CLAT_HUMAN
ID CLAT_HUMAN Reviewed; 748 AA.
AC P28329; A2BDF4; A2BDF5; Q16488; Q9BQ23; Q9BQ35; Q9BQE1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Choline O-acetyltransferase;
DE Short=CHOACTase;
DE Short=ChAT;
DE Short=Choline acetylase;
DE EC=2.3.1.6 {ECO:0000269|PubMed:17144655};
GN Name=CHAT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M), AND VARIANTS GLY-392 AND MET-461.
RC TISSUE=Spinal cord;
RX PubMed=1337937; DOI=10.1016/0169-328x(92)90237-6;
RA Oda Y., Nakanishi I., Deguchi T.;
RT "A complementary DNA for human choline acetyltransferase induces two forms
RT of enzyme with different molecular weights in cultured cells.";
RL Brain Res. Mol. Brain Res. 16:287-294(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS M; R AND S), ALTERNATIVE
RP SPLICING, VARIANTS CMS6 PRO-210; ALA-211; THR-305; CYS-420; LYS-441;
RP GLY-482; LEU-498; LEU-506 AND HIS-560, AND VARIANTS THR-120; GLY-392 AND
RP MET-461.
RX PubMed=11172068; DOI=10.1073/pnas.98.4.2017;
RA Ohno K., Tsujino A., Brengman J.M., Harper C.M., Bajzer Z., Udd B.,
RA Beyring R., Robb S., Kirkham F.J., Engel A.G.;
RT "Choline acetyltransferase mutations cause myasthenic syndrome associated
RT with episodic apnea in humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2017-2022(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM R), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 108-748 (ISOFORM M), AND VARIANTS THR-120 AND
RP MET-461.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 111-669, AND VARIANTS THR-120 AND MET-461.
RX PubMed=1388731; DOI=10.1089/dna.1992.11.593;
RA Lorenzi M.V., Trinidad A.C., Zhang R., Strauss W.L.;
RT "Two mRNAs are transcribed from the human gene for choline
RT acetyltransferase.";
RL DNA Cell Biol. 11:593-603(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-232.
RX PubMed=1339386; DOI=10.1016/0888-7543(92)90395-9;
RA Toussaint J.L., Geoffroy V., Schmitt M., Werner A., Garnier J.-M.,
RA Simoni P., Kempf J.;
RT "Human choline acetyltransferase (CHAT): partial gene sequence and
RT potential control regions.";
RL Genomics 12:412-416(1992).
RN [8]
RP PROTEIN SEQUENCE OF 161-182; 271-295; 340-352; 376-382; 404-415; 550-559;
RP 572-583; 620-632; 644-648; 650-662 AND 739-748.
RC TISSUE=Placenta;
RX PubMed=3183663; DOI=10.1111/j.1471-4159.1988.tb01166.x;
RA Hersh L.B., Takane K., Gylys K., Moomaw C., Slaughter C.;
RT "Conservation of amino acid sequences between human and porcine choline
RT acetyltransferase.";
RL J. Neurochem. 51:1843-1845(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 688-738.
RC TISSUE=Lymphocyte;
RX PubMed=1784419; DOI=10.1016/0304-3940(91)90299-9;
RA Cervini R., Rocchi M., DiDonato S., Finocchiaro G.;
RT "Isolation and sub-chromosomal localization of a DNA fragment of the human
RT choline acetyltransferase gene.";
RL Neurosci. Lett. 132:191-194(1991).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 120-733 IN COMPLEXES WITH CHOLINE
RP AND ACETYL COENZYME A, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17144655; DOI=10.1021/bi061536l;
RA Kim A.-R., Rylett R.J., Shilton B.H.;
RT "Substrate binding and catalytic mechanism of human choline
RT acetyltransferase.";
RL Biochemistry 45:14621-14631(2006).
RN [11]
RP VARIANT CMS6 THR-336.
RX PubMed=12756141; DOI=10.1001/archneur.60.5.761;
RA Kraner S., Laufenberg I., Strassburg H.M., Sieb J.P., Steinlein O.K.;
RT "Congenital myasthenic syndrome with episodic apnea in patients homozygous
RT for a CHAT missense mutation.";
RL Arch. Neurol. 60:761-763(2003).
CC -!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh)
CC from acetyl CoA and choline at cholinergic synapses.
CC {ECO:0000269|PubMed:17144655}.
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:0000269|PubMed:17144655};
CC -!- INTERACTION:
CC P28329-3; Q6H8Q1-8: ABLIM2; NbExp=3; IntAct=EBI-25837549, EBI-16436655;
CC P28329-3; Q8N302-2: AGGF1; NbExp=3; IntAct=EBI-25837549, EBI-25838028;
CC P28329-3; D3DTF8: APLN; NbExp=3; IntAct=EBI-25837549, EBI-22002556;
CC P28329-3; Q9NXL2-1: ARHGEF38; NbExp=3; IntAct=EBI-25837549, EBI-18172597;
CC P28329-3; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-25837549, EBI-10254793;
CC P28329-3; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-25837549, EBI-718459;
CC P28329-3; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-25837549, EBI-742750;
CC P28329-3; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-25837549, EBI-9092016;
CC P28329-3; Q9ULD4-2: BRPF3; NbExp=3; IntAct=EBI-25837549, EBI-23662416;
CC P28329-3; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-25837549, EBI-10693038;
CC P28329-3; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-25837549, EBI-7317823;
CC P28329-3; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-25837549, EBI-751596;
CC P28329-3; P20807-4: CAPN3; NbExp=3; IntAct=EBI-25837549, EBI-11532021;
CC P28329-3; O00257-3: CBX4; NbExp=3; IntAct=EBI-25837549, EBI-4392727;
CC P28329-3; Q6ZP82: CCDC141; NbExp=3; IntAct=EBI-25837549, EBI-928795;
CC P28329-3; O95674: CDS2; NbExp=3; IntAct=EBI-25837549, EBI-3913685;
CC P28329-3; Q9H3R5: CENPH; NbExp=3; IntAct=EBI-25837549, EBI-1003700;
CC P28329-3; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-25837549, EBI-749253;
CC P28329-3; Q9H2A9: CHST8; NbExp=3; IntAct=EBI-25837549, EBI-21642354;
CC P28329-3; Q92782-2: DPF1; NbExp=3; IntAct=EBI-25837549, EBI-23669343;
CC P28329-3; Q14117: DPYS; NbExp=3; IntAct=EBI-25837549, EBI-12275416;
CC P28329-3; O14641: DVL2; NbExp=3; IntAct=EBI-25837549, EBI-740850;
CC P28329-3; Q658K8: EEF1DP3; NbExp=3; IntAct=EBI-25837549, EBI-10248874;
CC P28329-3; Q6UXG2-3: ELAPOR1; NbExp=3; IntAct=EBI-25837549, EBI-12920100;
CC P28329-3; O00472: ELL2; NbExp=3; IntAct=EBI-25837549, EBI-395274;
CC P28329-3; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-25837549, EBI-10213520;
CC P28329-3; Q15910-2: EZH2; NbExp=3; IntAct=EBI-25837549, EBI-10699473;
CC P28329-3; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-25837549, EBI-8468186;
CC P28329-3; P15407: FOSL1; NbExp=3; IntAct=EBI-25837549, EBI-744510;
CC P28329-3; P55318: FOXA3; NbExp=3; IntAct=EBI-25837549, EBI-3910364;
CC P28329-3; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-25837549, EBI-9088619;
CC P28329-3; P23769-2: GATA2; NbExp=3; IntAct=EBI-25837549, EBI-21856389;
CC P28329-3; P23771: GATA3; NbExp=3; IntAct=EBI-25837549, EBI-6664760;
CC P28329-3; Q15486: GUSBP1; NbExp=3; IntAct=EBI-25837549, EBI-712457;
CC P28329-3; Q8IV36: HID1; NbExp=3; IntAct=EBI-25837549, EBI-743438;
CC P28329-3; Q4VB01: HOXB1; NbExp=3; IntAct=EBI-25837549, EBI-17494170;
CC P28329-3; Q53GQ0: HSD17B12; NbExp=3; IntAct=EBI-25837549, EBI-2963255;
CC P28329-3; P10809: HSPD1; NbExp=3; IntAct=EBI-25837549, EBI-352528;
CC P28329-3; P41134: ID1; NbExp=3; IntAct=EBI-25837549, EBI-1215527;
CC P28329-3; Q9NZH6: IL37; NbExp=3; IntAct=EBI-25837549, EBI-3862125;
CC P28329-3; Q8NA54: IQUB; NbExp=3; IntAct=EBI-25837549, EBI-10220600;
CC P28329-3; Q86U28: ISCA2; NbExp=3; IntAct=EBI-25837549, EBI-10258659;
CC P28329-3; P17275: JUNB; NbExp=3; IntAct=EBI-25837549, EBI-748062;
CC P28329-3; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-25837549, EBI-743960;
CC P28329-3; Q6P597: KLC3; NbExp=3; IntAct=EBI-25837549, EBI-1643885;
CC P28329-3; P08727: KRT19; NbExp=3; IntAct=EBI-25837549, EBI-742756;
CC P28329-3; Q14525: KRT33B; NbExp=3; IntAct=EBI-25837549, EBI-1049638;
CC P28329-3; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-25837549, EBI-10261141;
CC P28329-3; Q6IAA8: LAMTOR1; NbExp=3; IntAct=EBI-25837549, EBI-715385;
CC P28329-3; Q14847-2: LASP1; NbExp=3; IntAct=EBI-25837549, EBI-9088686;
CC P28329-3; P27338: MAOB; NbExp=3; IntAct=EBI-25837549, EBI-3911344;
CC P28329-3; Q9GZQ8: MAP1LC3B; NbExp=3; IntAct=EBI-25837549, EBI-373144;
CC P28329-3; Q53S70: MGC4677; NbExp=3; IntAct=EBI-25837549, EBI-10242717;
CC P28329-3; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-25837549, EBI-2801965;
CC P28329-3; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-25837549, EBI-25835557;
CC P28329-3; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-25837549, EBI-743811;
CC P28329-3; Q8TCY5: MRAP; NbExp=3; IntAct=EBI-25837549, EBI-9538727;
CC P28329-3; Q6IN84-2: MRM1; NbExp=3; IntAct=EBI-25837549, EBI-25835707;
CC P28329-3; Q96H12: MSANTD3; NbExp=3; IntAct=EBI-25837549, EBI-8466227;
CC P28329-3; P01106: MYC; NbExp=3; IntAct=EBI-25837549, EBI-447544;
CC P28329-3; P41271-2: NBL1; NbExp=3; IntAct=EBI-25837549, EBI-12135485;
CC P28329-3; P14598: NCF1; NbExp=3; IntAct=EBI-25837549, EBI-395044;
CC P28329-3; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-25837549, EBI-928842;
CC P28329-3; Q5BJF6-2: ODF2; NbExp=3; IntAct=EBI-25837549, EBI-9090919;
CC P28329-3; Q3SX64: ODF3L2; NbExp=3; IntAct=EBI-25837549, EBI-6660184;
CC P28329-3; Q9H8K7: PAAT; NbExp=3; IntAct=EBI-25837549, EBI-714785;
CC P28329-3; Q9NR21-5: PARP11; NbExp=3; IntAct=EBI-25837549, EBI-17159452;
CC P28329-3; Q5VU43-8: PDE4DIP; NbExp=3; IntAct=EBI-25837549, EBI-25837868;
CC P28329-3; Q13956: PDE6H; NbExp=3; IntAct=EBI-25837549, EBI-10231995;
CC P28329-3; Q5SXH7-1: PLEKHS1; NbExp=3; IntAct=EBI-25837549, EBI-26412802;
CC P28329-3; Q96T60: PNKP; NbExp=3; IntAct=EBI-25837549, EBI-1045072;
CC P28329-3; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-25837549, EBI-710402;
CC P28329-3; Q86UA1: PRPF39; NbExp=3; IntAct=EBI-25837549, EBI-2803203;
CC P28329-3; Q15311: RALBP1; NbExp=3; IntAct=EBI-25837549, EBI-749285;
CC P28329-3; Q8TBY0: RBM46; NbExp=3; IntAct=EBI-25837549, EBI-12068216;
CC P28329-3; Q04206: RELA; NbExp=3; IntAct=EBI-25837549, EBI-73886;
CC P28329-3; P47804-3: RGR; NbExp=3; IntAct=EBI-25837549, EBI-25834767;
CC P28329-3; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-25837549, EBI-751555;
CC P28329-3; P62899: RPL31; NbExp=3; IntAct=EBI-25837549, EBI-1053664;
CC P28329-3; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-25837549, EBI-10248967;
CC P28329-3; Q9BY12-3: SCAPER; NbExp=3; IntAct=EBI-25837549, EBI-25837959;
CC P28329-3; Q86SQ7-2: SDCCAG8; NbExp=3; IntAct=EBI-25837549, EBI-10696955;
CC P28329-3; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-25837549, EBI-10696971;
CC P28329-3; Q496A3: SPATS1; NbExp=3; IntAct=EBI-25837549, EBI-3923692;
CC P28329-3; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-25837549, EBI-7082156;
CC P28329-3; Q9C004: SPRY4; NbExp=3; IntAct=EBI-25837549, EBI-354861;
CC P28329-3; Q92783-2: STAM; NbExp=3; IntAct=EBI-25837549, EBI-12025738;
CC P28329-3; Q8N4C7: STX19; NbExp=3; IntAct=EBI-25837549, EBI-8484990;
CC P28329-3; O75528: TADA3; NbExp=3; IntAct=EBI-25837549, EBI-473249;
CC P28329-3; Q15814: TBCC; NbExp=3; IntAct=EBI-25837549, EBI-15695297;
CC P28329-3; O15273: TCAP; NbExp=3; IntAct=EBI-25837549, EBI-954089;
CC P28329-3; Q96A09: TENT5B; NbExp=3; IntAct=EBI-25837549, EBI-752030;
CC P28329-3; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-25837549, EBI-17438286;
CC P28329-3; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-25837549, EBI-10242677;
CC P28329-3; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-25837549, EBI-25831574;
CC P28329-3; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-25837549, EBI-11525489;
CC P28329-3; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-25837549, EBI-739485;
CC P28329-3; Q99598: TSNAX; NbExp=3; IntAct=EBI-25837549, EBI-742638;
CC P28329-3; P49459: UBE2A; NbExp=3; IntAct=EBI-25837549, EBI-2339348;
CC P28329-3; P11441: UBL4A; NbExp=3; IntAct=EBI-25837549, EBI-356983;
CC P28329-3; Q9H270: VPS11; NbExp=3; IntAct=EBI-25837549, EBI-373380;
CC P28329-3; P19544-6: WT1; NbExp=3; IntAct=EBI-25837549, EBI-11745701;
CC P28329-3; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-25837549, EBI-14104088;
CC P28329-3; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-25837549, EBI-18036029;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=M; Synonyms=83 kDa;
CC IsoId=P28329-1; Sequence=Displayed;
CC Name=S; Synonyms=74 kDa;
CC IsoId=P28329-2; Sequence=VSP_000790;
CC Name=R; Synonyms=70 kDa;
CC IsoId=P28329-3; Sequence=VSP_000791;
CC -!- DISEASE: Myasthenic syndrome, congenital, 6, presynaptic (CMS6)
CC [MIM:254210]: A form of congenital myasthenic syndrome, a group of
CC disorders characterized by failure of neuromuscular transmission,
CC including pre-synaptic, synaptic, and post-synaptic disorders that are
CC not of autoimmune origin. Clinical features are easy fatigability and
CC muscle weakness affecting the axial and limb muscles (with hypotonia in
CC early-onset forms), the ocular muscles (leading to ptosis and
CC ophthalmoplegia), and the facial and bulbar musculature (affecting
CC sucking and swallowing, and leading to dysphonia). The symptoms
CC fluctuate and worsen with physical effort. CMS6 affected individuals
CC have myasthenic symptoms since birth or early infancy, negative tests
CC for anti-AChR antibodies, and abrupt episodic crises with increased
CC weakness, bulbar paralysis, and apnea precipitated by undue exertion,
CC fever, or excitement. CMS6 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:11172068, ECO:0000269|PubMed:12756141}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Choline acetyltransferase entry;
CC URL="https://en.wikipedia.org/wiki/Choline_acetyltransferase";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S56138; AAA14245.1; -; mRNA.
DR EMBL; AF305907; AAK08953.1; -; mRNA.
DR EMBL; AF305906; AAK08950.1; -; Genomic_DNA.
DR EMBL; AF305894; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305895; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305896; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305897; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305898; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305899; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305900; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305901; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305902; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305903; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305904; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305905; AAK08950.1; JOINED; Genomic_DNA.
DR EMBL; AF305908; AAK08954.1; -; mRNA.
DR EMBL; AF305906; AAK08951.1; -; Genomic_DNA.
DR EMBL; AF305894; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305895; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305896; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305897; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305898; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305899; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305900; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305901; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305902; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305903; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305904; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305905; AAK08951.1; JOINED; Genomic_DNA.
DR EMBL; AF305909; AAK08955.1; -; mRNA.
DR EMBL; AF305906; AAK08952.1; -; Genomic_DNA.
DR EMBL; AF305894; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305895; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305896; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305897; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305898; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305899; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305900; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305901; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305902; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305903; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305904; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AF305905; AAK08952.1; JOINED; Genomic_DNA.
DR EMBL; AC073366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471187; EAW93086.1; -; Genomic_DNA.
DR EMBL; BC130615; AAI30616.1; -; mRNA.
DR EMBL; BC130617; AAI30618.1; -; mRNA.
DR EMBL; S45018; AAB23557.2; -; mRNA.
DR EMBL; X56585; CAA39923.1; -; Genomic_DNA.
DR EMBL; X56879; CAA40201.1; -; Genomic_DNA.
DR CCDS; CCDS44389.1; -. [P28329-2]
DR CCDS; CCDS7232.1; -. [P28329-1]
DR CCDS; CCDS7233.1; -. [P28329-3]
DR PIR; I52631; A60202.
DR RefSeq; NP_001136401.1; NM_001142929.1. [P28329-3]
DR RefSeq; NP_001136405.1; NM_001142933.1. [P28329-2]
DR RefSeq; NP_001136406.1; NM_001142934.1. [P28329-3]
DR RefSeq; NP_065574.3; NM_020549.4. [P28329-1]
DR RefSeq; NP_066264.3; NM_020984.3. [P28329-3]
DR RefSeq; NP_066265.3; NM_020985.3. [P28329-3]
DR RefSeq; NP_066266.3; NM_020986.3. [P28329-3]
DR PDB; 2FY2; X-ray; 2.25 A; A=120-733.
DR PDB; 2FY3; X-ray; 2.27 A; A=120-733.
DR PDB; 2FY4; X-ray; 2.30 A; A=120-733.
DR PDB; 2FY5; X-ray; 2.60 A; A=120-733.
DR PDB; 7AMD; X-ray; 2.25 A; A=120-733.
DR PDBsum; 2FY2; -.
DR PDBsum; 2FY3; -.
DR PDBsum; 2FY4; -.
DR PDBsum; 2FY5; -.
DR PDBsum; 7AMD; -.
DR AlphaFoldDB; P28329; -.
DR SMR; P28329; -.
DR BioGRID; 107528; 6.
DR IntAct; P28329; 105.
DR MINT; P28329; -.
DR STRING; 9606.ENSP00000337103; -.
DR BindingDB; P28329; -.
DR ChEMBL; CHEMBL4039; -.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR DrugBank; DB00184; Nicotine.
DR GlyGen; P28329; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P28329; -.
DR PhosphoSitePlus; P28329; -.
DR BioMuta; CHAT; -.
DR DMDM; 281185509; -.
DR MassIVE; P28329; -.
DR PaxDb; P28329; -.
DR PeptideAtlas; P28329; -.
DR PRIDE; P28329; -.
DR ProteomicsDB; 54466; -. [P28329-1]
DR ProteomicsDB; 54467; -. [P28329-2]
DR ProteomicsDB; 54468; -. [P28329-3]
DR Antibodypedia; 27616; 664 antibodies from 43 providers.
DR DNASU; 1103; -.
DR Ensembl; ENST00000337653.7; ENSP00000337103.2; ENSG00000070748.19. [P28329-1]
DR Ensembl; ENST00000339797.5; ENSP00000343486.1; ENSG00000070748.19. [P28329-3]
DR Ensembl; ENST00000351556.7; ENSP00000345878.3; ENSG00000070748.19. [P28329-3]
DR Ensembl; ENST00000395559.6; ENSP00000378926.2; ENSG00000070748.19. [P28329-3]
DR Ensembl; ENST00000395562.2; ENSP00000378929.2; ENSG00000070748.19. [P28329-2]
DR GeneID; 1103; -.
DR KEGG; hsa:1103; -.
DR MANE-Select; ENST00000337653.7; ENSP00000337103.2; NM_020549.5; NP_065574.4.
DR UCSC; uc001jhv.1; human. [P28329-1]
DR CTD; 1103; -.
DR DisGeNET; 1103; -.
DR GeneCards; CHAT; -.
DR GeneReviews; CHAT; -.
DR HGNC; HGNC:1912; CHAT.
DR HPA; ENSG00000070748; Group enriched (brain, placenta).
DR MalaCards; CHAT; -.
DR MIM; 118490; gene.
DR MIM; 254210; phenotype.
DR neXtProt; NX_P28329; -.
DR OpenTargets; ENSG00000070748; -.
DR Orphanet; 98914; Presynaptic congenital myasthenic syndromes.
DR PharmGKB; PA26448; -.
DR VEuPathDB; HostDB:ENSG00000070748; -.
DR eggNOG; KOG3717; Eukaryota.
DR GeneTree; ENSGT01050000244830; -.
DR HOGENOM; CLU_013513_3_0_1; -.
DR InParanoid; P28329; -.
DR OMA; MAYRDPV; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; P28329; -.
DR TreeFam; TF313836; -.
DR BRENDA; 2.3.1.6; 2681.
DR PathwayCommons; P28329; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR SABIO-RK; P28329; -.
DR SignaLink; P28329; -.
DR SIGNOR; P28329; -.
DR BioGRID-ORCS; 1103; 6 hits in 1064 CRISPR screens.
DR ChiTaRS; CHAT; human.
DR EvolutionaryTrace; P28329; -.
DR GeneWiki; Choline_acetyltransferase; -.
DR GenomeRNAi; 1103; -.
DR Pharos; P28329; Tchem.
DR PRO; PR:P28329; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P28329; protein.
DR Bgee; ENSG00000070748; Expressed in putamen and 50 other tissues.
DR ExpressionAtlas; P28329; baseline and differential.
DR Genevisible; P28329; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004102; F:choline O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0008292; P:acetylcholine biosynthetic process; IBA:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR GO; GO:0006836; P:neurotransmitter transport; TAS:Reactome.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 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; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing;
KW Congenital myasthenic syndrome; Direct protein sequencing; Disease variant;
KW Neurotransmitter biosynthesis; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..748
FT /note="Choline O-acetyltransferase"
FT /id="PRO_0000210154"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /note="Proton acceptor"
FT BINDING 520..532
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 558
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 659
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32738"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32738"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform R)"
FT /evidence="ECO:0000303|PubMed:11172068,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000791"
FT VAR_SEQ 1..95
FT /note="MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGGRGDPGDVGGPA
FT GNPGCSPHPRAATRPPPLPAHTPAHTPEWCGAASAEAAEPRRA -> MWPECRDEALST
FT V (in isoform S)"
FT /evidence="ECO:0000303|PubMed:11172068"
FT /id="VSP_000790"
FT VARIANT 47
FT /note="D -> E (in dbSNP:rs3810948)"
FT /id="VAR_046683"
FT VARIANT 120
FT /note="A -> T (in dbSNP:rs3810950)"
FT /evidence="ECO:0000269|PubMed:11172068,
FT ECO:0000269|PubMed:1388731, ECO:0000269|PubMed:15489334"
FT /id="VAR_011675"
FT VARIANT 210
FT /note="L -> P (in CMS6; impaired activity;
FT dbSNP:rs121912820)"
FT /evidence="ECO:0000269|PubMed:11172068"
FT /id="VAR_011666"
FT VARIANT 211
FT /note="P -> A (in CMS6; impaired activity;
FT dbSNP:rs121912815)"
FT /evidence="ECO:0000269|PubMed:11172068"
FT /id="VAR_011667"
FT VARIANT 222
FT /note="R -> P (in dbSNP:rs8178989)"
FT /id="VAR_046684"
FT VARIANT 243
FT /note="L -> F (in dbSNP:rs8178990)"
FT /id="VAR_046685"
FT VARIANT 299
FT /note="P -> L (in dbSNP:rs868749)"
FT /id="VAR_046686"
FT VARIANT 305
FT /note="I -> T (in CMS6; impaired activity;
FT dbSNP:rs75466054)"
FT /evidence="ECO:0000269|PubMed:11172068"
FT /id="VAR_011668"
FT VARIANT 336
FT /note="I -> T (in CMS6; dbSNP:rs121912823)"
FT /evidence="ECO:0000269|PubMed:12756141"
FT /id="VAR_038605"
FT VARIANT 392
FT /note="A -> G"
FT /evidence="ECO:0000269|PubMed:11172068,
FT ECO:0000269|PubMed:1337937"
FT /id="VAR_011676"
FT VARIANT 400
FT /note="D -> N (in dbSNP:rs8178991)"
FT /id="VAR_046687"
FT VARIANT 420
FT /note="R -> C (in CMS6; impaired activity;
FT dbSNP:rs121912822)"
FT /evidence="ECO:0000269|PubMed:11172068"
FT /id="VAR_011669"
FT VARIANT 441
FT /note="E -> K (in CMS6; completely lack activity;
FT dbSNP:rs121912816)"
FT /evidence="ECO:0000269|PubMed:11172068"
FT /id="VAR_011670"
FT VARIANT 461
FT /note="V -> M (in dbSNP:rs4838544)"
FT /evidence="ECO:0000269|PubMed:11172068,
FT ECO:0000269|PubMed:1337937, ECO:0000269|PubMed:1388731,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_046688"
FT VARIANT 482
FT /note="R -> G (in CMS6; impaired activity;
FT dbSNP:rs121912818)"
FT /evidence="ECO:0000269|PubMed:11172068"
FT /id="VAR_011671"
FT VARIANT 498
FT /note="S -> L (in CMS6; impaired activity;
FT dbSNP:rs121912821)"
FT /evidence="ECO:0000269|PubMed:11172068"
FT /id="VAR_011672"
FT VARIANT 506
FT /note="V -> L (in CMS6; impaired activity;
FT dbSNP:rs121912817)"
FT /evidence="ECO:0000269|PubMed:11172068"
FT /id="VAR_011673"
FT VARIANT 560
FT /note="R -> H (in CMS6; impaired activity;
FT dbSNP:rs121912819)"
FT /evidence="ECO:0000269|PubMed:11172068"
FT /id="VAR_011674"
FT CONFLICT 151
FT /note="R -> Q (in Ref. 7; CAA39923)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..262
FT /note="GQ -> PE (in Ref. 1; AAA14245)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="V -> L (in Ref. 6; AAB23557)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="G -> A (in Ref. 1; AAA14245)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="C -> S (in Ref. 6; AAB23557)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="V -> L (in Ref. 6; AAB23557)"
FT /evidence="ECO:0000305"
FT CONFLICT 629..630
FT /note="EL -> DV (in Ref. 6; AAB23557)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="T -> M (in Ref. 6; AAB23557)"
FT /evidence="ECO:0000305"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 175..189
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2FY5"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:2FY2"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 228..250
FT /evidence="ECO:0007829|PDB:2FY2"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:7AMD"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 300..308
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 326..340
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 350..355
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 372..382
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:2FY2"
FT TURN 413..418
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:2FY3"
FT HELIX 447..461
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 489..508
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 509..516
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 521..525
FT /evidence="ECO:0007829|PDB:2FY2"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 531..547
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 575..585
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 593..615
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 621..634
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 640..643
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 645..650
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 654..659
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 678..684
FT /evidence="ECO:0007829|PDB:2FY2"
FT STRAND 689..696
FT /evidence="ECO:0007829|PDB:2FY2"
FT HELIX 704..722
FT /evidence="ECO:0007829|PDB:2FY2"
SQ SEQUENCE 748 AA; 82536 MW; A902364081915391 CRC64;
MGLRTAKKRG LGGGGKWKRE EGGGTRGRRE VRPACFLQSG GRGDPGDVGG PAGNPGCSPH
PRAATRPPPL PAHTPAHTPE WCGAASAEAA EPRRAGPHLC IPAPGLTKTP ILEKVPRKMA
AKTPSSEESG LPKLPVPPLQ QTLATYLQCM RHLVSEEQFR KSQAIVQQFG APGGLGETLQ
QKLLERQEKT ANWVSEYWLN DMYLNNRLAL PVNSSPAVIF ARQHFPGTDD QLRFAASLIS
GVLSYKALLD SHSIPTDCAK GQLSGQPLCM KQYYGLFSSY RLPGHTQDTL VAQNSSIMPE
PEHVIVACCN QFFVLDVVIN FRRLSEGDLF TQLRKIVKMA SNEDERLPPI GLLTSDGRSE
WAEARTVLVK DSTNRDSLDM IERCICLVCL DAPGGVELSD THRALQLLHG GGYSKNGANR
WYDKSLQFVV GRDGTCGVVC EHSPFDGIVL VQCTEHLLKH VTQSSRKLIR ADSVSELPAP
RRLRWKCSPE IQGHLASSAE KLQRIVKNLD FIVYKFDNYG KTFIKKQKCS PDAFIQVALQ
LAFYRLHRRL VPTYESASIR RFQEGRVDNI RSATPEALAF VRAVTDHKAA VPASEKLLLL
KDAIRAQTAY TVMAITGMAI DNHLLALREL ARAMCKELPE MFMDETYLMS NRFVLSTSQV
PTTTEMFCCY GPVVPNGYGA CYNPQPETIL FCISSFHSCK ETSSSKFAKA VEESLIDMRD
LCSLLPPTES KPLATKEKAT RPSQGHQP
