ID   CLAT_CAEEL              Reviewed;         627 AA.
AC   P32756;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Choline O-acetyltransferase;
DE            Short=CHOACTase;
DE            Short=ChAT;
DE            Short=Choline acetylase;
DE            EC=2.3.1.6 {ECO:0000250|UniProtKB:P28329};
GN   Name=cha-1 {ECO:0000312|WormBase:ZC416.8b};
GN   ORFNames=ZC416.8 {ECO:0000312|WormBase:ZC416.8b};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=8158270; DOI=10.1523/jneurosci.14-04-02290.1994;
RA   Alfonso A., Grundahl K., McManus J.R., Rand J.B.;
RT   "Cloning and characterization of the choline acetyltransferase structural
RT   gene (cha-1) from C. elegans.";
RL   J. Neurosci. 14:2290-2300(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=28244369; DOI=10.7554/elife.24846;
RA   Schwarz J., Bringmann H.;
RT   "Analysis of the NK2 homeobox gene ceh-24 reveals sublateral motor neuron
RT   control of left-right turning during sleep.";
RL   Elife 6:0-0(2017).
CC   -!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh)
CC       from acetyl CoA and choline at cholinergic synapses (By similarity).
CC       Required in SIA sublateral cholinergic motor neurons for a left-right
CC       turning behavior that occurs during the lethargus phase of the normal
CC       sleep process called 'flipping' (PubMed:28244369). During 'flipping'
CC       animals rotate 180 degrees about their longitudinal axis
CC       (PubMed:28244369). {ECO:0000250|UniProtKB:P28329,
CC       ECO:0000269|PubMed:28244369}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + choline = acetylcholine + CoA;
CC         Xref=Rhea:RHEA:18821, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.6;
CC         Evidence={ECO:0000250|UniProtKB:P28329};
CC   -!- TISSUE SPECIFICITY: Expressed in SIA, SIB and SMB sublateral motor
CC       neurons. {ECO:0000269|PubMed:28244369}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in SIA sublateral motor
CC       neurons results in abnormal sleep behavior whereby larvae display a
CC       defect in 'flipping,' which is a left-right turning behavior that
CC       occurs during sleep. {ECO:0000269|PubMed:28244369}.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; L08969; AAA53659.1; -; mRNA.
DR   EMBL; L08970; AAA53660.1; -; Genomic_DNA.
DR   EMBL; FO080977; CCD68242.1; -; Genomic_DNA.
DR   PIR; T37293; T37293.
DR   RefSeq; NP_001023603.1; NM_001028432.2.
DR   AlphaFoldDB; P32756; -.
DR   SMR; P32756; -.
DR   STRING; 6239.ZC416.8b.1; -.
DR   EPD; P32756; -.
DR   PaxDb; 6239-ZC416-8b; -.
DR   PeptideAtlas; P32756; -.
DR   EnsemblMetazoa; ZC416.8b.1; ZC416.8b.1; WBGene00000481.
DR   GeneID; 24105307; -.
DR   KEGG; cel:CELE_CHA-1; -.
DR   AGR; WB:WBGene00000481; -.
DR   WormBase; ZC416.8b; CE17308; WBGene00000481; cha-1.
DR   eggNOG; KOG3717; Eukaryota.
DR   GeneTree; ENSGT01060000248556; -.
DR   HOGENOM; CLU_013513_3_1_1; -.
DR   InParanoid; P32756; -.
DR   OMA; MAMSSYE; -.
DR   OrthoDB; 1429709at2759; -.
DR   PhylomeDB; P32756; -.
DR   Reactome; R-CEL-1483191; Synthesis of PC.
DR   Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
DR   PRO; PR:P32756; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00000481; Expressed in larva and 3 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:WormBase.
DR   GO; GO:0060076; C:excitatory synapse; IDA:WormBase.
DR   GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR   GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR   GO; GO:0031090; C:organelle membrane; IDA:WormBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR   GO; GO:0045202; C:synapse; IDA:WormBase.
DR   GO; GO:0004102; F:choline O-acetyltransferase activity; IDA:WormBase.
DR   GO; GO:0008292; P:acetylcholine biosynthetic process; IDA:WormBase.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589:SF14; CHOLINE O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Neurotransmitter biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..627
FT                   /note="Choline O-acetyltransferase"
FT                   /id="PRO_0000210153"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         418..430
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         456
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         559
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   627 AA;  71317 MW;  59F52175E6F16494 CRC64;
     MEKEKVDELP PNDNWYETAL PKPPVPSLEA TLDRYLEYAA VVAVGQKASL ATTHDAAHKF
     VRQATPLQEQ LLEIAEKSPN WATKFWLPEM YMRVRMPTPV NSNPGYIFPK VKFETKEDHI
     KYTALLTRGL LEYKNLIDTK QVCREKSTGA QKLQMCMEQY DRVLSCYREP GVGEDTQIRK
     QKTNDGNEHV LVMCRNQTFL LHSRINGALV SYADVEYQLA QIEEISKINQ NNTANIGASG
     VGPRDNAALF WQDMLTVEQN SKSYEWVKSA LFVVCLDMED PIDYGKNDTM SISEKEKEFV
     ARGYSTLTGH GSSKFGLNRW YDATIQLVVS SSGVNGLCIE HSTAEGIVII NMAETAIRYA
     QKYFKSKMVW NDVRNVHPKS LTWHFSENSR NILKKQAEVF DELANELELE VLIFNEFGKD
     SIKNWRVSPD GFIQLIMQLA HYKTHGHLVS TYESASVRRF GAGRVDNIRA NTQEALEWVT
     AMASKKESKE RKLELFKKAV LKQVKVTLEN ISGYGVDNHL CALFCLARER EETTGEDIPS
     LFLDPLWSEV MRFPLSTSQV TTSLDIPDCY LTYGAVVRDG YGCPYNIQPD RVIFAPTAFR
     SDPRTDLQHF KKSLAGAMRD VKELLSN
//