[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Spinal cord; DOI=10.1016/0169-328X(90)90092-R; PubMed=2160042 [NCBI, ExPASy, EBI, Israel, Japan] Ishii K., Oda Y., Ichikawa T., Deguchi T.; "Complementary DNAs for choline acetyltransferase from spinal cords of rat and mouse: nucleotide sequences, expression in mammalian cells, and in situ hybridization."; Brain Res. Mol. Brain Res. 7:151-159(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32. TISSUE=Spinal cord; DOI=10.1016/0169-328X(93)90174-N; PubMed=8479291 [NCBI, ExPASy, EBI, Israel, Japan] Kengaku M., Misawa H., Deguchi T.; "Multiple mRNA species of choline acetyltransferase from rat spinal cord."; Brain Res. Mol. Brain Res. 18:71-76(1993).
[3]	MUTAGENESIS OF ARG-453. DOI=10.1074/jbc.270.49.29111; PubMed=7493935 [NCBI, ExPASy, EBI, Israel, Japan] Wu D., Hersh L.B.; "Identification of an active site arginine in rat choline acetyltransferase by alanine scanning mutagenesis."; J. Biol. Chem. 270:29111-29116(1995).
[4]	X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), AND SUBUNIT. DOI=10.1016/j.jsb.2004.06.005; PubMed=15477102 [NCBI, ExPASy, EBI, Israel, Japan] Govindasamy L., Pedersen B., Lian W., Kukar T., Gu Y., Jin S., Agbandje-McKenna M., Wu D., McKenna R.; "Structural insights and functional implications of choline acetyltransferase."; J. Struct. Biol. 148:226-235(2004).
[5]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-634 IN COMPLEX WITH COENZYME A. DOI=10.1038/sj.emboj.7600221; PubMed=15131697 [NCBI, ExPASy, EBI, Israel, Japan] Cai Y., Cronin C.N., Engel A.G., Ohno K., Hersh L.B., Rodgers D.W.; "Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders."; EMBO J. 23:2047-2058(2004).

Comments

FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
CATALYTIC ACTIVITY: Acetyl-CoA + choline = CoA + O-acetylcholine.
SUBUNIT: Monomer.
SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M88488; -; NOT_ANNOTATED_CDS; Genomic_DNA.

[EMBL / GenBank / DDBJ]

IPI00190700; -.

A48319; A48319.

3D structure databases

PDB

1Q6X; X-ray; 2.50 A; A/B=1-634.	[ExPASy / RCSB / EBI]
1T1U; X-ray; 1.55 A; A=2-640.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1Q6X; -.
1T1U; -.

ModBase

P32738.

Enzyme and pathway databases

BRENDA

2.3.1.6; 248.

Organism-specific databases

RGD

1304627; Chat.

Gene expression databases

ArrayExpress

P32738; -.

GermOnline

ENSRNOG00000025012; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from RGD).
GO:0019717;	Cellular component: synaptosome (inferred from direct assay from RGD).
GO:0033265;	Molecular function: choline binding (inferred from direct assay from RGD).
GO:0004102;	Molecular function: choline O-acetyltransferase activity (inferred from direct assay from RGD).
GO:0008292;	Biological process: acetylcholine biosynthetic process (inferred from direct assay from RGD).
GO:0001547;	Biological process: antral ovarian follicle growth (inferred from expression pattern from RGD).
GO:0007613;	Biological process: memory (inferred from mutant phenotype from RGD).
GO:0042493;	Biological process: response to drug (inferred from expression pattern from RGD).
GO:0045471;	Biological process: response to ethanol (inferred from expression pattern from RGD).
GO:0001666;	Biological process: response to hypoxia (inferred from expression pattern from RGD).
GO:0007584;	Biological process: response to nutrient (inferred from expression pattern from RGD).
QuickGo view.

Family and domain databases

InterPro

IPR000542; Carn_acyl_trans.
Graphical view of domain structure.

PANTHER

PTHR22589; Carn_acyl_trans; 1.

Pfam

PF00755; Carn_acyltransf; 1.
Pfam graphical view of domain structure.

PROSITE

PS00439; ACYLTRANSF_C_1; 1.
PS00440; ACYLTRANSF_C_2; 1.

Genome annotation databases

Ensembl

ENSRNOG00000025012; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P32738; -.

