SNF6_CAEEL
ID SNF6_CAEEL Reviewed; 714 AA.
AC O76689; Q49RB2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 5.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Sodium-dependent acetylcholine transporter;
DE AltName: Full=Sodium:neurotransmitter symporter family protein 6;
GN Name=snf-6 {ECO:0000312|WormBase:M01G5.5};
GN ORFNames=M01G5.5 {ECO:0000312|WormBase:M01G5.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH STN-1, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-144 AND
RP 712-THR--ALA-714.
RX PubMed=15318222; DOI=10.1038/nature02798;
RA Kim H., Rogers M.J., Richmond J.E., McIntire S.L.;
RT "SNF-6 is an acetylcholine transporter interacting with the dystrophin
RT complex in Caenorhabditis elegans.";
RL Nature 430:891-896(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Mediates sodium-dependent uptake of acetylcholine at
CC neuromuscular junctions during periods of increased synaptic activity,
CC may also prevent spillover to adjacent synaptic sites. Not involved in
CC the uptake of other neurotransmitters (GABA, glycine, proline and
CC glutamate) and there was also no inhibition of uptake by adding an
CC excess of other candidate substrates (GABA, glycine, taurine, creatine,
CC proline, alanine, carnitine, glutamate and betaine). Required for
CC muscle integrity; altered transport of acetylcholine due to loss of
CC dystrophin-glycoprotein complex (DGC) function results in muscle
CC degeneration. {ECO:0000269|PubMed:15318222}.
CC -!- SUBUNIT: Interacts with stn-1; part of the DGC.
CC {ECO:0000269|PubMed:15318222}.
CC -!- INTERACTION:
CC O76689; Q93646: stn-1; NbExp=2; IntAct=EBI-447522, EBI-447079;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15318222};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15318222}. Postsynaptic
CC cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC Note=The DGC is not necessary to establish snf-6 at the postsynaptic
CC membrane, but it is required for maintenance or stabilization.
CC -!- TISSUE SPECIFICITY: Body wall, and vulval and enteric muscles.
CC {ECO:0000269|PubMed:15318222}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. {ECO:0000305}.
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DR EMBL; AY661556; AAV70493.1; -; mRNA.
DR EMBL; BX284603; CCD73021.2; -; Genomic_DNA.
DR PIR; F88392; F88392.
DR PIR; T33425; T33425.
DR RefSeq; NP_497416.4; NM_065015.4.
DR AlphaFoldDB; O76689; -.
DR BioGRID; 56261; 6.
DR IntAct; O76689; 1.
DR STRING; 6239.M01G5.5; -.
DR TCDB; 2.A.22.2.7; the neurotransmitter:sodium symporter (nss) family.
DR iPTMnet; O76689; -.
DR EPD; O76689; -.
DR PaxDb; O76689; -.
DR PeptideAtlas; O76689; -.
DR EnsemblMetazoa; M01G5.5.1; M01G5.5.1; WBGene00004905.
DR UCSC; M01G5.5; c. elegans.
DR WormBase; M01G5.5; CE54177; WBGene00004905; snf-6.
DR eggNOG; KOG3660; Eukaryota.
DR GeneTree; ENSGT00940000154963; -.
DR HOGENOM; CLU_006855_9_6_1; -.
DR InParanoid; O76689; -.
DR OMA; DIEYPFE; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; O76689; -.
DR PRO; PR:O76689; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004905; Expressed in embryo and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; NAS:UniProtKB.
DR GO; GO:0005277; F:acetylcholine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005328; F:neurotransmitter:sodium symporter activity; NAS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0015870; P:acetylcholine transport; IDA:UniProtKB.
DR GO; GO:0015871; P:choline transport; IDA:UniProtKB.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; NAS:UniProtKB.
DR GO; GO:0001504; P:neurotransmitter uptake; NAS:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Neurotransmitter transport;
KW Postsynaptic cell membrane; Reference proteome; Symport; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..714
FT /note="Sodium-dependent acetylcholine transporter"
FT /id="PRO_0000214816"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..714
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 144
FT /note="G->D: In allele eg114; exaggerated bending of the
FT anterior body and head, and mild hypercontraction. Elevated
FT concentrations of acetylcholine at the NMJ."
FT /evidence="ECO:0000269|PubMed:15318222"
FT MUTAGEN 712..714
FT /note="Missing: Loss of interaction with stn-1."
FT /evidence="ECO:0000269|PubMed:15318222"
SQ SEQUENCE 714 AA; 80429 MW; 13B39595EBF83117 CRC64;
MSVSSNDPEQ RNGRGMASGN NVDMSLYPPF IKQLDAKLPD YTREGDIEYP FEEITGVGDE
NRIRGNWSNK SDYLLAVIGF TAGVGSFWKF PFLVFQHGGA AFLVPYLCML CLASLPMFFM
EMVLGQFSSS AAISVWKVVP LFKGIGFAQV TISGFFAVFF NIISAWTLFY LINSFSFSIP
WSNCANSWSG ENCTLGTRIQ CKEMNGTLLV NGSCIVEHAS SNETTVIPLH DLGSIPSLKY
FHNDVLMLSK GVDDFGTLNW YLGLCVLACW IAVFLCLFQG VKSSGKVVYV AVIVPFIILT
VLLTRLLTLD GSLAAVFYFL TPKWEILMDL HVWGEAAVQA FYSVSCCSGG LFTIASYSRF
HNNIYKDIWL VLIVDVIVSL VGCLLTFSAI GFTCYEFAIS LDKFHIRDGF HLVFVFLAEA
LAGVSVAPLY AGLFFIMILL VVHATQMFVV ETIVSSICDE YPERLRRNRR HVLTTVCALF
ILLSIPFCLS SGLFWMELLT QFVLTWPLVV IAFLECMAIN WVYGVDNMLD NAKWIVGYWP
PCYIFWKILF KFICPMVYLA ILCFLWLDWN SIQYESYQFP YWSILTAWCI ASFPLILIPI
VGIWQFCIAK GTITQKWWRV LYPDDAWGPA MAIHRAEKFP LQIPEARRLL LPPEVEIASS
RGVLQEEMPM SYDYNTSSAA DVRSNRSTGH GATDVRSVAA TNNTIPKFER ETAI
