SNF3_CAEEL
ID SNF3_CAEEL Reviewed; 600 AA.
AC G5EBN9;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Sodium- and chloride-dependent betaine transporter {ECO:0000250|UniProtKB:P48065};
DE AltName: Full=Betaine transporter SNF-3 {ECO:0000303|PubMed:24212673};
DE AltName: Full=Na(+)/Cl(-) betaine/GABA transporter {ECO:0000250|UniProtKB:P48065};
DE AltName: Full=Sodium:neurotransmitter symporter family protein 3;
GN Name=snf-3 {ECO:0000312|EMBL:CCD63487.1, ECO:0000312|WormBase:T13B5.1};
GN Synonyms=bgt-1 {ECO:0000312|EMBL:AAZ23105.1}; ORFNames=T13B5.1;
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, ECO:0000312|EMBL:ABF20556.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16641366; DOI=10.1091/mbc.e06-02-0155;
RA Mullen G.P., Mathews E.A., Saxena P., Fields S.D., McManus J.R.,
RA Moulder G., Barstead R.J., Quick M.W., Rand J.B.;
RT "The Caenorhabditis elegans snf-11 gene encodes a sodium-dependent GABA
RT transporter required for clearance of synaptic GABA.";
RL Mol. Biol. Cell 17:3021-3030(2006).
RN [2] {ECO:0000312|EMBL:AAZ23105.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jiang G.-L., Ganapathy V., Fei Y.-J.;
RT "Molecular cloning and functional characteristics of a Na+/Cl--coupled
RT betaine transporter, BGT-1, from Caenorhabditis elegans: Localization in
RT hypodermis and intestine and involvement in osmo-regulation.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:CCD63487.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD63487.1};
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).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:24212673};
RX PubMed=24212673; DOI=10.1038/nn.3575;
RA Peden A.S., Mac P., Fei Y.J., Castro C., Jiang G., Murfitt K.J.,
RA Miska E.A., Griffin J.L., Ganapathy V., Jorgensen E.M.;
RT "Betaine acts on a ligand-gated ion channel in the nervous system of the
RT nematode C. elegans.";
RL Nat. Neurosci. 16:1794-1801(2013).
CC -!- FUNCTION: Betaine transporter dependent on Na(+) and Cl(-) ions that
CC functions primarily in the epidermis to clear betaine from the
CC extracellular space. Elicits current in response to betaine but not in
CC response to GABA, L-carnitine, sarcosine, glycine or dimethylglycine.
CC {ECO:0000269|PubMed:24212673}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24212673};
CC Multi-pass membrane protein {ECO:0000305|PubMed:24212673}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the head, the excretory canal,
CC tail hypodermal cells, epidermis and vulval epithelial cells. Expressed
CC in the excretory canal-associated neuron and in some non-amphidial
CC sensory neurons in the head (at protein level).
CC {ECO:0000269|PubMed:16641366, ECO:0000269|PubMed:24212673}.
CC -!- DISRUPTION PHENOTYPE: Mutant worms are morphologically similar to the
CC wild-type but exhibit mild swimming defects and are lethargic when
CC crawling on a food-free environment with their movement being
CC interrupted by frequent pauses. Worms paralyze in the presence of
CC exogenous betaine. Simultaneous knockdown of snf-3 and egl-8 results in
CC uncoordinated, hypercontracted and paralyzed animals.
CC {ECO:0000269|PubMed:24212673}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC family. {ECO:0000255}.
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DR EMBL; DQ482733; ABF20556.1; -; mRNA.
DR EMBL; DQ118731; AAZ23105.1; -; mRNA.
DR EMBL; FO080410; CCD63487.1; -; Genomic_DNA.
DR PIR; T32456; T32456.
DR RefSeq; NP_493910.2; NM_061509.7.
DR AlphaFoldDB; G5EBN9; -.
DR SMR; G5EBN9; -.
DR BioGRID; 38868; 1.
DR STRING; 6239.T13B5.1; -.
DR EPD; G5EBN9; -.
DR PaxDb; G5EBN9; -.
DR PeptideAtlas; G5EBN9; -.
DR EnsemblMetazoa; T13B5.1.1; T13B5.1.1; WBGene00004902.
DR GeneID; 173493; -.
DR KEGG; cel:CELE_T13B5.1; -.
DR CTD; 173493; -.
DR WormBase; T13B5.1; CE30176; WBGene00004902; snf-3.
DR eggNOG; KOG3660; Eukaryota.
DR HOGENOM; CLU_006855_9_5_1; -.
DR InParanoid; G5EBN9; -.
DR OMA; SNLPMKQ; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; G5EBN9; -.
DR Reactome; R-CEL-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-CEL-442660; Na+/Cl- dependent neurotransmitter transporters.
DR Reactome; R-CEL-71288; Creatine metabolism.
DR Reactome; R-CEL-888593; Reuptake of GABA.
DR PRO; PR:G5EBN9; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004902; Expressed in larva and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0015199; F:amino-acid betaine transmembrane transporter activity; IDA:WormBase.
DR GO; GO:0005332; F:gamma-aminobutyric acid:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0015838; P:amino-acid betaine transport; IDA:WormBase.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
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; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Neurotransmitter transport;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..600
FT /note="Sodium- and chloride-dependent betaine transporter"
FT /id="PRO_0000425865"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 600 AA; 67391 MW; 0B7CF7000FC1FAB9 CRC64;
MGTSEHVPLP TDEAKAKELE QSQHSEEPDR GQWTGKFDFL MSMVAYAVGL GNVWRFPYLC
YKNGGGSFLV VYMIFFCLAA VPIFLMEVTV GQYLQKGAME MWLMCPLFRG VGIGNVVIAF
MCIAYFCVIV AWAMFYMISS IAWVFPWETC NNYWNDATCV TGKENFTELA RIKALVASAG
GHTQTSVEQF WEKRVLHDTG DISEFGGIQW ELFFIMAAAW LIVYFALWKG ITQARKFVYF
CALFPYVLIF ILLIRGLTLE GAGTGIYFYL KPNATRLLDT AVWKDAGTQV FYSYGVGFGA
LIALGSHNKF NHNCFKDAIT MCFINGCTSI TAGFAVFSIL GYMSHVAQKD ISEIVKPGVG
LAFLAYPEVA SNLPMKQVFA VLFFLMITIL GLDSQVCMME GLFTALEDAF PILRKYKKQS
LGIFCLFFFC IGIPMVTHSG SHWLTLFDAY GASGYALLFV VFFEVVGLAY GFGAHNIRKA
LHEMIGVTLP KGIEYVWKFC APATSLVLFV FCVVYYHPVK YPDGKDFPFW ANAFGWFLSS
CSMVVIPGYA IYYLFFTNKH LTLKERVRKG LNLDGSFESP AKKNLVNNAE ELKFIESSSQ
