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P13222 (CLAT_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Choline O-acetyltransferase

Short name=CHOACTase
Short name=ChAT
Short name=Choline acetylase
EC=2.3.1.6
Gene names
Name:CHAT
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 641640Choline O-acetyltransferase
PRO_0000210156

Regions

Region413 – 42513Coenzyme A binding By similarity

Sites

Active site3351Proton acceptor By similarity
Binding site4511Coenzyme A By similarity
Binding site5521Coenzyme A By similarity

Sequences

Sequence LengthMass (Da)Tools
P13222 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 90CFA6931F8CD393

FASTA64171,731
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03021 mRNA. Translation: AAA31000.1.
M27736 mRNA. Translation: AAA31015.1.
PIRA39961.
RefSeqNP_001001541.1. NM_001001541.1.
UniGeneSsc.16316.

3D structure databases

ProteinModelPortalP13222.
SMRP13222. Positions 23-617.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000011081.

Proteomic databases

PRIDEP13222.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000011376; ENSSSCP00000011081; ENSSSCG00000010392.
GeneID396896.
KEGGssc:396896.

Organism-specific databases

CTD1103.

Phylogenomic databases

eggNOGNOG70127.
GeneTreeENSGT00740000115446.
HOGENOMHOG000233845.
HOVERGENHBG107717.
KOK00623.
OMAHVIVACC.
OrthoDBEOG7WHH90.
TreeFamTF313836.

Family and domain databases

InterProIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERPTHR22589. PTHR22589. 1 hit.
PfamPF00755. Carn_acyltransf. 1 hit.
[Graphical view]
PROSITEPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLAT_PIG
AccessionPrimary (citable) accession number: P13222
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families