ID   CLAT_CHICK              Reviewed;         640 AA.
AC   Q90YJ9;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Choline O-acetyltransferase;
DE            Short=CHOACTase;
DE            Short=ChAT;
DE            Short=Choline acetylase;
DE            EC=2.3.1.6;
GN   Name=CHAT;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=15469882; DOI=10.1016/j.molbrainres.2004.06.014;
RA   Mukherjee R.S., Hausman R.E.;
RT   "Cloning of chicken choline acetyltransferase and its expression in early
RT   embryonic retina.";
RL   Brain Res. Mol. Brain Res. 129:54-66(2004).
CC   -!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh)
CC       from acetyl CoA and choline at cholinergic synapses. {ECO:0000250}.
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   -!- TISSUE SPECIFICITY: Detected in brain and in embryonic retina.
CC       {ECO:0000269|PubMed:15469882}.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AY044155; AAK94673.1; -; mRNA.
DR   RefSeq; NP_989941.1; NM_204610.1.
DR   AlphaFoldDB; Q90YJ9; -.
DR   SMR; Q90YJ9; -.
DR   STRING; 9031.ENSGALP00000003594; -.
DR   BindingDB; Q90YJ9; -.
DR   ChEMBL; CHEMBL2944; -.
DR   PaxDb; Q90YJ9; -.
DR   GeneID; 395314; -.
DR   KEGG; gga:395314; -.
DR   CTD; 1103; -.
DR   VEuPathDB; HostDB:geneid_395314; -.
DR   eggNOG; KOG3717; Eukaryota.
DR   InParanoid; Q90YJ9; -.
DR   OrthoDB; 559299at2759; -.
DR   PhylomeDB; Q90YJ9; -.
DR   PRO; PR:Q90YJ9; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0004102; F:choline O-acetyltransferase activity; IDA:AgBase.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0060416; P:response to growth hormone; IMP:AgBase.
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; PS00440; ACYLTRANSF_C_2; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Neurotransmitter biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..640
FT                   /note="Choline O-acetyltransferase"
FT                   /id="PRO_0000351549"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        334
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         412..424
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         450
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         551
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   640 AA;  72623 MW;  5D07FB959F4020E4 CRC64;
     MPDLEKDMQK KEKDSRSKDE PAVPKLPVPP LQQTLQMYLQ CMKHLVPEEQ FRKTKSIVEQ
     FGVAGGLGES LQLILEERRE ETTNWVFNYW LDDMYLNNRL ALPVNSSPAI IFARQNFKDV
     NDQLRFAANL ISGVQDYKAL LDSHALPVDF ARGQLSGQPL CMKQYYGLFS SYRLPGHTKD
     TLVAQKSCVM PEPEHIIVAC NNQLFVLDVG INFRRLSEGD LFTQLRKIAK MAENEEEMLP
     PIGLLTTDGR TEWAEARTIL MKDSTNRDSL DMIERCICLV CLDGTSGVEL NDTNMALQLL
     HGGGYHKNGA NRWYDKPMQF VVGRDGVCGT VCEHSPFDGI VLVQCTEHLL KHMKESSKKL
     LRADSVSELP APRRLRWKCS PEIQAHLASS AEKLQRIVKN LDFIAYKFVN YGKEFIKKQK
     TSPDAYIQVA LQLAFYRCHR RLVPTYESAS IRRFDEGRVD NIRSATAEAF AFVKAMIDDK
     PALSDSEKMQ RFKDAIAAQT NYTILAITGM AIDNHLLGLR EVAREHFKEL PEIFTDETYL
     TSNRFILSTS QVPTPMEMFC CYGPVVPNGY GACYNPQPEH ILFCISSFKD CKETSSDMLA
     KAVEESLLEI RDLCNKCSSS TAKSLAKQEE ATQLRSDRKL