ID CLAT_HUMAN STANDARD; PRT; 748 AA. AC P28329; Q16488; Q9BQ23; Q9BQ35; Q9BQE1; DT 01-DEC-1992 (Rel. 24, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Choline O-acetyltransferase (EC 2.3.1.6) (CHOACTase) (Choline DE acetylase) (ChAT). GN Name=CHAT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Spinal cord; RX MEDLINE=93180642; PubMed=1337937; RA Oda Y., Nakanishi I., Deguchi T.; RT "A complementary DNA for human choline acetyltransferase induces two RT forms of enzyme with different molecular weights in cultured cells."; RL Brain Res. Mol. Brain Res. 16:287-294(1992). RN [2] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, VARIANTS FIMG2 PRO-210; RP ALA-211; THR-305; CYS-420; LYS-441; GLY-482; LEU-498; LEU-506 AND RP HIS-560, AND VARIANTS THR-120 AND GLY-392. RX MEDLINE=21117155; 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 RT associated with episodic apnea in humans."; RL Proc. Natl. Acad. Sci. U.S.A. 98:2017-2022(2001). RN [3] RP SEQUENCE OF 111-669 FROM N.A. RX MEDLINE=93000480; PubMed=1388731; 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 [4] RP SEQUENCE OF 109-232 FROM N.A. RX MEDLINE=92155737; PubMed=1339386; 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 [5] RP SEQUENCE OF 688-738 FROM N.A. RC TISSUE=Lymphocytes; RX MEDLINE=92149876; PubMed=1784419; RA Cervini R., Rocchi M., DiDonato S., Finocchiaro G.; RT "Isolation and sub-chromosomal localization of a DNA fragment of the RT human choline acetyltransferase gene."; RL Neurosci. Lett. 132:191-194(1991). CC -!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine CC (ACh) from acetyl CoA and choline at cholinergic synapses. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + choline = CoA + O-acetylcholine. 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: Defects in CHAT are the cause of familial infantile CC myasthenia gravis 2 (FIMG2) [MIM:254210]; also known as CMS-EA. CC FIMG2 patients have myasthenic symptoms since birth or early CC infancy, negative tests for anti-AChR antibodies, and abrupt CC episodic crises with increased weakness, bulbar paralysis, and CC apnea precipitated by undue exertion, fever, or excitement. CC Inheritance is autosomal recessive. CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase CC family. 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; -. DR EMBL; AF305907; AAK08953.1; -. DR EMBL; AF305906; AAK08950.1; -. DR EMBL; AF305894; AAK08950.1; JOINED. DR EMBL; AF305895; AAK08950.1; JOINED. DR EMBL; AF305896; AAK08950.1; JOINED. DR EMBL; AF305897; AAK08950.1; JOINED. DR EMBL; AF305898; AAK08950.1; JOINED. DR EMBL; AF305899; AAK08950.1; JOINED. DR EMBL; AF305900; AAK08950.1; JOINED. DR EMBL; AF305901; AAK08950.1; JOINED. DR EMBL; AF305902; AAK08950.1; JOINED. DR EMBL; AF305903; AAK08950.1; JOINED. DR EMBL; AF305904; AAK08950.1; JOINED. DR EMBL; AF305905; AAK08950.1; JOINED. DR EMBL; AF305908; AAK08954.1; -. DR EMBL; AF305906; AAK08951.1; -. DR EMBL; AF305894; AAK08951.1; JOINED. DR EMBL; AF305895; AAK08951.1; JOINED. DR EMBL; AF305896; AAK08951.1; JOINED. DR EMBL; AF305897; AAK08951.1; JOINED. DR EMBL; AF305898; AAK08951.1; JOINED. DR EMBL; AF305899; AAK08951.1; JOINED. DR EMBL; AF305900; AAK08951.1; JOINED. DR EMBL; AF305901; AAK08951.1; JOINED. DR EMBL; AF305902; AAK08951.1; JOINED. DR EMBL; AF305903; AAK08951.1; JOINED. DR EMBL; AF305904; AAK08951.1; JOINED. DR EMBL; AF305905; AAK08951.1; JOINED. DR EMBL; AF305909; AAK08955.1; -. DR EMBL; AF305906; AAK08952.1; -. DR EMBL; AF305894; AAK08952.1; JOINED. DR EMBL; AF305895; AAK08952.1; JOINED. DR EMBL; AF305896; AAK08952.1; JOINED. DR EMBL; AF305897; AAK08952.1; JOINED. DR EMBL; AF305898; AAK08952.1; JOINED. DR EMBL; AF305899; AAK08952.1; JOINED. DR EMBL; AF305900; AAK08952.1; JOINED. DR EMBL; AF305901; AAK08952.1; JOINED. DR EMBL; AF305902; AAK08952.1; JOINED. DR EMBL; AF305903; AAK08952.1; JOINED. DR EMBL; AF305904; AAK08952.1; JOINED. DR EMBL; AF305905; AAK08952.1; JOINED. DR EMBL; S45018; AAB23557.2; -. DR EMBL; X56585; CAA39923.1; -. DR EMBL; X56879; CAA40201.1; -. DR PIR; I52631; A60202. DR HSSP; P43155; 1NM8. DR Genew; HGNC:1912; CHAT. DR MIM; 118490; -. DR MIM; 254210; -. DR GO; GO:0005737; C:cytoplasm; TAS. DR GO; GO:0005634; C:nucleus; TAS. DR InterPro; IPR000542; Carn_acyl_trans. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. KW Transferase; Acyltransferase; Neurotransmitter biosynthesis; KW Alternative splicing; Disease mutation; Polymorphism. FT ACT_SITE 442 442 Potential. FT VARSPLIC 1 95 MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGG FT RGDPGDVGGPAGNPGCSPHPRAATRPPPLPAHTPAHTPEWC FT GAASAEAAEPRRA -> MWPECRDEALSTV (in FT isoform S). FT /FTId=VSP_000790. FT VARSPLIC 1 118 Missing (in isoform R). FT /FTId=VSP_000791. FT VARIANT 120 120 A -> T. FT /FTId=VAR_011675. FT VARIANT 210 210 L -> P (in FIMG2; impaired activity). FT /FTId=VAR_011666. FT VARIANT 211 211 P -> A (in FIMG2; impaired activity). FT /FTId=VAR_011667. FT VARIANT 305 305 I -> T (in FIMG2; impaired activity). FT /FTId=VAR_011668. FT VARIANT 392 392 A -> G. FT /FTId=VAR_011676. FT VARIANT 420 420 R -> C (in FIMG2; impaired activity). FT /FTId=VAR_011669. FT VARIANT 441 441 E -> K (in FIMG2; completely lack FT activity). FT /FTId=VAR_011670. FT VARIANT 482 482 R -> G (in FIMG2; impaired activity). FT /FTId=VAR_011671. FT VARIANT 498 498 S -> L (in FIMG2; impaired activity). FT /FTId=VAR_011672. FT VARIANT 506 506 V -> L (in FIMG2; impaired activity). FT /FTId=VAR_011673. FT VARIANT 560 560 R -> H (in FIMG2; impaired activity). FT /FTId=VAR_011674. FT CONFLICT 151 151 R -> Q (in Ref. 4). FT CONFLICT 261 262 GQ -> PE (in Ref. 1). FT CONFLICT 396 396 V -> L (in Ref. 3). FT CONFLICT 434 434 G -> A (in Ref. 1). FT CONFLICT 529 529 C -> S (in Ref. 3). FT CONFLICT 567 567 V -> L (in Ref. 3). FT CONFLICT 629 630 EL -> DV (in Ref. 3). FT CONFLICT 664 664 T -> M (in Ref. 3). SQ SEQUENCE 748 AA; 82567 MW; 0D537659F876C497 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 MTQSSRKLIR 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 //