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-NOV-2009, entry version 70.
DE   RecName: Full=Choline O-acetyltransferase;
DE            Short=Choline acetylase;
DE            Short=CHOACTase;
DE            Short=ChAT;
DE            EC=2.3.1.6;
GN   Name=Chat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spinal cord;
RX   MEDLINE=90251122; 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
RT   rat and mouse: nucleotide sequences, expression in mammalian cells,
RT   and in situ 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   MEDLINE=93015919; PubMed=1400357;
RA   Misawa H., Ishii K., Deguchi T.;
RT   "Gene expression of mouse choline acetyltransferase. Alternative
RT   splicing and identification of a highly active promoter region.";
RL   J. Biol. Chem. 267:20392-20399(1992).
CC   -!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine
CC       (ACh) from acetyl CoA and choline at cholinergic synapses.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + choline = CoA + O-acetylcholine.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase
CC       family.
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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   IPI; IPI00224045; -.
DR   PIR; B43777; B43777.
DR   UniGene; Mm.442817; -.
DR   HSSP; P47934; 1NDF.
DR   SMR; Q03059; 24-616.
DR   STRING; Q03059; -.
DR   PhosphoSite; Q03059; -.
DR   PRIDE; Q03059; -.
DR   Ensembl; ENSMUST00000070125; ENSMUSP00000070865; ENSMUSG00000021919; Mus musculus.
DR   MGI; MGI:88392; Chat.
DR   HOVERGEN; Q03059; -.
DR   BRENDA; 2.3.1.6; 244.
DR   ArrayExpress; Q03059; -.
DR   Bgee; Q03059; -.
DR   CleanEx; MM_CHAT; -.
DR   Genevestigator; Q03059; -.
DR   GermOnline; ENSMUSG00000021919; Mus musculus.
DR   GO; GO:0043025; C:cell soma; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004102; F:choline O-acetyltransferase activity; IMP:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0007529; P:establishment of synaptic specificity at ne...; IMP:MGI.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0007622; P:rhythmic behavior; IMP:MGI.
DR   GO; GO:0043179; P:rhythmic excitation; IMP:MGI.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   PANTHER; PTHR22589; Carn_acyl_trans; 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; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    641       Choline O-acetyltransferase.
FT                                /FTId=PRO_0000210155.
FT   REGION      413    425       Coenzyme A binding (By similarity).
FT   ACT_SITE    335    335       Proton acceptor (By similarity).
FT   BINDING     451    451       Coenzyme A (By similarity).
FT   BINDING     552    552       Coenzyme A (By similarity).
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
//