SNF5_CAEEL
ID SNF5_CAEEL Reviewed; 728 AA.
AC G5EBM5;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Sodium-dependent transporter snf-5 {ECO:0000305};
DE AltName: Full=Sodium:neurotransmitter symporter family protein 5 {ECO:0000312|WormBase:Y46G5A.30};
GN Name=snf-5 {ECO:0000312|WormBase:Y46G5A.30};
GN ORFNames=Y46G5A.30 {ECO:0000312|WormBase:Y46G5A.30};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAX24101.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jiang G.-L., Fei Y.-J., Ganapathy V.;
RT "Functional identification of snf-5 as a Na+-coupled neutral amino acid
RT transporter in Caenorhabditis elegans.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23580723; DOI=10.1242/jeb.081497;
RA Metzler R., Meleshkevitch E.A., Fox J., Kim H., Boudko D.Y.;
RT "An SLC6 transporter of the novel B(0,)- system aids in absorption and
RT detection of nutrient amino acids in Caenorhabditis elegans.";
RL J. Exp. Biol. 216:2843-2857(2013).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30560135; DOI=10.3389/fmolb.2018.00109;
RA Spanier B., Wallwitz J., Zapoglou D., Idrissou B.M.G., Fischer C.,
RA Troll M., Petzold K., Daniel H.;
RT "The Reproduction Rate of Peptide Transporter PEPT-1 Deficient C. elegans
RT Is Dependent on Dietary Glutamate Supply.";
RL Front. Mol. Biosci. 5:109-109(2018).
CC -!- FUNCTION: Sodium-dependent amino acid transporter that mediates the
CC uptake of the L-enantiomers of various amino acids, including L-proline
CC and L-methionine, and also of acidic amino acids such as L-glutamic
CC acid and L-aspartic acid (PubMed:23580723) (Probable). May additionally
CC have a role in potassium-dependent amino acid absorption
CC (PubMed:23580723). In response to the availability of amino acid
CC nutrients, may play a role in dauer formation (PubMed:23580723). May
CC play a role in promoting fertility (PubMed:30560135).
CC {ECO:0000269|PubMed:23580723, ECO:0000269|PubMed:30560135,
CC ECO:0000305|PubMed:30560135}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23580723};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the INT-9 cells and posterior cells of
CC the alimentary canal of the intestine, gut epithelial cells, the
CC pharynx of some worms, two cells of the rectal gland, and in DVA, DVB
CC and DVC neurons and amphid sensory neurons ASI, ADF and ASK neurons.
CC {ECO:0000269|PubMed:23580723}.
CC -!- DISRUPTION PHENOTYPE: Impaired capacity to form and maintain dauer
CC larvae upon starvation (PubMed:23580723). RNAi-mediated knockdown in a
CC pept-1 (lg601) mutant background results in a reduced number of progeny
CC (PubMed:30560135). Dietary supplementation with glutamate does not
CC rescue this phenotype (PubMed:30560135). {ECO:0000269|PubMed:23580723,
CC ECO:0000269|PubMed:30560135}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. {ECO:0000255|RuleBase:RU003732}.
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DR EMBL; AY825249; AAX24101.1; -; mRNA.
DR EMBL; BX284602; CAB60372.4; -; Genomic_DNA.
DR RefSeq; NP_496735.1; NM_064334.4.
DR AlphaFoldDB; G5EBM5; -.
DR SMR; G5EBM5; -.
DR STRING; 6239.Y46G5A.30; -.
DR EPD; G5EBM5; -.
DR PaxDb; G5EBM5; -.
DR EnsemblMetazoa; Y46G5A.30.1; Y46G5A.30.1; WBGene00004904.
DR GeneID; 174923; -.
DR KEGG; cel:CELE_Y46G5A.30; -.
DR CTD; 174923; -.
DR WormBase; Y46G5A.30; CE29609; WBGene00004904; snf-5.
DR eggNOG; KOG3660; Eukaryota.
DR GeneTree; ENSGT00970000196103; -.
DR HOGENOM; CLU_006855_9_5_1; -.
DR InParanoid; G5EBM5; -.
DR OMA; VSWISIY; -.
DR OrthoDB; 607084at2759; -.
DR PhylomeDB; G5EBM5; -.
DR Reactome; R-CEL-442660; Na+/Cl- dependent neurotransmitter transporters.
DR Reactome; R-CEL-71288; Creatine metabolism.
DR PRO; PR:G5EBM5; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004904; Expressed in adult organism and 1 other tissue.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; 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; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Sodium; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..728
FT /note="Sodium-dependent transporter snf-5"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438855"
FT TOPO_DOM 1..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 85..105
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..119
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 120..140
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 163..183
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..285
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 286..306
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 315..335
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..364
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 365..386
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 397..417
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..451
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 452..472
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 496..516
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..531
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 532..552
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 579..599
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..616
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 617..637
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..728
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 99
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 100
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 104
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 372
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 469
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 204..214
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
SQ SEQUENCE 728 AA; 81692 MW; 09BE422B2D203436 CRC64;
MADSGSNEEA MKRQAPSVKF DSPSKPDPQQ VSQQSNQLSS QKSIQQSTQS KIDPSRIDTK
NTTVTTTRPT LDTPPEEEEE KRDGFGNSFE FVLTSLGLAV GLGNIWRFPT RAYNNGGSAF
LIPYLTCAFL FGLPAVYFEF LTGQYQGKSP PVIFRRVRPI LEGVGWMGVF VAALVAIYYI
VIVSWISIYM INICRGHFAL WSHCNNDWNN GTSCITMADQ YLCKNHTKVM ANSTLWNSSL
PIPDKMVYFN GACQDANGTD VSTATEQYFM TYIVQPSSGM LDFGGFNWPV FAAMSVCWLL
TGLGILKGAK IMGKISYVSV LVPYVLVVVL FINGVFQDGS GVGLEMYFGT PNYTKLYEQD
TWTEALKQLC FSLSVGHGGL ISLSSYSPKR NNIFRDALIV IIGDTTMSLV GGGAVFATLG
YLAKATGQDV KDVVKSGLSL AFVVYPEAMT RMPVPWLWCF IFFLMLFLLG ASTEIALVDV
FCSCIYDQYP RFRNRKWIVV IAWCSVLYCI GLVFSTRAGY YWFEMFDEYA AGFSSVCTVV
CELLVMMYIY GFRNVRDDIT EVVGHARNKF TGAIGAHSWY FTANWMVISP SIALILVGLS
FVREYPYMGR HDIYPAVFDI FGWFLSFLPV IIVPIFMLLN FIRCRNRGHS YRTLFMLQKQ
HASYRRIAAN YSKDQLALQD QLPDKEPWDE ENVDLTDSES ESRNAASGDV PIDDVATIDT
SSTYHQVY
