Choline acetyltransferase

Choline acetyltransferase
Identifiers
EC number	2.3.1.6
CAS number	9012-78-6
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles

Choline O-acetyltransferase
PDB rendering based on 2fy2.
Available structures PDB 2FY2, 2FY3, 2FY4, 2FY5
Identifiers
Symbols	CHAT; CHOACTASE; CMS1A; CMS1A2
External IDs	OMIM: 118490 MGI: 88392 HomoloGene: 40693 GeneCards: CHAT Gene
EC number	2.3.1.6
Gene Ontology Molecular function • choline O-acetyltransferase activity • acyltransferase activity • transferase activity Cellular component • nucleus • cytoplasm • mitochondrion • cytosol • axon • neuronal cell body Biological process • synaptic transmission • neurotransmitter secretion • neuromuscular synaptic transmission • muscle organ development • establishment of synaptic specificity at neuromuscular junction • rhythmic behavior • adult walking behavior • dendrite development • neuron differentiation • neurotransmitter biosynthetic process • rhythmic excitation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1103	12647
Ensembl	ENSG00000070748	ENSMUSG00000021919
UniProt	P28329	Q8BQN4
RefSeq (mRNA)	NM_001142929.1	NM_009891.2
RefSeq (protein)	NP_001136401.1	NP_034021.1
Location (UCSC)	Chr 10: 50.82 – 50.9 Mb	Chr 14: 33.22 – 33.28 Mb
PubMed search	[1]	[2]

Choline acetyltransferase (abbreviated "ChAT") is an enzyme that is synthesized within the body of a neuron. It is then transferred to the nerve terminal via axoplasmic flow. The role of choline acetyltransferase is to join Acetyl-CoA to choline, resulting in the formation of the neurotransmitter acetylcholine.^[1] In humans, the choline acetyltransferase enyzme is encoded by the CHAT gene.^[2]

Function

Cholinergic systems are implicated in numerous neurologic functions. Alteration in some cholinergic neurons may account for the disturbances of Alzheimer disease. The protein encoded by this gene synthesizes the neurotransmitter acetylcholine. Alternative splice variants that contain alternative 5' untranslated exons have been found. Three of the four described splice variants encode identical 69 kDa proteins, while one variant encodes both the 69 kDa and a larger 82 kDa protein.^[1]

• 

  Choline

• 

  Acetylcholine

It is often used as an immunohistochemical marker for motor neurons (motoneurons).

See also

• Acetyltransferase

References

1. ^ ^{a b} "Entrez Gene: CHAT choline acetyltransferase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1103. 
2. ^ Strauss WL, Kemper RR, Jayakar P, Kong CF, Hersh LB, Hilt DC, Rabin M (February 1991). "Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization". Genomics 9 (2): 396–8. doi:10.1016/0888-7543(91)90273-H. PMID 1840566. 

