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Choline O-acetyltransferase (CHOACTase) (ChAT) (Choline acetylase) (EC 2.3.1.6)

 CLAT_MOUSE              Reviewed;         641 AA.
Q03059;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 110.
RecName: Full=Choline O-acetyltransferase;
Short=CHOACTase;
Short=ChAT;
Short=Choline acetylase;
EC=2.3.1.6;
Name=Chat;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE.
TISSUE=Spinal cord;
PubMed=2160042; DOI=10.1016/0169-328X(90)90092-R;
Ishii K., Oda Y., Ichikawa T., Deguchi T.;
"Complementary DNAs for choline acetyltransferase from spinal cords of
rat and mouse: nucleotide sequences, expression in mammalian cells,
and in situ hybridization.";
Brain Res. Mol. Brain Res. 7:151-159(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-219.
TISSUE=Spinal cord;
PubMed=1400357;
Misawa H., Ishii K., Deguchi T.;
"Gene expression of mouse choline acetyltransferase. Alternative
splicing and identification of a highly active promoter region.";
J. Biol. Chem. 267:20392-20399(1992).
-!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine
(ACh) from acetyl CoA and choline at cholinergic synapses.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + choline = CoA + O-acetylcholine.
-!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase
family. {ECO:0000305}.
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EMBL; D12487; BAA02056.1; -; mRNA.
EMBL; D12486; BAA02055.1; -; Genomic_DNA.
EMBL; D12488; BAA20976.1; -; mRNA.
EMBL; D12489; BAA20977.1; -; mRNA.
EMBL; D12490; BAA02057.1; -; mRNA.
EMBL; D12491; BAA20978.1; -; mRNA.
EMBL; D12492; BAA20979.1; -; mRNA.
EMBL; D12493; BAA20980.1; -; mRNA.
PIR; B43777; B43777.
UniGene; Mm.442817; -.
ProteinModelPortal; Q03059; -.
SMR; Q03059; -.
STRING; 10090.ENSMUSP00000070865; -.
ChEMBL; CHEMBL5900; -.
GuidetoPHARMACOLOGY; 2480; -.
iPTMnet; Q03059; -.
PhosphoSitePlus; Q03059; -.
PaxDb; Q03059; -.
PRIDE; Q03059; -.
MGI; MGI:88392; Chat.
eggNOG; KOG3717; Eukaryota.
eggNOG; ENOG410XNZ9; LUCA.
HOVERGEN; HBG107717; -.
InParanoid; Q03059; -.
PhylomeDB; Q03059; -.
PRO; PR:Q03059; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CHAT; -.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0004102; F:choline O-acetyltransferase activity; IMP:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0016358; P:dendrite development; IMP:MGI.
GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; IMP:MGI.
GO; GO:0007517; P:muscle organ development; IMP:MGI.
GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:MGI.
GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0007622; P:rhythmic behavior; IMP:MGI.
GO; GO:0043179; P:rhythmic excitation; IMP:MGI.
InterPro; IPR000542; Carn_acyl_trans.
PANTHER; PTHR22589; PTHR22589; 1.
Pfam; PF00755; Carn_acyltransf; 1.
PROSITE; PS00439; ACYLTRANSF_C_1; 1.
PROSITE; PS00440; ACYLTRANSF_C_2; 1.
2: Evidence at transcript level;
Acyltransferase; Complete proteome; Neurotransmitter biosynthesis;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 641 Choline O-acetyltransferase.
/FTId=PRO_0000210155.
REGION 413 425 Coenzyme A binding. {ECO:0000250}.
ACT_SITE 335 335 Proton acceptor. {ECO:0000250}.
BINDING 451 451 Coenzyme A. {ECO:0000250}.
BINDING 552 552 Coenzyme A. {ECO:0000250}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000250|UniProtKB:P32738}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000250|UniProtKB:P32738}.
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


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