ID   CLAT_PIG                Reviewed;         641 AA.
AC   P13222;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 137.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ventral spinal cord;
RX   PubMed=3480542; DOI=10.1073/pnas.84.24.9280;
RA   Berrard S., Brice A., Lottspeich F., Braun A., Barde Y.-A., Mallet J.;
RT   "cDNA cloning and complete sequence of porcine choline acetyltransferase:
RT   in vitro translation of the corresponding RNA yields an active protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:9280-9284(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ventral spinal cord;
RX   PubMed=2713713; DOI=10.1016/0361-9230(89)90139-1;
RA   Berrard S., Brice A., Mallet J.;
RT   "Molecular genetic approach to the study of mammalian choline
RT   acetyltransferase.";
RL   Brain Res. Bull. 22:147-153(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-23.
RX   PubMed=8515278; DOI=10.1111/j.1471-4159.1993.tb03569.x;
RA   Hersh L.B., Kong C.F., Sampson C., Mues G., Li Y.P., Fisher A., Hilt D.,
RA   Baetge E.E.;
RT   "Comparison of the promoter region of the human and porcine choline
RT   acetyltransferase genes: localization of an important enhancer region.";
RL   J. Neurochem. 61:306-314(1993).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-12.
RC   TISSUE=Brain;
RX   PubMed=3794697; DOI=10.1111/j.1471-4159.1987.tb13121.x;
RA   Braun A., Barde Y.-A., Lottspeich F., Mewes H.-W., Thoenen H.;
RT   "N-terminal sequence of pig brain choline acetyltransferase purified by a
RT   rapid procedure.";
RL   J. Neurochem. 48:16-21(1987).
CC   -!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh)
CC       from acetyl CoA and choline at cholinergic synapses.
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   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; J03021; AAA31000.1; -; mRNA.
DR   EMBL; M27736; AAA31015.1; -; mRNA.
DR   PIR; A39961; A39961.
DR   RefSeq; NP_001001541.1; NM_001001541.1.
DR   AlphaFoldDB; P13222; -.
DR   SMR; P13222; -.
DR   STRING; 9823.ENSSSCP00000011081; -.
DR   PaxDb; 9823-ENSSSCP00000011081; -.
DR   PeptideAtlas; P13222; -.
DR   Ensembl; ENSSSCT00025104470.1; ENSSSCP00025046444.1; ENSSSCG00025075663.1.
DR   Ensembl; ENSSSCT00035003226.1; ENSSSCP00035001105.1; ENSSSCG00035002581.1.
DR   Ensembl; ENSSSCT00055026523.1; ENSSSCP00055021081.1; ENSSSCG00055013438.1.
DR   GeneID; 396896; -.
DR   KEGG; ssc:396896; -.
DR   CTD; 1103; -.
DR   eggNOG; KOG3717; Eukaryota.
DR   HOGENOM; CLU_013513_3_0_1; -.
DR   InParanoid; P13222; -.
DR   OrthoDB; 1429709at2759; -.
DR   TreeFam; TF313836; -.
DR   Reactome; R-SSC-1483191; Synthesis of PC.
DR   Reactome; R-SSC-264642; Acetylcholine Neurotransmitter Release Cycle.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
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   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; P13222; SS.
PE   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Neurotransmitter biosynthesis;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3794697"
FT   CHAIN           2..641
FT                   /note="Choline O-acetyltransferase"
FT                   /id="PRO_0000210156"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        335
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         413..425
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         552
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32738"
FT   MOD_RES         366
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32738"
SQ   SEQUENCE   641 AA;  71731 MW;  90CFA6931F8CD393 CRC64;
     MPILEKTPPK MAAKSPSSEE EPGLPKLPVP PLQQTLATYL RCMQHLVPEE QFRRSQAIVQ
     QFGAPGGLGE TLQQKLLERQ EQTANWVSEY WLNDMYLNNR LALPVNSSPA VIFARQHFQD
     TNDQLRFAAN LISGVLSYKA LLDSHSIPID CAKGQLSGQP LCMKQYYGLF SSYRLPGHTQ
     DTLVAQKSSV MPEPEHVIVA CCNQFFVLDV VINFRRLSEG DLFTQLRKIV RMASNEDERL
     PPIGLLTSDG RSEWAEARTV LVKDSTNRDS LDMIERCICL VCLDAPGGME LSDTNRALQL
     LHGGGCSKNG ANRWYDKSLQ FVVGRDGTCG VVCEHSPFDG IVLVQCTEHL LKHMVKSSKK
     MVRADSVSEL PAPRRLRWKC SPEIQGLLAS SAEKLQQIVK NLDFTVYKFD DYGKTFIKQQ
     KCSPDAFIQV ALQLAFYRLH GRLVPTYESA SIRRFHEGRV DNIRSATPEA LHFVKAITDH
     ASAMPDSEKL LLLKDAIRAQ TQYTVMAITG MAIDNHLLGL RELAREVCKE LPEMFTDETY
     LMSNRFVLST SQVPTTMEMF CCYGPVVPNG YGACYNPQPE SILFCISSFH GCKETSSTKF
     AKAVEESFIE MKGLCSLSQS GMGKPLATKE KVTRPSQVHQ P
//