LOCUS       NP_742006                614 aa            linear   ROD 04-FEB-2025
DEFINITION  acetylcholinesterase precursor [Rattus norvegicus].
ACCESSION   NP_742006 XP_038945767
VERSION     NP_742006.2
DBSOURCE    REFSEQ: accession NM_172009.3
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 614)
  AUTHORS   Crews,F.T., Fisher,R.P., Qin,L. and Vetreno,R.P.
  TITLE     HMGB1 neuroimmune signaling and REST-G9a gene repression contribute
            to ethanol-induced reversible suppression of the cholinergic neuron
            phenotype
  JOURNAL   Mol Psychiatry 28 (12), 5159-5172 (2023)
   PUBMED   37402853
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Javed,T., Habib,R., Ghafoor,S., Rumman,B., Awan,S., Ntepe,L.J.M.,
            Batool,S. and Nurulain,S.M.
  TITLE     Association of status of acetylcholinesterase and ACHE gene 3' UTR
            variants (rs17228602, rs17228616) with drug addiction vulnerability
            in pakistani population
  JOURNAL   Chem Biol Interact 308, 130-136 (2019)
   PUBMED   31129131
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Wu,J., Jin,T., Wang,H. and Li,S.T.
  TITLE     Sepsis decreases the activity of acetylcholinesterase by reducing
            its expression at the neuromuscular junction
  JOURNAL   Mol Med Rep 16 (4), 5263-5268 (2017)
   PUBMED   28849127
  REMARK    GeneRIF: sepsis decreased AChE activity by reducing its expression
            at the neuromuscular junction.
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Del Pino,J., Moyano,P., Diaz,G.G., Anadon,M.J., Diaz,M.J.,
            Garcia,J.M., Lobo,M., Pelayo,A., Sola,E. and Frejo,M.T.
  TITLE     Primary hippocampal neuronal cell death induction after acute and
            repeated paraquat exposures mediated by AChE variants alteration
            and cholinergic and glutamatergic transmission disruption
  JOURNAL   Toxicology 390, 88-99 (2017)
   PUBMED   28916328
  REMARK    GeneRIF: Paraquat-induced death of hippocampal neurons was
            partially mediated by AChE variants inducing and cholinergic and
            gultamatergic transmission disruption.
REFERENCE   5  (residues 1 to 614)
  AUTHORS   Tejero,R., Lopez-Manzaneda,M., Arumugam,S. and Tabares,L.
  TITLE     Synaptotagmin-2, and -1, linked to neurotransmission impairment and
            vulnerability in Spinal Muscular Atrophy
  JOURNAL   Hum Mol Genet 25 (21), 4703-4716 (2016)
   PUBMED   28173138
REFERENCE   6  (residues 1 to 614)
  AUTHORS   Dolgov,V.S.
  TITLE     [Sanitary and hygienic evaluation of a technological line for
            removing manure]
  JOURNAL   Veterinariia (12), 61-63 (1978)
   PUBMED   734904
REFERENCE   7  (residues 1 to 614)
  AUTHORS   Dabrowski,Z., Gregorczyk,J., Samochowiec,L., Wojcicki,J.,
            Lawczynski,L., Antoszczyk,M., Chrzanowska-Ansilewska,K., Jurek,D.
            and Sych,Z.
  TITLE     [Effect of truncal vagotomy on the exocrine function of the
            pancreas in the dog]
  JOURNAL   Pol Tyg Lek 33 (28), 1093-1095 (1978)
   PUBMED   704405
REFERENCE   8  (residues 1 to 614)
  AUTHORS   Packman,P.M., Godfrey,D.A., Williams,A.D. and Matschinsky,F.M.
  TITLE     Quantitative histochemical studies of the hypothalamus enzymes of
            acetylcholine metabolism
  JOURNAL   J Histochem Cytochem 25 (11), 1237-1246 (1977)
   PUBMED   334962
REFERENCE   9  (residues 1 to 614)
  AUTHORS   Godfrey,D.A. and Matschinsky,F.M.
  TITLE     Enzymes of the cholinergic system in islets of Langerhans
  JOURNAL   J Histochem Cytochem 23 (9), 645-651 (1975)
   PUBMED   126256
REFERENCE   10 (residues 1 to 614)
  AUTHORS   Flumerfelt,B.A. and Lewis,P.R.
  TITLE     Cholinesterase activity in the hypoglossal nucleus of the rat and
            the changes produced by axotomy: a light and electron microscopic
            study
  JOURNAL   J Anat 119 (Pt 2), 309-331 (1975)
   PUBMED   1133098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Apr 7, 2023 this sequence version replaced
            XP_038945767.1, NP_742006.1.
            
            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 :: BC094521.1, SRR26643292.47454.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..614
                     /product="acetylcholinesterase precursor"
                     /EC_number="3.1.1.7"
                     /note="glycolipid-anchored form of acetylcholinesterase"
                     /calculated_mol_wt=64869
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3346
     mat_peptide     32..614
                     /product="Acetylcholinesterase. /id=PRO_0000008590"
                     /note="propagated from UniProtKB/Swiss-Prot (P37136.1)"
                     /calculated_mol_wt=64869
     Region          37..563
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            order(151..153,233..235,238,393,397..398,433,479,482)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(234,365,478)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Site            296
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P37136.1)"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P37136.1)"
     Site            495
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P37136.1)"
     Region          578..611
                     /region_name="AChE_tetra"
                     /note="Acetylcholinesterase tetramerization domain;
                     pfam08674"
                     /db_xref="CDD:430146"
     CDS             1..614
                     /gene="Ache"
                     /coded_by="NM_172009.3:110..1954"
                     /db_xref="GeneID:83817"
                     /db_xref="RGD:69313"
ORIGIN      
        1 mrppwyplht pslaspllfl llsllgggar aegredpqll vrvrggqlrg irlkapggpv
       61 saflgipfae ppvgsrrfmp pepkrpwsgi ldattfqnvc yqyvdtlypg fegtemwnpn
      121 relsedclyl nvwtpyprpt sptpvliwiy gggfysgass ldvydgrfla qvegtvlvsm
      181 nyrvgtfgfl alpgsrdapg nvglldqrla lqwvqeniaa fggdpmsvtl fgesagaasv
      241 gmhilslpsr slfhravlqs gtpngpwatv sagearrrat llarlvgcpp ggaggndtel
      301 isclrtrpaq dlvdhewhvl pqesifrfsf vpvvdgdfls dtpealintg dfqdlqvlvg
      361 vvkdegsyfl vygvpgfskd neslisraqf lagvrigvpq asdlaaeavv lhytdwlhpe
      421 dpahlrdams avvgdhnvvc pvaqlagrla aqgarvyayi fehrastltw plwmgvphgy
      481 eiefifglpl dpslnytvee rifaqrlmky wtnfartgdp ndprdskspr wppyttaaqq
      541 yvslnlkple vrrglraqtc afwnrflpkl lsatdtldea erqwkaefhr wssymvhwkn
      601 qfdhyskqer csdl
//
