CLAT_PIG
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 03-AUG-2022, entry version 129.
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; P13222; -.
DR PeptideAtlas; P13222; -.
DR PRIDE; P13222; -.
DR Ensembl; ENSSSCT00025104470; ENSSSCP00025046444; ENSSSCG00025075663.
DR Ensembl; ENSSSCT00035003226; ENSSSCP00035001105; ENSSSCG00035002581.
DR Ensembl; ENSSSCT00055026523; ENSSSCP00055021081; ENSSSCG00055013438.
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; 559299at2759; -.
DR TreeFam; TF313836; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P13222; SS.
DR GO; GO:0004102; F:choline O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
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; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
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
