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P07668

- CLAT_DROME

UniProt

P07668 - CLAT_DROME

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Protein

Choline O-acetyltransferase

Gene

Cha

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei419 – 4191Proton acceptor1 Publication
Binding sitei534 – 5341Coenzyme ABy similarity
Sitei584 – 5852Cleavage
Binding sitei656 – 6561Coenzyme ABy similarity

GO - Molecular functioni

  1. choline O-acetyltransferase activity Source: UniProtKB

GO - Biological processi

  1. acetylcholine biosynthetic process Source: UniProtKB
  2. nervous system development Source: UniProtKB
  3. neuromuscular synaptic transmission Source: FlyBase
  4. synaptic transmission Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Neurotransmitter biosynthesis

Enzyme and pathway databases

ReactomeiREACT_181231. Synthesis of PC.

Names & Taxonomyi

Protein namesi
Recommended name:
Choline O-acetyltransferase (EC:2.3.1.6)
Short name:
CHOACTase
Short name:
ChAT
Short name:
Choline acetylase
Cleaved into the following 3 chains:
Gene namesi
Name:Cha
ORF Names:CG12345
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0000303. Cha.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi261 – 2611H → L or Q: No effect. 1 Publication
Mutagenesisi386 – 3861H → L: Loss of activity. 1 Publication
Mutagenesisi386 – 3861H → Q: No effect. 1 Publication
Mutagenesisi419 – 4191H → L or Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 721Choline O-acetyltransferase 67 kDa chainPRO_0000004423
Chaini? – 584Choline O-acetyltransferase 54 kDa chainPRO_0000004421
Chaini1 – 721721Choline O-acetyltransferasePRO_0000004420Add
BLAST
Chaini585 – 721137Choline O-acetyltransferase 13 kDa chainPRO_0000004422Add
BLAST

Post-translational modificationi

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

Proteomic databases

PaxDbiP07668.
PRIDEiP07668.

Expressioni

Gene expression databases

BgeeiP07668.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-20557N.
IntActiP07668. 1 interaction.
MINTiMINT-1569592.

Structurei

3D structure databases

ProteinModelPortaliP07668.
SMRiP07668. Positions 88-718.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni496 – 50813Coenzyme A bindingBy similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG70127.
GeneTreeiENSGT00760000119220.
InParanoidiP07668.
KOiK00623.
OMAiFCLARER.
OrthoDBiEOG7WHH90.
PhylomeDBiP07668.

Family and domain databases

InterProiIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERiPTHR22589. PTHR22589. 1 hit.
PfamiPF00755. Carn_acyltransf. 1 hit.
[Graphical view]
PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform A (identifier: P07668-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MASNEASTSA AGSGPESAAL FSKLRSFSIG SGPNSPQRVV SNLRGFLTHR
60 70 80 90 100
LSNITPSDTG WKDSILSIPK KWLSTAESVD EFGFPDTLPK VPVPALDETM
110 120 130 140 150
ADYIRALEPI TTPAQLERTK ELIRQFSAPQ GIGARLHQYL LDKREAEDNW
160 170 180 190 200
AYYYWLNEMY MDIRIPLPIN SNPGMVFPPR RFKTVHDVAH FAARLLDGIL
210 220 230 240 250
SHREMLDSGE LPLERAASRE KNQPLCMAQY YRLLGSCRRP GVKQDSQFLP
260 270 280 290 300
SRERLNDEDR HVVVICRNQM YCVVLQASDR GKLSESEIAS QILYVLSDAP
310 320 330 340 350
CLPAKPVPVG LLTAEPRSTW ARDREMLQED ERNQRNLELI ETAQVVLCLD
360 370 380 390 400
EPLAGNFNAR GFTGATPTVH RAGDRDETNM AHEMIHGGGS EYNSGNRWFD
410 420 430 440 450
KTMQLIICTD GTWGLCYEHS CSEGIAVVQL LEKIYKKIEE HPDEDNGLPQ
460 470 480 490 500
HHLPPPERLE WHVGPQLQLR FAQASKSVDK CIDDLDFYVY RYQSYGKTFI
510 520 530 540 550
KSCQVSPDVY IQLALQLAHY KLYGRLVATY ESASTRRFLH GRVDCIRAAS
560 570 580 590 600
TEALEWAKAM CQGEGANVPL ESDREDEEES RKVKFSIYSK DHLRELFRCA
610 620 630 640 650
VARQTEVMVK NILGNGIDIP LLGLREASIE VTGEMHELFK DESYIISQCF
660 670 680 690 700
LLSTSQVACS TDSFMGYGPV TPRGYGCSYN PHPEQIVFCV SAFYSCEDTS
710 720
ASRYAKSLQD SLDIMRDLLQ N
Length:721
Mass (Da):81,328
Last modified:December 1, 2000 - v3
Checksum:i1867F3B8421F994E
GO
Isoform B (identifier: P07668-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     583-589: Missing.

