CLAT_RAT
ID CLAT_RAT Reviewed; 640 AA.
AC P32738; Q63849; Q64342;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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] OF 1-32.
RC TISSUE=Spinal cord;
RX PubMed=8479291; DOI=10.1016/0169-328x(93)90174-n;
RA Kengaku M., Misawa H., Deguchi T.;
RT "Multiple mRNA species of choline acetyltransferase from rat spinal cord.";
RL Brain Res. Mol. Brain Res. 18:71-76(1993).
RN [3]
RP MUTAGENESIS OF ARG-453.
RX PubMed=7493935; DOI=10.1074/jbc.270.49.29111;
RA Wu D., Hersh L.B.;
RT "Identification of an active site arginine in rat choline acetyltransferase
RT by alanine scanning mutagenesis.";
RL J. Biol. Chem. 270:29111-29116(1995).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-365, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), AND SUBUNIT.
RX PubMed=15477102; DOI=10.1016/j.jsb.2004.06.005;
RA Govindasamy L., Pedersen B., Lian W., Kukar T., Gu Y., Jin S.,
RA Agbandje-McKenna M., Wu D., McKenna R.;
RT "Structural insights and functional implications of choline
RT acetyltransferase.";
RL J. Struct. Biol. 148:226-235(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-634 IN COMPLEX WITH COENZYME A.
RX PubMed=15131697; DOI=10.1038/sj.emboj.7600221;
RA Cai Y., Cronin C.N., Engel A.G., Ohno K., Hersh L.B., Rodgers D.W.;
RT "Choline acetyltransferase structure reveals distribution of mutations that
RT cause motor disorders.";
RL EMBO J. 23:2047-2058(2004).
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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15131697,
CC ECO:0000269|PubMed:15477102}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; M88488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A48319; A48319.
DR PDB; 1Q6X; X-ray; 2.50 A; A/B=1-634.
DR PDB; 1T1U; X-ray; 1.55 A; A=2-640.
DR PDBsum; 1Q6X; -.
DR PDBsum; 1T1U; -.
DR AlphaFoldDB; P32738; -.
DR SMR; P32738; -.
DR STRING; 10116.ENSRNOP00000036251; -.
DR BindingDB; P32738; -.
DR ChEMBL; CHEMBL3945; -.
DR DrugCentral; P32738; -.
DR iPTMnet; P32738; -.
DR PhosphoSitePlus; P32738; -.
DR PaxDb; P32738; -.
DR PRIDE; P32738; -.
DR UCSC; RGD:1304627; rat.
DR RGD; 1304627; Chat.
DR eggNOG; KOG3717; Eukaryota.
DR InParanoid; P32738; -.
DR BRENDA; 2.3.1.6; 5301.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR Reactome; R-RNO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR EvolutionaryTrace; P32738; -.
DR PRO; PR:P32738; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0033265; F:choline binding; IDA:RGD.
DR GO; GO:0004102; F:choline O-acetyltransferase activity; IDA:RGD.
DR GO; GO:0008292; P:acetylcholine biosynthetic process; IDA:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0001547; P:antral ovarian follicle growth; IEP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; ISO:RGD.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0007517; P:muscle organ development; ISO:RGD.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; TAS:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007622; P:rhythmic behavior; ISO:RGD.
DR GO; GO:0043179; P:rhythmic excitation; ISO:RGD.
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 3D-structure; Acyltransferase; Neurotransmitter biosynthesis;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..640
FT /note="Choline O-acetyltransferase"
FT /id="PRO_0000210157"
FT REGION 614..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 412..424
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000305"
FT BINDING 450
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 551
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 453
FT /note="R->A,E,Q: Increases KM for coenzyme A and
FT acetylcholine."
FT /evidence="ECO:0000269|PubMed:7493935"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:1T1U"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 120..143
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1T1U"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1Q6X"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:1T1U"
FT TURN 305..310
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 339..353
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 381..400
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 423..439
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 467..474
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 485..507
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 513..525
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 537..542
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 546..551
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 555..561
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 570..576
FT /evidence="ECO:0007829|PDB:1T1U"
FT STRAND 581..588
FT /evidence="ECO:0007829|PDB:1T1U"
FT HELIX 596..614
FT /evidence="ECO:0007829|PDB:1T1U"
SQ SEQUENCE 640 AA; 71864 MW; E5FEA20EBBFA2EC6 CRC64;
MPILEKAPQK MPVKASSWEE LDLPKLPVPP LQQTLATYLQ CMQHLVPEEQ FRKSQAIVKR
FGAPGGLGET LQEKLLERQE KTANWVSEYW LNDMYLNNRL ALPVNSSPAV IFARQHFQDT
NDQLRFAACL ISGVLSYKTL LDSHSLPTDW AKGQLSGQPL CMKQYYRLFS SYRLPGHTQD
TLVAQKSSIM PEPEHVIVAC CNQFFVLDVV INFRRLSEGD LFTQLRKIVK MASNEDERLP
PIGLLTSDGR SEWAKARTVL LKDSTNRDSL DMIERCICLV CLDGPGTGEL SDTHRALQLL
HGGGCSLNGA NRWYDKSLQF VVGRDGTCGV VCEHSPFDGI VLVQCTEHLL KHMMTSNKKL
VRADSVSELP APRRLRLKCS PETQGHLASS AEKLQRIVKN LDFIVYKFDN YGKTFIKKQK
YSPDGFIQVA LQLAYYRLYQ RLVPTYESAS IRRFQEGRVD NIRSATPEAL AFVQAMTDHK
AAMPASEKLQ LLQTAMQAHK QYTVMAITGM AIDNHLLALR ELARDLCKEP PEMFMDETYL
MSNRFVLSTS QVPTTMEMFC CYGPVVPNGN GACYNPQPEA ITFCISSFHS CKETSSVEFA
EAVGASLVDM RDLCSSRQPA DSKPPAPKEK ARGPSQAKQS
