VACHT_MOUSE
ID VACHT_MOUSE Reviewed; 530 AA.
AC O35304;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Vesicular acetylcholine transporter;
DE Short=VAChT;
DE AltName: Full=Solute carrier family 18 member 3;
GN Name=Slc18a3; Synonyms=Vacht;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=9427309; DOI=10.1097/00001756-199711100-00011;
RA Naciff J.M., Misawa H., Dedman J.R.;
RT "Molecular characterization of the mouse vesicular acetylcholine
RT transporter gene.";
RL NeuroReport 8:3467-3473(1997).
RN [2]
RP INTERACTION WITH SEC14L1, AND REGION.
RX PubMed=17092608; DOI=10.1016/j.neuint.2006.09.010;
RA Ribeiro F.M., Ferreira L.T., Marion S., Fontes S., Gomez M., Ferguson S.S.,
RA Prado M.A., Prado V.F.;
RT "SEC14-like protein 1 interacts with cholinergic transporters.";
RL Neurochem. Int. 50:356-364(2007).
CC -!- FUNCTION: Involved in acetylcholine transport into synaptic vesicles.
CC {ECO:0000250|UniProtKB:Q16572}.
CC -!- SUBUNIT: Interacts with SEC14L1. {ECO:0000269|PubMed:17092608}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the spinal cord, brain (excluding the
CC cerebellum), brain stem and cholinergic tissues. Not expressed in
CC peripheral tissues such as liver and kidney.
CC {ECO:0000269|PubMed:9427309}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC transporter family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF019045; AAD09151.1; -; Genomic_DNA.
DR CCDS; CCDS79291.1; -.
DR AlphaFoldDB; O35304; -.
DR SMR; O35304; -.
DR STRING; 10090.ENSMUSP00000139829; -.
DR GlyGen; O35304; 2 sites.
DR iPTMnet; O35304; -.
DR PhosphoSitePlus; O35304; -.
DR PRIDE; O35304; -.
DR ProteomicsDB; 297907; -.
DR ABCD; O35304; 2 sequenced antibodies.
DR MGI; MGI:1101061; Slc18a3.
DR eggNOG; KOG3764; Eukaryota.
DR InParanoid; O35304; -.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:O35304; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35304; protein.
DR GO; GO:0030121; C:AP-1 adaptor complex; ISO:MGI.
DR GO; GO:0030122; C:AP-2 adaptor complex; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; IDA:MGI.
DR GO; GO:0005277; F:acetylcholine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0008504; F:monoamine transmembrane transporter activity; TAS:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015870; P:acetylcholine transport; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IDA:SynGO.
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 1: Evidence at protein level;
KW Glycoprotein; Membrane; Neurotransmitter transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..530
FT /note="Vesicular acetylcholine transporter"
FT /id="PRO_0000127519"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..125
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..182
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..242
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..325
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..388
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..447
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 471..530
FT /note="Mediates interaction with SEC14L1"
FT /evidence="ECO:0000269|PubMed:17092608"
FT REGION 504..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 530 AA; 56615 MW; 08526F29B4E8EEDD CRC64;
MEPTAPTGQA RAAATKLSEA VGAALQEPQR QRRLVLVIVC VALLLDNMLY MVIVPIVPDY
IAHMRGGSES PTLISEVWEP TLPPPTLANA SAYLANTSAS PTAAGSARSI LRPRYPTESE
DVKIGVLFAS KAILQLLVNP LSGPFIDRMS YDVPLLIGLG VMFASTVMFA FAEDYATFFA
ARSLQGLGSA FADTSGIAMI ADKYPEEPER SRALGVALAF ISFGSLVAPP FGGILYEFAG
KRVPFLVLAA VSLFDALLLL AVAKPFSAAA RARANLPVGT PIHRLMLDPY IAVVAGALTT
CNIPLAFLEP TIATWMKHTM AASEWEMGMV WLPAFVPHVL GVYLTVRLAA RYPHLQWLYG
ALGLAVIGVS SCVVPACRSF APLVVSLCGL CFGIALVDTA LLPTLAFLVD VRHVSVYGSV
YAIADISYSV AYALGPIVAG HIVHSLGFEQ LSLGMGLANL LYAPVLLLLR NVGLLTRSRS
ERDVLLDEPP QGLYDAVRLR EVQGKDGGEP CSPPGPFDGC EDDYNYYSRS