LOCUS       NP_001101263             701 aa            linear   ROD 23-MAR-2023
DEFINITION  acetyl-coenzyme A synthetase, cytoplasmic [Rattus norvegicus].
ACCESSION   NP_001101263 XP_001064684 XP_230773
VERSION     NP_001101263.1
DBSOURCE    REFSEQ: accession NM_001107793.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Li Z, Sun T, He Z, Li Z, Zhang W, Wang J and Xiang H.
  TITLE     SCFAs Ameliorate Chronic Postsurgical Pain-Related Cognition
            Dysfunction via the ACSS2-HDAC2 Axis in Rats
  JOURNAL   Mol Neurobiol 59 (10), 6211-6227 (2022)
   PUBMED   35902549
  REMARK    GeneRIF: SCFAs Ameliorate Chronic Postsurgical Pain-Related
            Cognition Dysfunction via the ACSS2-HDAC2 Axis in Rats.
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Krencz I, Sebestyen A, Papay J, Jeney A, Hujber Z, Burger CD,
            Keller CA and Khoor A.
  TITLE     In situ analysis of mTORC1/2 and cellular metabolism-related
            proteins in human Lymphangioleiomyomatosis
  JOURNAL   Hum Pathol 79, 199-207 (2018)
   PUBMED   29885404
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Dodhia S, Celis K, Aylward A, Cai Y, Fontana ME, Trespalacios A,
            Hoffman DC, Alfonso HO, Eisig SB, Su GH, Chung WK and Haddad J Jr.
  TITLE     ACSS2 gene variant associated with cleft lip and palate in two
            independent Hispanic populations
  JOURNAL   Laryngoscope 127 (10), E336-E339 (2017)
   PUBMED   28543373
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Yoshimura Y, Araki A, Maruta H, Takahashi Y and Yamashita H.
  TITLE     Molecular cloning of rat acss3 and characterization of mammalian
            propionyl-CoA synthetase in the liver mitochondrial matrix
  JOURNAL   J Biochem 161 (3), 279-289 (2017)
   PUBMED   28003429
REFERENCE   5  (residues 1 to 701)
  AUTHORS   Lakhter AJ, Hamilton J, Konger RL, Brustovetsky N, Broxmeyer HE and
            Naidu SR.
  TITLE     Glucose-independent Acetate Metabolism Promotes Melanoma Cell
            Survival and Tumor Growth
  JOURNAL   J Biol Chem 291 (42), 21869-21879 (2016)
   PUBMED   27539851
REFERENCE   6  (residues 1 to 701)
  AUTHORS   Watkins PA, Maiguel D, Jia Z and Pevsner J.
  TITLE     Evidence for 26 distinct acyl-coenzyme A synthetase genes in the
            human genome
  JOURNAL   J Lipid Res 48 (12), 2736-2750 (2007)
   PUBMED   17762044
REFERENCE   7  (residues 1 to 701)
  AUTHORS   Hallows WC, Lee S and Denu JM.
  TITLE     Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
  JOURNAL   Proc Natl Acad Sci U S A 103 (27), 10230-10235 (2006)
   PUBMED   16790548
REFERENCE   8  (residues 1 to 701)
  AUTHORS   Fujino T, Kondo J, Ishikawa M, Morikawa K and Yamamoto TT.
  TITLE     Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in
            the oxidation of acetate
  JOURNAL   J Biol Chem 276 (14), 11420-11426 (2001)
   PUBMED   11150295
REFERENCE   9  (residues 1 to 701)
  AUTHORS   Luong A, Hannah VC, Brown MS and Goldstein JL.
  TITLE     Molecular characterization of human acetyl-CoA synthetase, an
            enzyme regulated by sterol regulatory element-binding proteins
  JOURNAL   J Biol Chem 275 (34), 26458-26466 (2000)
   PUBMED   10843999
REFERENCE   10 (residues 1 to 701)
  AUTHORS   Barth,C., Sladek,M. and Decker,K.
  TITLE     The subcellular distribution of short-chain fatty acyl-CoA
            synthetase activity in rat tissues
  JOURNAL   Biochim Biophys Acta 248 (1), 24-33 (1971)
   PUBMED   4334748
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474050.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_230773.4, XP_001064684.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..701
                     /product="acetyl-coenzyme A synthetase, cytoplasmic"
                     /EC_number="6.2.1.1"
                     /note="acetyl-Coenzyme A synthetase 2 (ADP forming)"
                     /calculated_mol_wt=78757
     Region          45..685
                     /region_name="ACS"
                     /note="Acetyl-CoA synthetase (also known as acetate-CoA
                     ligase and acetyl-activating enzyme); cd05966"
                     /db_xref="CDD:341270"
     Site            order(191..193,219,222,224,357,362..363,385..387,411..412,
                     415,438..441,463..468,552,564,567,575..578,636,641..642)
                     /site_type="active"
                     /db_xref="CDD:341270"
     Site            order(191..193,219,222,224,357,363,385..387,411..412,415,
                     575..577,636,641)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341270"
     Site            order(313,316..321,323..324)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341270"
     Site            order(362..363,438..441,463..468,552,564,567,578)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341270"
     Site            order(362..363,438..439,466)
                     /site_type="other"
                     /note="acetate binding site [chemical binding]"
                     /db_xref="CDD:341270"
     CDS             1..701
                     /gene="Acss2"
                     /gene_synonym="Acas2"
                     /coded_by="NM_001107793.1:65..2170"
                     /db_xref="GeneID:311569"
                     /db_xref="RGD:1305489"
ORIGIN      
        1 mglpeerrks gsgsrareet gaegrvrgws pppevrrsah vpslqryrel hrrsveepre
       61 fwgniakefy wktpcpgpfl qynfdvtkgk iftewmkgat tnicynvldr nvhekklgdk
      121 vafywegnep gettkityre llvqvcqfsn vlrkqgvqkg drvaiympmi lelvvamlac
      181 arlgalhsiv fagfsaeslc erildssccl littdafyrg eklvnlkela deslekcrek
      241 gfpvrccivv khlgraelgm ndspsqsppv krpcpdvqis wnegvdlwwh elmqqagdef
      301 epewcdaedp lfilytsgst gkpkgvvhtv ggymlyvatt fkyvfdfhpe dvfwctadig
      361 witghsyvty gplangatsv lfegiptypd egrlwsivdk ykvtkfytap tairmlmkfg
      421 ddpvtkhsra slqvlgtvge pinpeawlwy hrvvgsqrcp ivdtfwqtet gghmltplpg
      481 atpmkpgsas fpffgvapai lnesgeeleg eaegylvfkq pwpgimrtvy gnhtrfetty
      541 fkkfpgyyvt gdgcrrdqdg yywitgridd mlnvsghlls taevesalve heavaeaavv
      601 ghphpvkgec lycfvtlcdg htfsptltee lkkqirekig piatpdyiqn apglpktrsg
      661 kimrrvlrki aqndhdlgdt stvadpsvin hlfshrcltt q
//
