ID CLAT_MOUSE Reviewed; 641 AA. AC Q03059; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 08-NOV-2023, entry version 132. 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 Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Spinal cord; RX PubMed=2160042; DOI=10.1016/0169-328x(90)90092-r; RA Ishii K., Oda Y., Ichikawa T., Deguchi T.; RT "Complementary DNAs for choline acetyltransferase from spinal cords of rat RT and mouse: nucleotide sequences, expression in mammalian cells, and in situ RT hybridization."; RL Brain Res. Mol. Brain Res. 7:151-159(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-219. RC TISSUE=Spinal cord; RX PubMed=1400357; DOI=10.1016/s0021-9258(19)88714-8; RA Misawa H., Ishii K., Deguchi T.; RT "Gene expression of mouse choline acetyltransferase. Alternative splicing RT and identification of a highly active promoter region."; RL J. Biol. Chem. 267:20392-20399(1992). 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}. 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; D12487; BAA02056.1; -; mRNA. DR EMBL; D12486; BAA02055.1; -; Genomic_DNA. DR EMBL; D12488; BAA20976.1; -; mRNA. DR EMBL; D12489; BAA20977.1; -; mRNA. DR EMBL; D12490; BAA02057.1; -; mRNA. DR EMBL; D12491; BAA20978.1; -; mRNA. DR EMBL; D12492; BAA20979.1; -; mRNA. DR EMBL; D12493; BAA20980.1; -; mRNA. DR PIR; B43777; B43777. DR AlphaFoldDB; Q03059; -. DR SMR; Q03059; -. DR STRING; 10090.ENSMUSP00000070865; -. DR ChEMBL; CHEMBL5900; -. DR GuidetoPHARMACOLOGY; 2480; -. DR iPTMnet; Q03059; -. DR PhosphoSitePlus; Q03059; -. DR PaxDb; 10090-ENSMUSP00000070865; -. DR ProteomicsDB; 283520; -. DR AGR; MGI:88392; -. DR MGI; MGI:88392; Chat. DR eggNOG; KOG3717; Eukaryota. DR InParanoid; Q03059; -. DR PhylomeDB; Q03059; -. DR BRENDA; 2.3.1.6; 3474. DR Reactome; R-MMU-1483191; Synthesis of PC. DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle. DR ChiTaRS; Sh2d3c; mouse. DR PRO; PR:Q03059; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q03059; Protein. DR GO; GO:0030424; C:axon; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0043005; C:neuron projection; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IDA:MGI. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0033265; F:choline binding; ISO:MGI. DR GO; GO:0004102; F:choline O-acetyltransferase activity; IMP:MGI. DR GO; GO:0008292; P:acetylcholine biosynthetic process; ISO:MGI. DR GO; GO:0007628; P:adult walking behavior; IMP:MGI. DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI. DR GO; GO:0016358; P:dendrite development; IMP:MGI. DR GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; IMP:MGI. DR GO; GO:0007613; P:memory; ISO:MGI. DR GO; GO:0007517; P:muscle organ development; IMP:MGI. DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI. DR GO; GO:0030182; P:neuron differentiation; IMP:MGI. DR GO; GO:0007622; P:rhythmic behavior; IMP:MGI. DR GO; GO:0043179; P:rhythmic excitation; IMP:MGI. 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 2: Evidence at transcript level; KW Acyltransferase; Neurotransmitter biosynthesis; Phosphoprotein; KW Reference proteome; Transferase. FT CHAIN 1..641 FT /note="Choline O-acetyltransferase" FT /id="PRO_0000210155" FT REGION 615..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; 71853 MW; 9BE0010779C8AE6D CRC64; MPILEKVPPK MPVQASSCEE VLDLPKLPVP PLQQTLATYL QCMQHLVPEE QFRKSQAIVK RFGAPGGLGE TLQEKLLERQ EKTANWVSEY WLNDMYLNNR LALPVNSSPA VIFARQHFQD TNDQLRFAAS LISGVLSYKA LLDSQSIPTD WAKGQLSGQP LCMKQYYRLF SSYRLPGHTQ DTLVAQKSSI MPEPEHVIVA CCNQFFVLDV VINFRRLSEG DLFTQLRKIV KMASNEDERL PPIGLLTSDG RSEWAKARTV LLKDSTNRDS LDMIERCICL VCLDGPGTGD LSDTHRALQL LHGGGCSLNG ANRWYDKSLQ FVVGRDGTCG VVCEHSPFDG IVLVQCTEHL LKHMMTGNKK LVRVDSVSEL PAPRRLRWKC SPETQGHLAS SAEKLQRIVK NLDFIVYKFD NYGKTFIKKQ KCSPDGFIQV ALQLAYYRLY QRLVPTYESA SIRRFQEGRV DNIRSATPEA LAFVQAMTDH KAAVLASEKL QLLQRAIQAQ TEYTVMAITG MAIDNHLLAL RELARDLCKE PPEMFMDETY LMSNRFILST SQVPTTMEMF CCYGPVVPNG YGACYNPHAE AITFCISSFH GCKETSSVEF AEAVGASLVD MRDLCSSRQP ADSKPPTAKE RARGPSQAKQ S //