Hmdb loader
Identification
HMDB Protein ID HMDBP00524
Secondary Accession Numbers
  • 5772
  • HMDBP06048
Name Acetylcholinesterase
Synonyms
  1. AChE
Gene Name ACHE
Protein Type Enzyme
Biological Properties
General Function Involved in carboxylesterase activity
Specific Function Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.
Pathways
  • Cholinergic synapse
  • Glycerophospholipid metabolism
  • Phospholipid Biosynthesis
Reactions
Acetylcholine + Water → Choline + Acetic acid details
GO Classification
Biological Process
acetylcholine catabolic process in synaptic cleft
amyloid precursor protein metabolic process
cell adhesion
cell proliferation
choline metabolic process
DNA replication
muscle organ development
negative regulation of synaptic transmission, cholinergic
neurotransmitter biosynthetic process
neurotransmitter receptor biosynthetic process
osteoblast development
phosphatidylcholine biosynthetic process
positive regulation of protein secretion
receptor internalization
regulation of axonogenesis
regulation of dendrite morphogenesis
regulation of receptor recycling
response to wounding
retina development in camera-type eye
synapse assembly
protein tetramerization
Cellular Component
cell surface
anchored to membrane
plasma membrane
basal lamina
cell junction
dendrite
endoplasmic reticulum lumen
Golgi apparatus
neuromuscular junction
perinuclear region of cytoplasm
postsynaptic membrane
presynaptic membrane
synaptic cleft
nucleus
extracellular space
axon
Component
membrane
cell part
Function
cholinesterase activity
hydrolase activity, acting on ester bonds
catalytic activity
hydrolase activity
carboxylesterase activity
Molecular Function
acetylcholine binding
acetylcholinesterase activity
beta-amyloid binding
collagen binding
laminin binding
carboxylesterase activity
serine hydrolase activity
protein homodimerization activity
Cellular Location
  1. Lipid-anchor
  2. Extracellular side
  3. Isoform H:Cell membrane
  4. GPI- anchor
Gene Properties
Chromosome Location 7
Locus 7q22
SNPs ACHE
Gene Sequence
>1845 bp
ATGAGGCCCCCGCAGTGTCTGCTGCACACGCCTTCCCTGGCTTCCCCACTCCTTCTCCTC
CTCCTCTGGCTCCTGGGTGGAGGAGTGGGGGCTGAGGGCCGGGAGGATGCAGAGCTGCTG
GTGACGGTGCGTGGGGGCCGGCTGCGGGGCATTCGCCTGAAGACCCCCGGGGGCCCTGTC
TCTGCTTTCCTGGGCATCCCCTTTGCGGAGCCACCCATGGGACCCCGTCGCTTTCTGCCA
CCGGAGCCCAAGCAGCCTTGGTCAGGGGTGGTAGACGCTACAACCTTCCAGAGTGTCTGC
TACCAATATGTGGACACCCTATACCCAGGTTTTGAGGGCACCGAGATGTGGAACCCCAAC
CGTGAGCTGAGCGAGGACTGCCTGTACCTCAACGTGTGGACACCATACCCCCGGCCTACA
TCCCCCACCCCTGTCCTCGTCTGGATCTATGGGGGTGGCTTCTACAGTGGGGCCTCCTCC
TTGGACGTGTACGATGGCCGCTTCTTGGTACAGGCCGAGAGGACTGTGCTGGTGTCCATG
AACTACCGGGTGGGAGCCTTTGGCTTCCTGGCCCTGCCGGGGAGCCGAGAGGCCCCGGGC
AATGTGGGTCTCCTGGATCAGAGGCTGGCCCTGCAGTGGGTGCAGGAGAACGTGGCAGCC
TTCGGGGGTGACCCGACATCAGTGACGCTGTTTGGGGAGAGCGCGGGAGCCGCCTCGGTG
GGCATGCACCTGCTGTCCCCGCCCAGCCGGGGCCTGTTCCACAGGGCCGTGCTGCAGAGC
GGTGCCCCCAATGGACCCTGGGCCACGGTGGGCATGGGAGAGGCCCGTCGCAGGGCCACG
CAGCTGGCCCACCTTGTGGGCTGTCCTCCAGGCGGCACTGGTGGGAATGACACAGAGCTG
GTAGCCTGCCTTCGGACACGACCAGCGCAGGTCCTGGTGAACCACGAATGGCACGTGCTG
CCTCAAGAAAGCGTCTTCCGGTTCTCCTTCGTGCCTGTGGTAGATGGAGACTTCCTCAGT
GACACCCCAGAGGCCCTCATCAACGCGGGAGACTTCCACGGCCTGCAGGTGCTGGTGGGT
GTGGTGAAGGATGAGGGCTCGTATTTTCTGGTTTACGGGGCCCCAGGCTTCAGCAAAGAC
AACGAGTCTCTCATCAGCCGGGCCGAGTTCCTGGCCGGGGTGCGGGTCGGGGTTCCCCAG
GTAAGTGACCTGGCAGCCGAGGCTGTGGTCCTGCATTACACAGACTGGCTGCATCCCGAG
GACCCGGCACGCCTGAGGGAGGCCCTGAGCGATGTGGTGGGCGACCACAATGTCGTGTGC
CCCGTGGCCCAGCTGGCTGGGCGACTGGCTGCCCAGGGTGCCCGGGTCTACGCCTACGTC
TTTGAACACCGTGCTTCCACGCTCTCCTGGCCCCTGTGGATGGGGGTGCCCCACGGCTAC
