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Choline O-acetyltransferase (CHOACTase) (ChAT) (Choline acetylase) (EC 2.3.1.6) [Cleaved into: Choline O-acetyltransferase 67 kDa chain; Choline O-acetyltransferase 54 kDa chain; Choline O-acetyltransferase 13 kDa chain]

 CLAT_DROME              Reviewed;         721 AA.
P07668; Q8MQR2; Q9TXC6; Q9VE41;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 3.
27-SEP-2017, entry version 151.
RecName: Full=Choline O-acetyltransferase;
Short=CHOACTase;
Short=ChAT;
Short=Choline acetylase;
EC=2.3.1.6;
Contains:
RecName: Full=Choline O-acetyltransferase 67 kDa chain;
Contains:
RecName: Full=Choline O-acetyltransferase 54 kDa chain;
Contains:
RecName: Full=Choline O-acetyltransferase 13 kDa chain;
Name=Cha; ORFNames=CG12345;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Head;
PubMed=3086876; DOI=10.1073/pnas.83.11.4081;
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.;
"Cloning of Drosophila choline acetyltransferase cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 83:4081-4085(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), SEQUENCE REVISION, AND
INITIATION CODON GTG.
PubMed=2123874;
Sugihara H., Andrisani V., Salvaterra P.M.;
"Drosophila choline acetyltransferase uses a non-AUG initiation codon
and full length RNA is inefficiently translated.";
J. Biol. Chem. 265:21714-21719(1990).
[3]
SEQUENCE REVISION.
Salvaterra P.M.;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM C).
PubMed=1717651; DOI=10.1111/j.1471-4159.1991.tb06362.x;
Sugihara H., Andrisani V., Salvaterra P.M.;
"Genomic organization of Drosophila choline acetyltransferase.";
J. Neurochem. 57:1636-1642(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[6]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[8]
PROTEIN SEQUENCE OF 585-594, AND CLEAVAGE.
PubMed=2723644; DOI=10.1111/j.1471-4159.1989.tb07274.x;
Slemmon J.R.;
"Sequence analysis of a proteolyzed site in Drosophila choline
acetyltransferase.";
J. Neurochem. 52:1898-1904(1989).
[9]
FUNCTION, AND CLEAVAGE.
PubMed=1851526; DOI=10.1016/0169-328X(91)90008-L;
Slemmon J.R., Campbell G.A., Selski D.J., Bramson H.N.;
"The amino terminus of the putative Drosophila choline
acetyltransferase precursor is cleaved to yield the 67 kDa enzyme.";
Brain Res. Mol. Brain Res. 9:245-252(1991).
[10]
INTERACTION BETWEEN 54 KDA AND 13 KDA CHAINS.
Slemmon J.R., Salvaterra P.M., Roberts E.;
"Molecular characterization of choline acetyltransferase from
Drosophila melanogaster.";
Neurochem. Int. 6:519-525(1984).
[11]
MUTAGENESIS OF HIS-261; HIS-386 AND HIS-419, AND ACTIVE SITE.
PubMed=8515270; DOI=10.1111/j.1471-4159.1993.tb03561.x;
Carbini L.A., Hersh L.B.;
"Functional analysis of conserved histidines in choline
acetyltransferase by site-directed mutagenesis.";
J. Neurochem. 61:247-253(1993).
-!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine
(ACh) from acetyl CoA and choline at cholinergic synapses.
{ECO:0000269|PubMed:1851526}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + choline = CoA + O-acetylcholine.
-!- SUBUNIT: The 54 kDa and 13 kDa chains exist as a heterodimer.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=A;
IsoId=P07668-1; Sequence=Displayed;
Name=B;
IsoId=P07668-2; Sequence=VSP_008316;
Note=No experimental confirmation available.;
Name=C;
IsoId=P07668-3; Sequence=VSP_011397;
-!- PTM: The N-terminus of choline O-acetyltransferase 67 kDa and 54
kDa chains are blocked.
-!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM75026.1; Type=Frameshift; Positions=310; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M63724; AAA28406.2; -; mRNA.
EMBL; AE014297; AAF55588.5; -; Genomic_DNA.
EMBL; AE014297; AAS65177.2; -; Genomic_DNA.
EMBL; AY128433; AAM75026.1; ALT_FRAME; mRNA.
PIR; A24889; A24889.
PIR; A36526; A36526.
RefSeq; NP_477004.5; NM_057656.3. [P07668-1]
RefSeq; NP_996239.2; NM_206517.2. [P07668-2]
UniGene; Dm.1244; -.
ProteinModelPortal; P07668; -.
SMR; P07668; -.
BioGrid; 67255; 1.
DIP; DIP-20557N; -.
IntAct; P07668; 3.
MINT; MINT-1569592; -.
STRING; 7227.FBpp0088397; -.
PaxDb; P07668; -.
PRIDE; P07668; -.
