M., Morikawa K., Yamamoto T.T.;
RT "Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the
RT oxidation of acetate.";
RL J. Biol. Chem. 276:11420-11426(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, ACETYLATION AT LYS-661,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16790548; DOI=10.1073/pnas.0604392103;
RA Hallows W.C., Lee S., Denu J.M.;
RT "Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10230-10235(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-263; SER-265 AND
RP SER-267, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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 [11]
RP SUBCELLULAR LOCATION.
RX PubMed=28552616; DOI=10.1016/j.molcel.2017.04.026;
RA Li X., Yu W., Qian X., Xia Y., Zheng Y., Lee J.H., Li W., Lyu J., Rao G.,
RA Zhang X., Qian C.N., Rozen S.G., Jiang T., Lu Z.;
RT "Nucleus-Translocated ACSS2 Promotes Gene Transcription for Lysosomal
RT Biogenesis and Autophagy.";
RL Mol. Cell 66:684-697(2017).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH CREBBP.
RX PubMed=28562591; DOI=10.1038/nature22405;
RA Mews P., Donahue G., Drake A.M., Luczak V., Abel T., Berger S.L.;
RT "Acetyl-CoA synthetase regulates histone acetylation and hippocampal
RT memory.";
RL Nature 546:381-386(2017).
CC -!- FUNCTION: Catalyzes the synthesis of acetyl-CoA from short-chain fatty
CC acids (PubMed:11150295, PubMed:16790548, PubMed:28562591). Acetate is
CC the preferred substrate but can also utilize propionate with a much
CC lower affinity (PubMed:11150295). Nuclear ACSS2 promotes glucose
CC deprivation-induced lysosomal biogenesis and autophagy, tumor cell
CC survival and brain tumorigenesis (By similarity). Glucose deprivation
CC results in AMPK-mediated phosphorylation of ACSS2 leading to its
CC translocation to the nucleus where it binds to TFEB and locally
CC produces acetyl-CoA for histone acetylation in the promoter regions of
CC TFEB target genes thereby activating their transcription (By
CC similarity). The regulation of genes associated with autophagy and
CC lysosomal activity through ACSS2 is important for brain tumorigenesis
CC and tumor survival (By similarity). Acts as a chromatin-bound
CC transcriptional coactivator that up-regulates histone acetylation and
CC expression of neuronal genes (PubMed:28562591). Can be recruited to the
CC loci of memory-related neuronal genes to maintain a local acetyl-CoA
CC pool, providing the substrate for histone acetylation and promoting the
CC expression of specific genes, which is essential for maintaining long-
CC term spatial memory (PubMed:28562591). {ECO:0000250|UniProtKB:Q9NR19,
CC ECO:0000269|PubMed:11150295, ECO:0000269|PubMed:16790548,
CC ECO:0000269|PubMed:28562591}.
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:11150295, ECO:0000269|PubMed:16790548,
CC ECO:0000269|PubMed:28562591};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC Evidence={ECO:0000305|PubMed:11150295, ECO:0000305|PubMed:16790548};
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:0000269|PubMed:11150295};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC Evidence={ECO:0000305|PubMed:11150295};
CC -!- ACTIVITY REGULATION: Inhibited by acetylation at Lys-661 and activated
CC by deacetylation mediated by the deacetylases SIRT1 and SIRT3.
CC {ECO:0000269|PubMed:16790548}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for acetate {ECO:0000269|PubMed:11150295};
CC KM=3.4 mM for propionate {ECO:0000269|PubMed:11150295};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with TFEB (By similarity).
CC AMPK-mediated phosphorylated form at Ser-659 interacts with KPNA1; this
CC interaction results in nuclear translocation of ACSS2 (By similarity).
CC Interacts with the 'Thr-172' phosphorylated form of PRKAA2 (By
CC similarity). Interacts with CREBBP (PubMed:28562591).
CC {ECO:0000250|UniProtKB:Q9NR19, ECO:0000269|PubMed:28562591}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11150295,
CC ECO:0000269|PubMed:28552616}. Cytoplasm {ECO:0000269|PubMed:28562591}.
CC Nucleus {ECO:0000269|PubMed:28552616, ECO:0000269|PubMed:28562591}.
CC Note=Glucose deprivation results in its AMPK-dependent phosphorylation
CC and subsequent nuclear translocation. Phosphorylation at Ser-659, leads
CC to exposure of its nuclear localization signal which is required for
CC its interaction with KPNA1 and subsequent translocation to the nucleus
CC (By similarity). Found in the cytoplasm in undifferentiated neurons and
CC upon differentiation, translocates to nucleus (PubMed:28562591).
CC {ECO:0000250|UniProtKB:Q9NR19, ECO:0000269|PubMed:28562591}.
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus.
CC {ECO:0000269|PubMed:28562591}.
CC -!- PTM: Reversibly acetylated at Lys-661 (PubMed:16790548). The acetyl-CoA
CC synthase activity is inhibited by acetylation and activated by
CC deacetylation mediated by the deacetylases SIRT1 and SIRT3.
CC {ECO:0000269|PubMed:16790548}.
CC -!- DISRUPTION PHENOTYPE: Knockdown in the hippocampus decreases histone
CC acetylation and is accompanied by impaired object location memory and
CC defective up-regulation of immediate early genes following training.