GAGATCGAGTTCATCTTTGGGATCCCCCTGGACCCCTCTCGAAACTACACGGCAGAGGAG
AAAATCTTCGCCCAGCGACTGATGCGATACTGGGCCAACTTTGCCCGCACAGGGGATCCC
AATGAGCCCCGAGACCCCAAGGCCCCACAATGGCCCCCGTACACGGCGGGGGCTCAGCAG
TACGTTAGTCTGGACCTGCGGCCGCTGGAGGTGCGGCGGGGGCTGCGCGCCCAGGCCTGC
GCCTTCTGGAACCGCTTCCTCCCCAAATTGCTCAGCGCCACCGACACGCTCGACGAGGCG
GAGCGCCAGTGGAAGGCCGAGTTCCACCGCTGGAGCTCCTACATGGTGCACTGGAAGAAC
CAGTTCGACCACTACAGCAAGCAGGATCGCTGCTCAGACCTGTGA
Protein Properties
Number of Residues 614
Molecular Weight 67795.525
Theoretical pI 6.291
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Acetylcholinesterase
MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV
SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN
RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM
NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV
GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL
VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG
VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE
DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY
EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ
YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQDRCSDL
GenBank ID Protein 177975
UniProtKB/Swiss-Prot ID P22303
UniProtKB/Swiss-Prot Entry Name ACES_HUMAN
PDB IDs
GenBank Gene ID M55040
GeneCard ID ACHE
GenAtlas ID ACHE
HGNC ID HGNC:108
References
General References
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  4. Soreq H, Ben-Aziz R, Prody CA, Seidman S, Gnatt A, Neville L, Lieman-Hurwitz J, Lev-Lehman E, Ginzberg D, Lipidot-Lifson Y, et al.: Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9688-92. [PubMed:2263619 ]
  5. Karpel R, Ben Aziz-Aloya R, Sternfeld M, Ehrlich G, Ginzberg D, Tarroni P, Clementi F, Zakut H, Soreq H: Expression of three alternative acetylcholinesterase messenger RNAs in human tumor cell lines of different tissue origins. Exp Cell Res. 1994 Feb;210(2):268-77. [PubMed:8299725 ]
  6. Wilson MD, Riemer C, Martindale DW, Schnupf P, Boright AP, Cheung TL, Hardy DM, Schwartz S, Scherer SW, Tsui LC, Miller W, Koop BF: Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5. Nucleic Acids Res. 2001 Mar 15;29(6):1352-65. [PubMed:11239002 ]
  7. Chhajlani V, Derr D, Earles B, Schmell E, August T: Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase. FEBS Lett. 1989 Apr 24;247(2):279-82. [PubMed:2714437 ]
  8. Velan B, Grosfeld H, Kronman C, Leitner M, Gozes Y, Lazar A, Flashner Y, Marcus D, Cohen S, Shafferman A: The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant. J Biol Chem. 1991 Dec 15;266(35):23977-84. [PubMed:1748670 ]
  9. Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D, et al.: Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J Biol Chem. 1992 Sep 5;267(25):17640-8. [PubMed:1517212 ]
  10. Yang L, He HY, Zhang XJ: Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells. Neurosci Res. 2002 Apr;42(4):261-8. [PubMed:11985878 ]
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  12. Kryger G, Harel M, Giles K, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL: Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II. Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1385-94. [PubMed:11053835 ]
  13. Dvir H, Harel M, Bon S, Liu WQ, Vidal M, Garbay C, Sussman JL, Massoulie J, Silman I: The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. EMBO J. 2004 Nov 10;23(22):4394-405. Epub 2004 Nov 4. [PubMed:15526038 ]
  14. Bartels CF, Zelinski T, Lockridge O: Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polymorphism. Am J Hum Genet. 1993 May;52(5):928-36. [PubMed:8488842 ]