Further reading

• Oda Y (2000). "Choline acetyltransferase: the structure, distribution and pathologic changes in the central nervous system". Pathol. Int. 49 (11): 921–37. doi:10.1046/j.1440-1827.1999.00977.x. PMID 10594838. 
• Oda Y, Nakanishi I, Deguchi T (1993). "A complementary DNA for human choline acetyltransferase induces two forms of enzyme with different molecular weights in cultured cells". Brain Res. Mol. Brain Res. 16 (3–4): 287–94. doi:10.1016/0169-328X(92)90237-6. PMID 1337937. 
• Toussaint JL, Geoffroy V, Schmitt M et al. (1992). "Human choline acetyltransferase (CHAT): partial gene sequence and potential control regions". Genomics 12 (2): 412–6. doi:10.1016/0888-7543(92)90395-9. PMID 1339386. 
• Lorenzi MV, Trinidad AC, Zhang R, Strauss WL (1992). "Two mRNAs are transcribed from the human gene for choline acetyltransferase". DNA Cell Biol. 11 (8): 593–603. doi:10.1089/dna.1992.11.593. PMID 1388731. 
• Misawa H, Ishii K, Deguchi T (1992). "Gene expression of mouse choline acetyltransferase. Alternative splicing and identification of a highly active promoter region". J. Biol. Chem. 267 (28): 20392–9. PMID 1400357. 
• Cervini R, Rocchi M, DiDonato S, Finocchiaro G (1992). "Isolation and sub-chromosomal localization of a DNA fragment of the human choline acetyltransferase gene". Neurosci. Lett. 132 (2): 191–4. doi:10.1016/0304-3940(91)90299-9. PMID 1784419. 
• Strauss WL, Kemper RR, Jayakar P et al. (1991). "Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization". Genomics 9 (2): 396–8. doi:10.1016/0888-7543(91)90273-H. PMID 1840566. 
• Viegas-Péquignot E, Berrard S, Brice A et al. (1991). "Localization of a 900-bp-long fragment of the human choline acetyltransferase gene to 10q11.2 by nonradioactive in situ hybridization". Genomics 9 (1): 210–2. doi:10.1016/0888-7543(91)90242-7. PMID 2004764. 
• Itoh N, Slemmon JR, Hawke DH et al. (1986). "Cloning of Drosophila choline acetyltransferase cDNA". Proc. Natl. Acad. Sci. U.S.A. 83 (11): 4081–5. doi:10.1073/pnas.83.11.4081. PMC 323670. PMID 3086876. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=323670. 
• Hersh LB, Takane K, Gylys K et al. (1988). "Conservation of amino acid sequences between human and porcine choline acetyltransferase". J. Neurochem. 51 (6): 1843–5. doi:10.1111/j.1471-4159.1988.tb01166.x. PMID 3183663. 
• Berrard S, Brice A, Lottspeich F et al. (1988). "cDNA cloning and complete sequence of porcine choline acetyltransferase: in vitro translation of the corresponding RNA yields an active protein". Proc. Natl. Acad. Sci. U.S.A. 84 (24): 9280–4. doi:10.1073/pnas.84.24.9280. PMC 373252. PMID 3480542. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=373252. 
• Chireux MA, Le Van Thai A, Weber MJ (1995). "Human choline acetyltransferase gene: localization of alternative first exons". J. Neurosci. Res. 40 (4): 427–38. doi:10.1002/jnr.490400402. PMID 7616604. 
• Bausero P, Schmitt M, Toussaint JL et al. (1993). "Identification and analysis of the human choline acetyltransferase gene promoter". Neuroreport 4 (3): 287–90. doi:10.1097/00001756-199303000-00015. PMID 7682855. 
• Quirin-Stricker C, Nappey V, Simoni P et al. (1994). "Trans-activation by thyroid hormone receptors of the 5' flanking region of the human ChAT gene". Brain Res. Mol. Brain Res. 23 (3): 253–65. doi:10.1016/0169-328X(94)90232-1. PMID 8057782. 
• Erickson JD, Varoqui H, Schäfer MK et al. (1994). "Functional identification of a vesicular acetylcholine transporter and its expression from a "cholinergic" gene locus". J. Biol. Chem. 269 (35): 21929–32. PMID 8071310. 
• Kengaku M, Misawa H, Deguchi T (1993). "Multiple mRNA species of choline acetyltransferase from rat spinal cord". Brain Res. Mol. Brain Res. 18 (1–2): 71–6. doi:10.1016/0169-328X(93)90174-N. PMID 8479291. 
• Misawa H, Matsuura J, Oda Y et al. (1997). "Human choline acetyltransferase mRNAs with different 5'-region produce a 69-kDa major translation product". Brain Res. Mol. Brain Res. 44 (2): 323–33. doi:10.1016/S0169-328X(96)00231-8. PMID 9073174. 
• Lönnerberg P, Ibáñez CF (1999). "Novel, testis-specific mRNA transcripts encoding N-terminally truncated choline acetyltransferase". Mol. Reprod. Dev. 53 (3): 274–81. doi:10.1002/(SICI)1098-2795(199907)53:3<274::AID-MRD3>3.0.CO;2-8. PMID 10369388. 
• Sakakibara A, Hattori S (2000). "Chat, a Cas/HEF1-associated adaptor protein that integrates multiple signaling pathways". J. Biol. Chem. 275 (9): 6404–10. doi:10.1074/jbc.275.9.6404. PMID 10692442. 

External links

• MeSH Choline+Acetyltransferase

2fy3: Structures of ligand bound human choline acetyltransferase provides insight into regulation of acetylcholine synthesis

2fy4: Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis

2fy5: Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis