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P32738 (CLAT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length640 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.

Subunit structure

Monomer. Ref.4

Sequence similarities

Belongs to the carnitine/choline acetyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 640639Choline O-acetyltransferase
PRO_0000210157

Regions

Region412 – 42413Coenzyme A binding Probable

Sites

Active site3341Proton acceptor By similarity
Binding site4501Coenzyme A By similarity
Binding site5511Coenzyme A By similarity

Experimental info

Mutagenesis4531R → A, E or Q: Increases KM for coenzyme A and acetylcholine. Ref.3

Secondary structure

1 ............................................................................................... 640
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32738 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E5FEA20EBBFA2EC6

FASTA64071,864
        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

« Hide

References

[1]"Complementary DNAs for choline acetyltransferase from spinal cords of rat and mouse: nucleotide sequences, expression in mammalian cells, and in situ hybridization."
Ishii K., Oda Y., Ichikawa T., Deguchi T.
Brain Res. Mol. Brain Res. 7:151-159(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Spinal cord.
[2]"Multiple mRNA species of choline acetyltransferase from rat spinal cord."
Kengaku M., Misawa H., Deguchi T.
Brain Res. Mol. Brain Res. 18:71-76(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
Tissue: Spinal cord.
[3]"Identification of an active site arginine in rat choline acetyltransferase by alanine scanning mutagenesis."
Wu D., Hersh L.B.
J. Biol. Chem. 270:29111-29116(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-453.
[4]"Structural insights and functional implications of choline acetyltransferase."
Govindasamy L., Pedersen B., Lian W., Kukar T., Gu Y., Jin S., Agbandje-McKenna M., Wu D., McKenna R.
J. Struct. Biol. 148:226-235(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), SUBUNIT.
[5]"Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders."
Cai Y., Cronin C.N., Engel A.G., Ohno K., Hersh L.B., Rodgers D.W.
EMBO J. 23:2047-2058(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-634 IN COMPLEX WITH COENZYME A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M88488 Genomic DNA. No translation available.
IPIIPI00190700.
PIRA48319.
UniGeneRn.45116.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q6XX-ray2.50A/B1-634[»]
1T1UX-ray1.55A2-640[»]
ProteinModelPortalP32738.
SMRP32738. Positions 20-616.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000063149.

Proteomic databases

PaxDbP32738.
PRIDEP32738.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:1304627. rat.

Organism-specific databases

RGD1304627. Chat.

Phylogenomic databases

eggNOGNOG70127.
HOGENOMHOG000233845.
HOVERGENHBG107717.
InParanoidP32738.

Gene expression databases

GenevestigatorP32738.
GermOnlineENSRNOG00000025012. Rattus norvegicus.

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...

Other

BindingDBP32738.
ChEMBLCHEMBL3945.
EvolutionaryTraceP32738.

Entry information

Entry nameCLAT_RAT
AccessionPrimary (citable) accession number: P32738
Secondary accession number(s): Q63849, Q64342
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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