Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07668 (CLAT_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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:Cha
ORF Names:CG12345
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length721 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. Ref.9

Catalytic activity

Acetyl-CoA + choline = CoA + O-acetylcholine.

Subunit structure

The 54 kDa and 13 kDa chains exist as a heterodimer.

Post-translational modification

The N-terminus of choline O-acetyltransferase 67 kDa and 54 kDa chains are blocked.

Sequence similarities

Belongs to the carnitine/choline acetyltransferase family.

Sequence caution

The sequence AAM75026.1 differs from that shown. Reason: Frameshift at position 310.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P07668-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P07668-2)

The sequence of this isoform differs from the canonical sequence as follows:
     583-589: Missing.
Note: No experimental confirmation available.
Isoform C (identifier: P07668-3)

The sequence of this isoform differs from the canonical sequence as follows:
     60-85: GWKDSILSIPKKWLSTAESVDEFGFP → MERLDSVDTKEMALNGRVCGRVWIP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Choline O-acetyltransferase
PRO_0000004420
Chain? – 584Choline O-acetyltransferase 54 kDa chainPRO_0000004421
Chain585 – 721137Choline O-acetyltransferase 13 kDa chain
PRO_0000004422
Chain? – 721Choline O-acetyltransferase 67 kDa chainPRO_0000004423

Regions

Region496 – 50813Coenzyme A binding By similarity

Sites

Active site4191Proton acceptor Ref.11
Binding site5341Coenzyme A By similarity
Binding site6561Coenzyme A By similarity
Site584 – 5852Cleavage

Natural variations

Alternative sequence60 – 8526GWKDS…EFGFP → MERLDSVDTKEMALNGRVCG RVWIP in isoform C.
VSP_011397
Alternative sequence583 – 5897Missing in isoform B.
VSP_008316

Experimental info

Mutagenesis2611H → L or Q: No effect. Ref.11
Mutagenesis3861H → L: Loss of activity. Ref.11
Mutagenesis3861H → Q: No effect. Ref.11
Mutagenesis4191H → L or Q: Loss of activity. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified December 1, 2000. Version 3.
Checksum: 1867F3B8421F994E

FASTA72181,328
        10         20         30         40         50         60 
MASNEASTSA AGSGPESAAL FSKLRSFSIG SGPNSPQRVV SNLRGFLTHR LSNITPSDTG 

        70         80         90        100        110        120 
WKDSILSIPK KWLSTAESVD EFGFPDTLPK VPVPALDETM ADYIRALEPI TTPAQLERTK 

       130        140        150        160        170        180 
ELIRQFSAPQ GIGARLHQYL LDKREAEDNW AYYYWLNEMY MDIRIPLPIN SNPGMVFPPR 

       190        200        210        220        230        240 
RFKTVHDVAH FAARLLDGIL SHREMLDSGE LPLERAASRE KNQPLCMAQY YRLLGSCRRP 

       250        260        270        280        290        300 
GVKQDSQFLP SRERLNDEDR HVVVICRNQM YCVVLQASDR GKLSESEIAS QILYVLSDAP 

       310        320        330        340        350        360 
CLPAKPVPVG LLTAEPRSTW ARDREMLQED ERNQRNLELI ETAQVVLCLD EPLAGNFNAR 

       370        380        390        400        410        420 
GFTGATPTVH RAGDRDETNM AHEMIHGGGS EYNSGNRWFD KTMQLIICTD GTWGLCYEHS 

       430        440        450        460        470        480 
CSEGIAVVQL LEKIYKKIEE HPDEDNGLPQ HHLPPPERLE WHVGPQLQLR FAQASKSVDK 

       490        500        510        520        530        540 
CIDDLDFYVY RYQSYGKTFI KSCQVSPDVY IQLALQLAHY KLYGRLVATY ESASTRRFLH 

       550        560        570        580        590        600 
GRVDCIRAAS TEALEWAKAM CQGEGANVPL ESDREDEEES RKVKFSIYSK DHLRELFRCA 

       610        620        630        640        650        660 
VARQTEVMVK NILGNGIDIP LLGLREASIE VTGEMHELFK DESYIISQCF LLSTSQVACS 

       670        680        690        700        710        720 
TDSFMGYGPV TPRGYGCSYN PHPEQIVFCV SAFYSCEDTS ASRYAKSLQD SLDIMRDLLQ 


N 

« Hide

Isoform B [UniParc].

