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Database: UniProt
Entry: M3YCZ0_MUSPF
LinkDB: M3YCZ0_MUSPF
Original site: M3YCZ0_MUSPF 
ID   M3YCZ0_MUSPF            Unreviewed;       748 AA.
AC   M3YCZ0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Choline O-acetyltransferase {ECO:0000256|ARBA:ARBA00040495};
DE            EC=2.3.1.6 {ECO:0000256|ARBA:ARBA00039091};
GN   Name=CHAT {ECO:0000313|Ensembl:ENSMPUP00000009197.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000009197.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000009197.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-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   EMBL; AEYP01064655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01064656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M3YCZ0; -.
DR   STRING; 9669.ENSMPUP00000009197; -.
DR   Ensembl; ENSMPUT00000009350.1; ENSMPUP00000009197.1; ENSMPUG00000009272.1.
DR   eggNOG; KOG3717; Eukaryota.
DR   GeneTree; ENSGT01060000248556; -.
DR   HOGENOM; CLU_013513_3_0_1; -.
DR   InParanoid; M3YCZ0; -.
DR   OMA; MAMSSYE; -.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          134..713
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        442
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   748 AA;  82874 MW;  434F1B0A3B8F8381 CRC64;
     EDWERERRGG AEGGREKERG EGGGTRGGRS QARPGRRQPV GRPRGPGDVG VSTADRGPHR
     RTADAPSLPA HTPAPSLAWC GGAAANAAEP RRAAKHLSVG SQPGVTTMPI LEKVPQKMAA
     KTPSTEEEPE LPKLPVPPLQ QTLATYLRCM QHLVPEEQFR RSQAIVQRFG APGGLGDTLQ
     QKLLERQKKT ANWVSEYWLN DMYLNNRLAL PVNSSPAVIF ARQHFPDTND QLRFAANLIS
     GVLHYKTLLD SHSIPTDCAK GQLSGQPLCM KQYYGLFSSY RLPGHTQDTL VAQKSSVMPE
     PEHVIVACCN QFFVLDVVIN FRRLSEGDLF TQLRKIVKMA SNEDERLPPI GLLTSEGRSE
     WAEARTVLVK DSTNRDALDM IERCICLVCL DAPAGVELSD TNRALQLLHG GGCSKNGANR
     WYDKSLQFVV GRDGTCGVVC EHSPFDGIVL VQCTEHLLKH MVKSSKKLVR ADSVSELPAP
     RRLRWKCSPE IQGLLASSAE KLQRIVKNLD FIVYKFDIFG KTFIKKQKCS PDAFIQVALQ
     LAFYRLHRRL VATYESASIR RFQEGRVDNI RSATPEALSF VKAVTDHKAA VPDSEKLLLL
     KDAIRAQTEY TVMAITGMAI DNHLLALREL ARDTCKELPE MFTDETYLTS NRFVLSTSQV
     PTTMEMFCCY GPVVPDGYGA CYNPQPENIL FCISSFHGCK ETSSTKFAKA VEESLLEMRD
     LCSPPQSTGG KPLAPQEKAT RPIQGHQP
//
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