GeneID; 42249; -.
KEGG; dme:Dmel_CG12345; -.
CTD; 1103; -.
FlyBase; FBgn0000303; Cha.
eggNOG; KOG3717; Eukaryota.
eggNOG; ENOG410XNZ9; LUCA.
InParanoid; P07668; -.
KO; K00623; -.
OrthoDB; EOG091G038F; -.
PhylomeDB; P07668; -.
Reactome; R-DME-1483191; Synthesis of PC.
Reactome; R-DME-264642; Acetylcholine Neurotransmitter Release Cycle.
GenomeRNAi; 42249; -.
PRO; PR:P07668; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0000303; -.
Genevisible; P07668; DM.
GO; GO:0005829; C:cytosol; NAS:UniProtKB.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0004102; F:choline O-acetyltransferase activity; IDA:UniProtKB.
GO; GO:0008292; P:acetylcholine biosynthetic process; IMP:FlyBase.
GO; GO:0007268; P:chemical synaptic transmission; TAS:UniProtKB.
GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
InterPro; IPR000542; Carn_acyl_trans.
PANTHER; PTHR22589; PTHR22589; 1.
Pfam; PF00755; Carn_acyltransf; 1.
PROSITE; PS00439; ACYLTRANSF_C_1; 1.
PROSITE; PS00440; ACYLTRANSF_C_2; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome;
Direct protein sequencing; Neurotransmitter biosynthesis;
Reference proteome; Transferase.
CHAIN 1 721 Choline O-acetyltransferase.
/FTId=PRO_0000004420.
CHAIN ? 584 Choline O-acetyltransferase 54 kDa chain.
/FTId=PRO_0000004421.
CHAIN 585 721 Choline O-acetyltransferase 13 kDa chain.
/FTId=PRO_0000004422.
CHAIN ? 721 Choline O-acetyltransferase 67 kDa chain.
/FTId=PRO_0000004423.
REGION 496 508 Coenzyme A binding. {ECO:0000250}.
ACT_SITE 419 419 Proton acceptor.
{ECO:0000269|PubMed:8515270}.
BINDING 534 534 Coenzyme A. {ECO:0000250}.
BINDING 656 656 Coenzyme A. {ECO:0000250}.
SITE 584 585 Cleavage.
VAR_SEQ 60 85 GWKDSILSIPKKWLSTAESVDEFGFP -> MERLDSVDTKE
MALNGRVCGRVWIP (in isoform C).
{ECO:0000305}.
/FTId=VSP_011397.
VAR_SEQ 583 589 Missing (in isoform B).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_008316.
MUTAGEN 261 261 H->L,Q: No effect.
{ECO:0000269|PubMed:8515270}.
MUTAGEN 386 386 H->L: Loss of activity.
{ECO:0000269|PubMed:8515270}.
MUTAGEN 386 386 H->Q: No effect.
{ECO:0000269|PubMed:8515270}.
MUTAGEN 419 419 H->L,Q: Loss of activity.
{ECO:0000269|PubMed:8515270}.
SEQUENCE 721 AA; 81328 MW; 1867F3B8421F994E CRC64;
MASNEASTSA AGSGPESAAL FSKLRSFSIG SGPNSPQRVV SNLRGFLTHR LSNITPSDTG
WKDSILSIPK KWLSTAESVD EFGFPDTLPK VPVPALDETM ADYIRALEPI TTPAQLERTK
ELIRQFSAPQ GIGARLHQYL LDKREAEDNW AYYYWLNEMY MDIRIPLPIN SNPGMVFPPR
RFKTVHDVAH FAARLLDGIL SHREMLDSGE LPLERAASRE KNQPLCMAQY YRLLGSCRRP
GVKQDSQFLP SRERLNDEDR HVVVICRNQM YCVVLQASDR GKLSESEIAS QILYVLSDAP
CLPAKPVPVG LLTAEPRSTW ARDREMLQED ERNQRNLELI ETAQVVLCLD EPLAGNFNAR
GFTGATPTVH RAGDRDETNM AHEMIHGGGS EYNSGNRWFD KTMQLIICTD GTWGLCYEHS
CSEGIAVVQL LEKIYKKIEE HPDEDNGLPQ HHLPPPERLE WHVGPQLQLR FAQASKSVDK
CIDDLDFYVY RYQSYGKTFI KSCQVSPDVY IQLALQLAHY KLYGRLVATY ESASTRRFLH
GRVDCIRAAS TEALEWAKAM CQGEGANVPL ESDREDEEES RKVKFSIYSK DHLRELFRCA
VARQTEVMVK NILGNGIDIP LLGLREASIE VTGEMHELFK DESYIISQCF LLSTSQVACS
TDSFMGYGPV TPRGYGCSYN PHPEQIVFCV SAFYSCEDTS ASRYAKSLQD SLDIMRDLLQ
N


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