CLAT_MOUSE
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 03-AUG-2022, entry version 128.
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}.
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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; Q03059; -.
DR PRIDE; Q03059; -.
DR ProteomicsDB; 283520; -.
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; -; 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 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