Other

ProtoNet

P32738.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acyltransferase; Neurotransmitter biosynthesis; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 640`	`639`	`Choline O-acetyltransferase.`	`PRO_0000210157`
`REGION`	`412 424`	`13`	`Coenzyme A binding (Probable).`
`ACT_SITE`	`334 334`		`Proton acceptor (By similarity).`
`BINDING`	`450 450`		`Coenzyme A (By similarity).`
`BINDING`	`551 551`		`Coenzyme A (By similarity).`
`MUTAGEN`	`453 453`		`R->A,E,Q: Increases KM for coenzyme A and acetylcholine.`
`HELIX`	`31 42`	`12`
`HELIX`	`43 45`	`3`
`HELIX`	`48 61`	`14`
`HELIX`	`67 81`	`15`
`STRAND`	`82 84`	`3`
`HELIX`	`87 94`	`8`
`TURN`	`95 97`	`3`
`HELIX`	`102 105`	`4`
`STRAND`	`109 112`	`4`
`HELIX`	`120 143`	`24`
`STRAND`	`151 153`	`3`
`STRAND`	`156 158`	`3`
`HELIX`	`165 167`	`3`
`TURN`	`168 170`	`3`
`STRAND`	`171 174`	`4`
`STRAND`	`177 179`	`3`
`STRAND`	`181 184`	`4`
`STRAND`	`188 191`	`4`
`STRAND`	`195 200`	`6`
`STRAND`	`203 211`	`9`
`HELIX`	`218 232`	`15`
`HELIX`	`242 247`	`6`
`HELIX`	`250 260`	`11`
`HELIX`	`264 274`	`11`
`STRAND`	`279 282`	`4`
`HELIX`	`292 301`	`10`
`TURN`	`305 310`	`6`
`STRAND`	`316 322`	`7`
`STRAND`	`328 332`	`5`
`HELIX`	`339 353`	`15`
`STRAND`	`361 363`	`3`
`HELIX`	`381 400`	`20`
`STRAND`	`401 408`	`8`
`HELIX`	`413 418`	`6`
`HELIX`	`423 439`	`17`
`STRAND`	`445 450`	`6`
`STRAND`	`459 462`	`4`
`HELIX`	`467 474`	`8`
`STRAND`	`476 479`	`4`
`STRAND`	`481 483`	`3`
`HELIX`	`485 507`	`23`
`HELIX`	`513 525`	`13`
`HELIX`	`532 535`	`4`
`HELIX`	`537 542`	`6`
`STRAND`	`546 551`	`6`
`STRAND`	`555 561`	`7`
`STRAND`	`570 576`	`7`
`STRAND`	`581 588`	`8`
`HELIX`	`596 614`	`19`

Sequence information

Length: 640 AA [This is the length of the unprocessed precursor]

Molecular weight: 71864 Da [This is the MW of the unprocessed precursor]

CRC64: E5FEA20EBBFA2EC6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPILEKAPQK MPVKASSWEE LDLPKLPVPP LQQTLATYLQ CMQHLVPEEQ FRKSQAIVKR 

        70         80         90        100        110        120 
FGAPGGLGET LQEKLLERQE KTANWVSEYW LNDMYLNNRL ALPVNSSPAV IFARQHFQDT 

       130        140        150        160        170        180 
NDQLRFAACL ISGVLSYKTL LDSHSLPTDW AKGQLSGQPL CMKQYYRLFS SYRLPGHTQD 

       190        200        210        220        230        240 
TLVAQKSSIM PEPEHVIVAC CNQFFVLDVV INFRRLSEGD LFTQLRKIVK MASNEDERLP 

       250        260        270        280        290        300 
PIGLLTSDGR SEWAKARTVL LKDSTNRDSL DMIERCICLV CLDGPGTGEL SDTHRALQLL 

       310        320        330        340        350        360 
HGGGCSLNGA NRWYDKSLQF VVGRDGTCGV VCEHSPFDGI VLVQCTEHLL KHMMTSNKKL 

       370        380        390        400        410        420 
VRADSVSELP APRRLRLKCS PETQGHLASS AEKLQRIVKN LDFIVYKFDN YGKTFIKKQK 

       430        440        450        460        470        480 
YSPDGFIQVA LQLAYYRLYQ RLVPTYESAS IRRFQEGRVD NIRSATPEAL AFVQAMTDHK 

       490        500        510        520        530        540 
AAMPASEKLQ LLQTAMQAHK QYTVMAITGM AIDNHLLALR ELARDLCKEP PEMFMDETYL 

       550        560        570        580        590        600 
MSNRFVLSTS QVPTTMEMFC CYGPVVPNGN GACYNPQPEA ITFCISSFHS CKETSSVEFA 

       610        620        630        640 
EAVGASLVDM RDLCSSRQPA DSKPPAPKEK ARGPSQAKQS

P32738 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools