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   27-MAR-2024, entry version 208.
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; Q3SX64: CIMAP1D; NbExp=3; IntAct=EBI-25837549, EBI-6660184;
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; 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";
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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   GlyCosmos; P28329; 3 sites, 1 glycan.
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; 9606-ENSP00000337103; -.
DR   PeptideAtlas; P28329; -.
DR   ProteomicsDB; 54466; -. [P28329-1]
DR   ProteomicsDB; 54467; -. [P28329-2]
DR   ProteomicsDB; 54468; -. [P28329-3]
DR   Antibodypedia; 27616; 786 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   AGR; HGNC:1912; -.
DR   CTD; 1103; -.
DR   DisGeNET; 1103; -.
DR   GeneCards; CHAT; -.
DR   GeneReviews; CHAT; -.
DR   HGNC; HGNC:1912; CHAT.
DR   HPA; ENSG00000070748; Tissue enhanced (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; ENSGT01060000248556; -.
DR   HOGENOM; CLU_013513_3_0_1; -.
DR   InParanoid; P28329; -.
DR   OMA; MAMSSYE; -.
DR   OrthoDB; 1429709at2759; -.
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 1143 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 primordial germ cell in gonad and 51 other cell types or tissues.
DR   ExpressionAtlas; P28329; baseline and differential.
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; 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.
DR   Genevisible; P28329; HS.
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
//