ID   VACHT_TETCF             Reviewed;         515 AA.
AC   P81721; Q9PW50;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Vesicular acetylcholine transporter;
DE            Short=VAChT;
DE   AltName: Full=TorVAChT;
OS   Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX   NCBI_TaxID=7787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IMPORTANCE OF CYS RESIDUES.
RX   PubMed=10737633; DOI=10.1046/j.1471-4159.2000.0741739.x;
RA   Keller J.E., Bravo D.T., Parsons S.M.;
RT   "Modification of cysteines reveals linkage to acetylcholine and vesamicol
RT   binding sites in the vesicular acetylcholine transporter of Torpedo
RT   californica.";
RL   J. Neurochem. 74:1739-1748(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 50-410, AND TISSUE SPECIFICITY.
RC   TISSUE=Electric lobe;
RX   PubMed=7938002; DOI=10.1073/pnas.91.22.10620;
RA   Roghani A., Feldman J., Kohan S.A., Shirzadi A., Gundersen C.B., Brecha N.,
RA   Edwards R.H.;
RT   "Molecular cloning of a putative vesicular transporter for acetylcholine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:10620-10624(1994).
CC   -!- FUNCTION: Involved in acetylcholine transport into synaptic vesicles.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Electric lobe. {ECO:0000269|PubMed:7938002}.
CC   -!- DOMAIN: Two classes of cysteines are involved in transport of
CC       acetylcholine. Binding of acetylcholine to VAChT involves one class of
CC       cysteine located at the cytoplasmic N-terminus and binding of vesamicol
CC       involves both. Organomercurial-mediated modification of two cysteine
CC       residues inhibits binding of vesamicol.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC       transporter family. {ECO:0000305}.
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DR   EMBL; AF172824; AAD50292.1; -; mRNA.
DR   AlphaFoldDB; P81721; -.
DR   SMR; P81721; -.
DR   BindingDB; P81721; -.
DR   ChEMBL; CHEMBL3313; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Neurotransmitter transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..515
FT                   /note="Vesicular acetylcholine transporter"
FT                   /id="PRO_0000127522"
FT   TOPO_DOM        1..40
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..112
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..169
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..229
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..310
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        332..341
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..367
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..404
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        426..432
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        433..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        454..515
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          489..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        50
FT                   /note="M -> A (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="V -> I (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="E -> G (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="A -> V (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   515 AA;  56110 MW;  F48BB2E5086FE936 CRC64;
     MGVTMAVGLA KAAMGKISSA IGERSKRISG AMNEPRRKRK ILLVIVCIAM LLDNMLYMVI
     VPIIPNYLET IRTYKLVYIT TPSNGTNGSL LNSTQRAVLE RNPNANEDIQ IGVLFASKAI
     LQLLSNPFTG TFIDRVGYDI PLLIGLTIMF FSTITFAFGE SYAVLFAARS LQGLGSAFAD
     TSGIAMIADK YTEESERTQA LGIALAFISF GSLVAPPFGG VLYQFAGKWV PFLVLSFVCL
     LDGILLLMVV TPFASRTREN MLQGTPIYKL MIDPYIAVVA GALTTCNIPL AFLEPTISNW
     MKKTMNASEW QMGITWLPAF FPHILGVYIT VKLAAKYPNY QWFYGAVGLV IIGASSCTIP
     ACRNFEELII PLCALCFGIA LVDTALLPTL AFLVDIRYVS VYGSVYAIAD ISYSVAYALG
     PIMAGQIVHD LGFVQLNLGM GLVNILYAPA LLFLRNVCQM KPSLSERNIL LEEGPKGLYD
     TIIMEERKAA KEPHGSSSGN HSVHAVLSDQ EGYSE