Checksum: D1341DDD1AEC7C8F
Show »

FASTA71480,503
Isoform C [UniParc].

Checksum: 3266AED3FA211FC1
Show »

FASTA72081,266

References

« Hide 'large scale' references
[1]"Cloning of Drosophila choline acetyltransferase cDNA."
Itoh N., Slemmon J.R., Hawke D.H., Williamson R., Morita E., Itakura K., Roberts E., Shively J.E., Crawford G.D., Salvaterra P.M.
Proc. Natl. Acad. Sci. U.S.A. 83:4081-4085(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Head.
[2]"Drosophila choline acetyltransferase uses a non-AUG initiation codon and full length RNA is inefficiently translated."
Sugihara H., Andrisani V., Salvaterra P.M.
J. Biol. Chem. 265:21714-21719(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), SEQUENCE REVISION, INITIATION CODON GTG.
[3]Salvaterra P.M.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Genomic organization of Drosophila choline acetyltransferase."
Sugihara H., Andrisani V., Salvaterra P.M.
J. Neurochem. 57:1636-1642(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM C).
[5]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[6]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[7]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Strain: Berkeley.
Tissue: Head.
[8]"Sequence analysis of a proteolyzed site in Drosophila choline acetyltransferase."
Slemmon J.R.
J. Neurochem. 52:1898-1904(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 585-594, CLEAVAGE.
[9]"The amino terminus of the putative Drosophila choline acetyltransferase precursor is cleaved to yield the 67 kDa enzyme."
Slemmon J.R., Campbell G.A., Selski D.J., Bramson H.N.
Brain Res. Mol. Brain Res. 9:245-252(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CLEAVAGE.
[10]"Molecular characterization of choline acetyltransferase from Drosophila melanogaster."
Slemmon J.R., Salvaterra P.M., Roberts E.
Neurochem. Int. 6:519-525(1984)
Cited for: INTERACTION BETWEEN 54 KDA AND 13 KDA CHAINS.
[11]"Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis."
Carbini L.A., Hersh L.B.
J. Neurochem. 61:247-253(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-261; HIS-386 AND HIS-419, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63724 mRNA. Translation: AAA28406.2.
AE014297 Genomic DNA. Translation: AAF55588.5.
AE014297 Genomic DNA. Translation: AAS65177.2.
AY128433 mRNA. Translation: AAM75026.1. Frameshift.
PIRA24889.
A36526.
RefSeqNP_477004.5. NM_057656.2. [P07668-1]
NP_996239.2. NM_206517.1. [P07668-2]
UniGeneDm.1244.

3D structure databases

ProteinModelPortalP07668.
SMRP07668. Positions 88-718.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-20557N.
IntActP07668. 1 interaction.
MINTMINT-1569592.

Proteomic databases

PaxDbP07668.
PRIDEP07668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089367; FBpp0088397; FBgn0000303. [P07668-1]
GeneID42249.
KEGGdme:Dmel_CG12345.

Organism-specific databases

CTD42249.
FlyBaseFBgn0000303. Cha.

Phylogenomic databases

eggNOGNOG70127.
GeneTreeENSGT00740000115446.
InParanoidP07668.
KOK00623.
OMAFCLARER.
OrthoDBEOG7WHH90.
PhylomeDBP07668.

Gene expression databases

BgeeP07668.

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

GenomeRNAi42249.
NextBio827879.
PROP07668.

Entry information

Entry nameCLAT_DROME
AccessionPrimary (citable) accession number: P07668
Secondary accession number(s): Q8MQR2, Q9TXC6, Q9VE41
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase