ID G3ND37_GASAC Unreviewed; 627 AA.
AC G3ND37;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Choline O-acetyltransferase {ECO:0000256|ARBA:ARBA00040495};
DE EC=2.3.1.6 {ECO:0000256|ARBA:ARBA00039091};
GN Name=CHAT {ECO:0000313|Ensembl:ENSGACP00000003237.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000003237.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000003237.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000003237.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh)
CC from acetyl CoA and choline at cholinergic synapses.
CC {ECO:0000256|ARBA:ARBA00037088}.
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:0000256|ARBA:ARBA00036720};
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR AlphaFoldDB; G3ND37; -.
DR STRING; 69293.ENSGACP00000003237; -.
DR Ensembl; ENSGACT00000003248.1; ENSGACP00000003237.1; ENSGACG00000002482.1.
DR eggNOG; KOG3717; Eukaryota.
DR GeneTree; ENSGT01060000248556; -.
DR InParanoid; G3ND37; -.
DR OMA; QCSEFLM; -.
DR TreeFam; TF313836; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000002482; Expressed in camera-type eye and 1 other cell type or tissue.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003801};
KW Neurotransmitter biosynthesis {ECO:0000256|ARBA:ARBA00022979};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 30..609
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 627 AA; 70228 MW; C096D3D80BFB6C47 CRC64;
LTGLECKDAN HGETDGQRQK NPRHQMLPKV PVPPLKQTLD TYLKCVQHLV KEEQFKKTKA
VVEKFGAPGG VGEVLQKKLL ERRDKTTNWV YDYWLEDMYL NNRLALPVNS SPVMVFPKQM
FRDHKDALRF AAGLIGGVLE YAALIDARAL PVDFARGQLA GTPLCMEQYY RLFKSYRYPG
LKTDTLEVQM DAASSAPRHI VVACKNQFFV LDVVANSKQL TESEILSQLE EIMTMAEKAD
EKLPPFGILT SDGRTEWAQA RDALTKDQTN RDSLALIESC LCVVCLDEPS GLEPRDTNRA
LMMLHGGGRE KNGANRWYDK SMQFVVGMDG ICGVVCEHSA FEGIVMVQCS EYLVKYIAAG
ASKMARSSSI RKLPAPRRLP WKCNAHIQGL LTASGDRLQR VVDNLDMDVF KFNVYGKEFI
KKQKMSPDAF IQVALQLAFY KCNRRLVTTY ESASIRRFQQ GRVDNIRSAT PEALAFVMSM
TDERANVSDS EKIRRLIDAI NAQTNYTIAA ITGMAIDNHL LGLLRIAKEL NVAKPEIFCD
ETYLASNQFV LSTSQVPTTV EMFCCYGPVV PNGYGACYNP QSDHIIFCVS SFWENTQTSS
AVFVKALNES LEEIRDVCNR SGAAATK
//
