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Database: UniProt
Entry: H2LRM3_ORYLA
LinkDB: H2LRM3_ORYLA
Original site: H2LRM3_ORYLA 
ID   H2LRM3_ORYLA            Unreviewed;       669 AA.
AC   H2LRM3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Choline O-acetyltransferase {ECO:0000256|ARBA:ARBA00040495};
DE            EC=2.3.1.6 {ECO:0000256|ARBA:ARBA00039091};
GN   Name=chata {ECO:0000313|Ensembl:ENSORLP00000008722.2};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000008722.2, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000008722.2, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000008722.2,
RC   ECO:0000313|Proteomes:UP000001038};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000008722.2}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000008722.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh)
CC       from acetyl CoA and choline at cholinergic synapses.
CC       {ECO:0000256|ARBA:ARBA00037088}.
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         Evidence={ECO:0000256|ARBA:ARBA00036720};
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   AlphaFoldDB; H2LRM3; -.
DR   Ensembl; ENSORLT00000008723.2; ENSORLP00000008722.2; ENSORLG00000006943.2.
DR   eggNOG; KOG3717; Eukaryota.
DR   GeneTree; ENSGT01060000248556; -.
DR   HOGENOM; CLU_013513_3_1_1; -.
DR   TreeFam; TF313836; -.
DR   Proteomes; UP000001038; Chromosome 15.
DR   Bgee; ENSORLG00000006943; Expressed in bone element and 6 other cell types or tissues.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003801};
KW   Neurotransmitter biosynthesis {ECO:0000256|ARBA:ARBA00022979};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          18..593
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          610..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   669 AA;  75290 MW;  70F74A1145B30D9E CRC64;
     SKQTEKAPAS LPIGLPKLPL PDLKDTLDMY LRCVKHLLTE EQFNKTQKIV KQFEAPGGVG
     ELLQSKLVEK REKTANWVFD YWLNDMYLNN RVALPVNSSP VMVFPQQNFR APIDSLKFAA
     HLISGVLEYK ALLDCSHDLP VDCARGQLAG TPLCMEQYHR LFTSHRLPGL EKDTLVALES
     SMMPDPEHMI VACKNQFFVL NVVINFCRLN ERDLLIQLEK IKKMAESGED RLPPVGLLTS
     DGRTEWAEAR SILMRESINR DSLDMIERSM CLVCLDEASG PELSDTTRAM LMLHGGGAAK
     NGGNRWYDKP MQFVVGEDGC CGVVCEHSPF EGIVLVQCTE YLLKYMIGSP SKLVRAASVS
     KLPAPRKLHW KCSPEIQKRI SSSADKLQRL VKNLDMNVHK FCDYGKEFIK KQKMSPDAFI
     QVALQLAYYR CHGRMVSTYE SASTRRFQKG RVDNIRSATP EALAFIRAMT DGKLNSKKMR
     MLREAITAQT NYTVLAISGM AIDNHLLGLR EIAQEMKMEK PEIFKDAAYL ISNHFLLSTS
     QVPTTVEMFC CYGPVVQNGY GVCYNPQSDH IIFSVSSFHE SPETCSAEFV KHLLQGLQDM
     MDLCNECSTD PNTAERRKGP TLEPHSQASQ LEKTLQRESD PTKGKSPAQT NVQIQSQSSA
     KVKKNNEKK
//
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