Note: No experimental confirmation available.

Show »
Length:714
Mass (Da):80,503
Checksum:iD1341DDD1AEC7C8F
GO
Isoform C (identifier: P07668-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:720
Mass (Da):81,266
Checksum:i3266AED3FA211FC1
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei60 – 8526GWKDS…EFGFP → MERLDSVDTKEMALNGRVCG RVWIP in isoform C. CuratedVSP_011397Add
BLAST
Alternative sequencei583 – 5897Missing in isoform B. 1 PublicationVSP_008316

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63724 mRNA. Translation: AAA28406.2.
AE014297 Genomic DNA. Translation: AAF55588.5.
AE014297 Genomic DNA. Translation: AAS65177.2.
AY128433 mRNA. Translation: AAM75026.1. Frameshift.
PIRiA24889.
A36526.
RefSeqiNP_477004.5. NM_057656.3. [P07668-1]
NP_996239.2. NM_206517.2. [P07668-2]
UniGeneiDm.1244.

Genome annotation databases

EnsemblMetazoaiFBtr0089367; FBpp0088397; FBgn0000303. [P07668-1]
GeneIDi42249.
KEGGidme:Dmel_CG12345.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63724 mRNA. Translation: AAA28406.2 .
AE014297 Genomic DNA. Translation: AAF55588.5 .
AE014297 Genomic DNA. Translation: AAS65177.2 .
AY128433 mRNA. Translation: AAM75026.1 . Frameshift.
PIRi A24889.
A36526.
RefSeqi NP_477004.5. NM_057656.3. [P07668-1 ]
NP_996239.2. NM_206517.2. [P07668-2 ]
UniGenei Dm.1244.

3D structure databases

ProteinModelPortali P07668.
SMRi P07668. Positions 88-718.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-20557N.
IntActi P07668. 1 interaction.
MINTi MINT-1569592.

Proteomic databases

PaxDbi P07668.
PRIDEi P07668.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0089367 ; FBpp0088397 ; FBgn0000303 . [P07668-1 ]
GeneIDi 42249.
KEGGi dme:Dmel_CG12345.

Organism-specific databases

CTDi 42249.
FlyBasei FBgn0000303. Cha.

Phylogenomic databases

eggNOGi NOG70127.
GeneTreei ENSGT00760000119220.
InParanoidi P07668.
KOi K00623.
OMAi FCLARER.
OrthoDBi EOG7WHH90.
PhylomeDBi P07668.

Enzyme and pathway databases

Reactomei REACT_181231. Synthesis of PC.

Miscellaneous databases

GenomeRNAii 42249.
NextBioi 827879.
PROi P07668.

Gene expression databases

Bgeei P07668.

Family and domain databases

InterProi IPR000542. Carn_acyl_trans.
[Graphical view ]
PANTHERi PTHR22589. PTHR22589. 1 hit.
Pfami PF00755. Carn_acyltransf. 1 hit.
[Graphical view ]
PROSITEi PS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  7. 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.

Entry informationi

Entry nameiCLAT_DROME
AccessioniPrimary (citable) accession number: P07668
Secondary accession number(s): Q8MQR2, Q9TXC6, Q9VE41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 1, 2000
Last modified: October 29, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3