ID   VACHT_TORMA             Reviewed;         511 AA.
AC   Q91498;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Vesicular acetylcholine transporter;
DE            Short=VAChT;
DE   AltName: Full=Vesamicol-binding protein;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Electric lobe;
RX   PubMed=8143858; DOI=10.1016/0014-5793(94)80592-x;
RA   Varoqui H., Diebler M.-F., Meunier F.-M., Rand J.B., Usdin T.B.,
RA   Bonner T.I., Eiden L.E., Erickson J.D.;
RT   "Cloning and expression of the vesamicol binding protein from the marine
RT   ray Torpedo. Homology with the putative vesicular acetylcholine transporter
RT   UNC-17 from Caenorhabditis elegans.";
RL   FEBS Lett. 342:97-102(1994).
CC   -!- FUNCTION: Involved in acetylcholine transport into synaptic vesicles.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: High expression in the electric lobe of the brain.
CC       {ECO:0000269|PubMed:8143858}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC       transporter family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC59647.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U05591; AAC59647.1; ALT_INIT; mRNA.
DR   PIR; S43685; S43685.
DR   AlphaFoldDB; Q91498; -.
DR   SMR; Q91498; -.
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..511
FT                   /note="Vesicular acetylcholine transporter"
FT                   /id="PRO_0000127523"
FT   TOPO_DOM        1..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..108
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..165
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..197
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..225
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..267
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..306
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        328..337
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..363
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        385..400
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..428
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        450..511
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          485..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   511 AA;  55715 MW;  228AB43BF963994C CRC64;
     MAVGQAKAAM GKISSAIGER SKRISGAMNE PRRKRKILLV IVCIAMLLDN MLYMVIVPII
     PNYLETIRTY KLVYITTPSN GTNGSLLNST QRAVLERNPN ANEDIQIGVL FASKAILQLL
     SNPFTGTFID RVGYDIPLLI GLTIMFFSTI TFAFGESYAI LFAARSLQGL GSAFADTSGI
     AMIADKYTEE SERTQALGIA LAFISFGSLV APPFGGVLYQ FAGKWVPFLV LSFVCLLDGI
     LLLMVVTPFA SRTRVNTLQG TPIYKLMIDP YIAVVAGALT TCNIPLAFLE PTISNWMKKT
     MNASEWQMGI TWLPAFFPHI LGVYITVKLA AKYPNYQWLY GAVGLVIIGA SSCTIPACRN
     FEELIIPLCA LCFGIALVDT ALLPTLAFLV DIRYVSVYGS VYAIADISYS VAYALGPIMA
     GQIVHDLGFV QLNLGMGLVN ILYAPGLLFL RNVCQMKPSL SERNILLEEG PKGLYDTIIM
     EERKEAKEPH GTSSGNHSVH AVLSDQEGYS E