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P07668

- CLAT_DROME

UniProt

P07668 - CLAT_DROME

Protein

Choline O-acetyltransferase

Gene

Cha

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (01 Dec 2000)
      Previous versions | rss
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    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

    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

    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.
    GeneTreeiENSGT00740000115446.
    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

    MASNEASTSA AGSGPESAAL FSKLRSFSIG SGPNSPQRVV SNLRGFLTHR    50
    LSNITPSDTG WKDSILSIPK KWLSTAESVD EFGFPDTLPK VPVPALDETM 100
    ADYIRALEPI TTPAQLERTK ELIRQFSAPQ GIGARLHQYL LDKREAEDNW 150
    AYYYWLNEMY MDIRIPLPIN SNPGMVFPPR RFKTVHDVAH FAARLLDGIL 200
    SHREMLDSGE LPLERAASRE KNQPLCMAQY YRLLGSCRRP GVKQDSQFLP 250
    SRERLNDEDR HVVVICRNQM YCVVLQASDR GKLSESEIAS QILYVLSDAP 300
    CLPAKPVPVG LLTAEPRSTW ARDREMLQED ERNQRNLELI ETAQVVLCLD 350
    EPLAGNFNAR GFTGATPTVH RAGDRDETNM AHEMIHGGGS EYNSGNRWFD 400
    KTMQLIICTD GTWGLCYEHS CSEGIAVVQL LEKIYKKIEE HPDEDNGLPQ 450
    HHLPPPERLE WHVGPQLQLR FAQASKSVDK CIDDLDFYVY RYQSYGKTFI 500
    KSCQVSPDVY IQLALQLAHY KLYGRLVATY ESASTRRFLH GRVDCIRAAS 550
    TEALEWAKAM CQGEGANVPL ESDREDEEES RKVKFSIYSK DHLRELFRCA 600
    VARQTEVMVK NILGNGIDIP LLGLREASIE VTGEMHELFK DESYIISQCF 650
    LLSTSQVACS TDSFMGYGPV TPRGYGCSYN PHPEQIVFCV SAFYSCEDTS 700
    ASRYAKSLQD SLDIMRDLLQ N 721
    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_057656.2. [P07668-1]
    NP_996239.2. NM_206517.1. [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_057656.2. [P07668-1 ]
    NP_996239.2. NM_206517.1. [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 ENSGT00740000115446.
    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

    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 1, 2014
    This is version 132 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