[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Ventral spinal cord; PubMed=3480542 [NCBI, ExPASy, EBI, Israel, Japan] Berrard S., Brice A., Lottspeich F., Braun A., Barde Y.-A., Mallet J.; "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. 84:9280-9284(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Ventral spinal cord; DOI=10.1016/0361-9230(89)90139-1; PubMed=2713713 [NCBI, ExPASy, EBI, Israel, Japan] Berrard S., Brice A., Mallet J.; "Molecular genetic approach to the study of mammalian choline acetyltransferase."; Brain Res. Bull. 22:147-153(1989).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-23. PubMed=8515278 [NCBI, ExPASy, EBI, Israel, Japan] Hersh L.B., Kong C.F., Sampson C., Mues G., Li Y.P., Fisher A., Hilt D., Baetge E.E.; "Comparison of the promoter region of the human and porcine choline acetyltransferase genes: localization of an important enhancer region."; J. Neurochem. 61:306-314(1993).
[4]	PROTEIN SEQUENCE OF 2-12. TISSUE=Brain; PubMed=3794697 [NCBI, ExPASy, EBI, Israel, Japan] Braun A., Barde Y.-A., Lottspeich F., Mewes H.-W., Thoenen H.; "N-terminal sequence of pig brain choline acetyltransferase purified by a rapid procedure."; J. Neurochem. 48:16-21(1987).

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.
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

J03021; AAA31000.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M27736; AAA31015.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A39961; A39961.

NP_001001541.1; -.

3D structure databases

HSSP

P43155; 1NM8. [HSSP ENTRY / PDB]

SMR

P13222; 20-617.

ModBase

P13222.

Ontologies

GO:0004102;	Molecular function: choline O-acetyltransferase activity (inferred from electronic annotation from EC).
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.

BLOCKS

P13222.

Genome annotation databases

GeneID

396896; -.

KEGG

ssc:396896; -.

Phylogenomic databases

HOVERGEN

P13222; -.

Other

ProtoNet

P13222.

UniRef

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

Keywords

Acyltransferase; Direct protein sequencing; Neurotransmitter biosynthesis; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 641`	`640`	`Choline O-acetyltransferase.`	`PRO_0000210156`
`REGION`	`413 425`	`13`	`Coenzyme A binding (By similarity).`
`ACT_SITE`	`335 335`		`Proton acceptor (By similarity).`

Sequence information

Length: 641 AA [This is the length of the unprocessed precursor]

Molecular weight: 71731 Da [This is the MW of the unprocessed precursor]

CRC64: 90CFA6931F8CD393 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPILEKTPPK MAAKSPSSEE EPGLPKLPVP PLQQTLATYL RCMQHLVPEE QFRRSQAIVQ 

        70         80         90        100        110        120 
QFGAPGGLGE TLQQKLLERQ EQTANWVSEY WLNDMYLNNR LALPVNSSPA VIFARQHFQD 

       130        140        150        160        170        180 
TNDQLRFAAN LISGVLSYKA LLDSHSIPID CAKGQLSGQP LCMKQYYGLF SSYRLPGHTQ 

       190        200        210        220        230        240 
DTLVAQKSSV MPEPEHVIVA CCNQFFVLDV VINFRRLSEG DLFTQLRKIV RMASNEDERL 

       250        260        270        280        290        300 
PPIGLLTSDG RSEWAEARTV LVKDSTNRDS LDMIERCICL VCLDAPGGME LSDTNRALQL 

       310        320        330        340        350        360 
LHGGGCSKNG ANRWYDKSLQ FVVGRDGTCG VVCEHSPFDG IVLVQCTEHL LKHMVKSSKK 

       370        380        390        400        410        420 
MVRADSVSEL PAPRRLRWKC SPEIQGLLAS SAEKLQQIVK NLDFTVYKFD DYGKTFIKQQ 

       430        440        450        460        470        480 
KCSPDAFIQV ALQLAFYRLH GRLVPTYESA SIRRFHEGRV DNIRSATPEA LHFVKAITDH 

       490        500        510        520        530        540 
ASAMPDSEKL LLLKDAIRAQ TQYTVMAITG MAIDNHLLGL RELAREVCKE LPEMFTDETY 

       550        560        570        580        590        600 
LMSNRFVLST SQVPTTMEMF CCYGPVVPNG YGACYNPQPE SILFCISSFH GCKETSSTKF 

       610        620        630        640 
AKAVEESFIE MKGLCSLSQS GMGKPLATKE KVTRPSQVHQ P

P13222 in FASTA format

View entry in original UniProtKB/Swiss-Prot 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