CC {ECO:0000269|PubMed:28562591}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF216873; AAF24510.1; -; mRNA.
DR EMBL; AK053877; BAC35571.1; -; mRNA.
DR EMBL; AL844852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051432; AAH51432.1; -; mRNA.
DR CCDS; CCDS16950.1; -.
DR RefSeq; NP_062785.2; NM_019811.3.
DR AlphaFoldDB; Q9QXG4; -.
DR SMR; Q9QXG4; -.
DR BioGRID; 208597; 2.
DR DIP; DIP-61210N; -.
DR IntAct; Q9QXG4; 3.
DR STRING; 10090.ENSMUSP00000029135; -.
DR ChEMBL; CHEMBL2924; -.
DR iPTMnet; Q9QXG4; -.
DR PhosphoSitePlus; Q9QXG4; -.
DR SwissPalm; Q9QXG4; -.
DR EPD; Q9QXG4; -.
DR jPOST; Q9QXG4; -.
DR MaxQB; Q9QXG4; -.
DR PaxDb; 10090-ENSMUSP00000029135; -.
DR ProteomicsDB; 285543; -.
DR Pumba; Q9QXG4; -.
DR Antibodypedia; 1332; 515 antibodies from 33 providers.
DR DNASU; 60525; -.
DR Ensembl; ENSMUST00000029135.15; ENSMUSP00000029135.9; ENSMUSG00000027605.19.
DR GeneID; 60525; -.
DR KEGG; mmu:60525; -.
DR UCSC; uc008nku.1; mouse.
DR AGR; MGI:1890410; -.
DR CTD; 55902; -.
DR MGI; MGI:1890410; Acss2.
DR VEuPathDB; HostDB:ENSMUSG00000027605; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000156358; -.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q9QXG4; -.
DR OMA; INVSYNC; -.
DR OrthoDB; 144557at2759; -.
DR TreeFam; TF300417; -.
DR Reactome; R-MMU-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-MMU-71384; Ethanol oxidation.
DR BioGRID-ORCS; 60525; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Acss2; mouse.
DR PRO; PR:Q9QXG4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9QXG4; Protein.
DR Bgee; ENSMUSG00000027605; Expressed in aorta tunica adventitia and 252 other cell types or tissues.
DR ExpressionAtlas; Q9QXG4; baseline and differential.
DR Genevisible; Q9QXG4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0019413; P:acetate biosynthetic process; ISO:MGI.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IDA:MGI.
DR GO; GO:0008610; P:lipid biosynthetic process; ISO:MGI.
DR GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IMP:UniProtKB.
DR GO; GO:0019542; P:propionate biosynthetic process; ISO:MGI.
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; 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 PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF126; ACETYL-COENZYME A SYNTHETASE, CYTOPLASMIC; 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.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ATP-binding; Cytoplasm; Ligase; Lipid metabolism;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..701
FT /note="Acetyl-coenzyme A synthetase, cytoplasmic"
FT /id="PRO_0000208424"
FT REGION 1..107
FT /note="Interaction with TFEB"
FT /evidence="ECO:0000250|UniProtKB:Q9NR19"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 656..668
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9NR19"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219..222
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 439..441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 463..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 575
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 636
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 418
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR19"
FT MOD_RES 659
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q9NR19"
FT MOD_RES 661
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16790548"
FT CONFLICT 498..500
FT /note="PAI -> LQS (in Ref. 1; AAF24510)"
FT /evidence="ECO:0000305"
FT CONFLICT 655..657
FT /note="PKT -> LKP (in Ref. 1; AAF24510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 78862 MW; D1EA6312CD4527D7 CRC64;
MGLPEERRKS GSGSRAREET GAEGRVRGWS PPPEVRRSAH VPSLQRYREL HRRSVEEPRE
FWGNIAKEFY WKTACPGPFL QYNFDVTKGK IFTEWMKGAT TNICYNVLDR NVHEKKLGDK
VAFYWEGNEP GETTKITYRE LLVQVCQFSN VLRKQGIQKG DRVAIYMPMI LELVVAMLAC
ARLGALHSIV FAGFSAESLC ERILDSSCCL LITTDAFYRG EKLVNLKELA DESLEKCREK
GFPVRCCIVV KHLGRAELGM NDSPSQSPPV KRPCPDVQIC WNEGVDLWWH ELMQQAGDEC
EPEWCDAEDP LFILYTSGST GKPKGVVHTI GGYMLYVATT FKYVFDFHPE DVFWCTADIG
WITGHSYVTY GPLANGATSV LFEGIPTYPD EGRLWSIVDK YKVTKFYTAP TAIRMLMKFG
DDPVTKHSRA SLQVLGTVGE PINPEAWLWY HRVVGSQRCP IVDTFWQTET GGHMLTPLPG
ATPMKPGSAS FPFFGVAPAI LNESGEELEG EAEGYLVFKQ PWPGIMRTVY GNHTRFETTY
FKKFPGYYVT GDGCRRDQDG YYWITGRIDD MLNVSGHLLS TAEVESALVE HEAVAEAAVV
GHPHPVKGEC LYCFVTLCDG HTFSPTLTEE LKKQIREKIG PIATPDYIQN APGLPKTRSG
KIMRRVLRKI AQNDHDLGDT STVADPSVIN HLFSHRCLTT Q
//
