Reviewed, UniProtKB/Swiss-Prot P13222 (CLAT_PIG)

Names and origin

Protein names

Recommended name:
    Choline O-acetyltransferase
      Short name(s)=CHOACTase, Choline acetylase, ChAT
    EC=2.3.1.6

Gene names

Name:

CHAT

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	641 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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.
Sequence similarities	Belongs to the carnitine/choline acetyltransferase family.

Ontologies

Keywords
Biological process	Neurotransmitter biosynthesis
Molecular function	Acyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	choline O-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 641	640	Choline O-acetyltransferase
Regions
	Region	413 – 425	13	Coenzyme A binding By similarity
Sites
	Active site	335	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13222-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 90CFA6931F8CD393	FASTA	641	71,731
	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

References

[1]	"cDNA cloning and complete sequence of porcine choline acetyltransferase: in vitro translation of the corresponding RNA yields an active protein." Berrard S., Brice A., Lottspeich F., Braun A., Barde Y.-A., Mallet J. Proc. Natl. Acad. Sci. U.S.A. 84:9280-9284(1987) [PubMed: 3480542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ventral spinal cord.
[2]	"Molecular genetic approach to the study of mammalian choline acetyltransferase." Berrard S., Brice A., Mallet J. Brain Res. Bull. 22:147-153(1989) [PubMed: 2713713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ventral spinal cord.
[3]	"Comparison of the promoter region of the human and porcine choline acetyltransferase genes: localization of an important enhancer region." Hersh L.B., Kong C.F., Sampson C., Mues G., Li Y.P., Fisher A., Hilt D., Baetge E.E. J. Neurochem. 61:306-314(1993) [PubMed: 8515278] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-23.
[4]	"N-terminal sequence of pig brain choline acetyltransferase purified by a rapid procedure." Braun A., Barde Y.-A., Lottspeich F., Mewes H.-W., Thoenen H. J. Neurochem. 48:16-21(1987) [PubMed: 3794697] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-12. Tissue: Brain.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03021 mRNA. Translation: AAA31000.1. M27736 mRNA. Translation: AAA31015.1.
PIR	A39961.
RefSeq	NP_001001541.1.
UniGene	Ssc.16316
3D structure databases
HSSP	HSSP built from PDB template 1NM8 based on UniProtKB P43155.
SMR	P13222. Positions 20-617.
ModBase	Search...
Genome annotation databases
GeneID	396896.
KEGG	ssc:396896.
Phylogenomic databases
HOVERGEN	P13222.
Family and domain databases
InterPro	IPR000542. Carn_acyl_trans. [Graphical view]
PANTHER	PTHR22589. Carn_acyl_trans. 1 hit.
Pfam	PF00755. Carn_acyltransf. 1 hit. [Graphical view]
PROSITE	PS00439. ACYLTRANSF_C_1. 1 hit. PS00440. ACYLTRANSF_C_2. 1 hit. [Graphical view]
ProDom	P13222. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

CLAT_PIG

Accession

Primary (citable) accession number: P13222

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	July 22, 2008
This is version 56 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)