EAT4_CAEEL
ID EAT4_CAEEL Reviewed; 576 AA.
AC P34644; Q9TZN7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable vesicular glutamate transporter eat-4;
DE AltName: Full=Abnormal pharyngeal pumping eat-4;
GN Name=eat-4 {ECO:0000312|WormBase:ZK512.6a};
GN ORFNames=ZK512.6 {ECO:0000312|WormBase:ZK512.6a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-576, FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=9870947; DOI=10.1523/jneurosci.19-01-00159.1999;
RA Lee R.Y.N., Sawin E.R., Chalfie M., Horvitz H.R., Avery L.;
RT "EAT-4, a homolog of a mammalian sodium-dependent inorganic phosphate
RT cotransporter, is necessary for glutamatergic neurotransmission in
RT caenorhabditis elegans.";
RL J. Neurosci. 19:159-167(1999).
RN [4]
RP FUNCTION.
RX PubMed=9526004; DOI=10.1523/jneurosci.18-08-02871.1998;
RA Berger A.J., Hart A.C., Kaplan J.M.;
RT "G alphas-induced neurodegeneration in Caenorhabditis elegans.";
RL J. Neurosci. 18:2871-2880(1998).
RN [5]
RP FUNCTION.
RX PubMed=10818169; DOI=10.1523/jneurosci.20-11-04337.2000;
RA Rankin C.H., Wicks S.R.;
RT "Mutations of the caenorhabditis elegans brain-specific inorganic phosphate
RT transporter eat-4 affect habituation of the tap-withdrawal response without
RT affecting the response itself.";
RL J. Neurosci. 20:4337-4344(2000).
RN [6]
RP FUNCTION.
RX PubMed=14762140; DOI=10.1523/jneurosci.1569-03.2004;
RA Hills T., Brockie P.J., Maricq A.V.;
RT "Dopamine and glutamate control area-restricted search behavior in
RT Caenorhabditis elegans.";
RL J. Neurosci. 24:1217-1225(2004).
RN [7]
RP FUNCTION.
RX PubMed=15371514; DOI=10.1523/jneurosci.2587-04.2004;
RA Aronoff R., Mellem J.E., Maricq A.V., Sprengel R., Seeburg P.H.;
RT "Neuronal toxicity in Caenorhabditis elegans from an editing site mutant in
RT glutamate receptor channels.";
RL J. Neurosci. 24:8135-8140(2004).
RN [8]
RP FUNCTION.
RX PubMed=14981253; DOI=10.1073/pnas.0306156101;
RA Grunwald M.E., Mellem J.E., Strutz N., Maricq A.V., Kaplan J.M.;
RT "Clathrin-mediated endocytosis is required for compensatory regulation of
RT GLR-1 glutamate receptors after activity blockade.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3190-3195(2004).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17611271; DOI=10.1523/jneurosci.1405-07.2007;
RA Liu T., Kim K., Li C., Barr M.M.;
RT "FMRFamide-like neuropeptides and mechanosensory touch receptor neurons
RT regulate male sexual turning behavior in Caenorhabditis elegans.";
RL J. Neurosci. 27:7174-7182(2007).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25009271; DOI=10.1523/jneurosci.0012-14.2014;
RA Harris G., Shen Y., Ha H., Donato A., Wallis S., Zhang X., Zhang Y.;
RT "Dissecting the signaling mechanisms underlying recognition and preference
RT of food odors.";
RL J. Neurosci. 34:9389-9403(2014).
RN [11]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=28065609; DOI=10.1016/j.cub.2016.11.045;
RA Serrano-Saiz E., Oren-Suissa M., Bayer E.A., Hobert O.;
RT "Sexually Dimorphic Differentiation of a C. elegans Hub Neuron Is Cell
RT Autonomously Controlled by a Conserved Transcription Factor.";
RL Curr. Biol. 27:199-209(2017).
CC -!- FUNCTION: Required for glutamatergic synaptic transmission
CC (PubMed:10818169, PubMed:14762140, PubMed:14981253, PubMed:15371514,
CC PubMed:9526004, PubMed:9870947). In AWB and AWC sensory neurons,
CC required for the detection of preferred food sources, probably via
CC glutamatergic neurotransmission from sensory neurons (PubMed:25009271).
CC Negatively regulates the turning step of male mating behavior
CC (PubMed:17611271). {ECO:0000269|PubMed:10818169,
CC ECO:0000269|PubMed:14762140, ECO:0000269|PubMed:14981253,
CC ECO:0000269|PubMed:15371514, ECO:0000269|PubMed:17611271,
CC ECO:0000269|PubMed:9526004, ECO:0000269|PubMed:9870947}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Synapse.
CC -!- TISSUE SPECIFICITY: Expressed in neurons of the pharynx and the
CC extrapharyngeal nervous system. Highly expressed in male PHC sensory
CC neurons (PubMed:28065609). {ECO:0000269|PubMed:28065609,
CC ECO:0000269|PubMed:9870947}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in male PHC sensory neurons from
CC the late L4 larval stage/young adult stage.
CC {ECO:0000269|PubMed:28065609}.
CC -!- DISRUPTION PHENOTYPE: Defective preference between different food odors
CC (PubMed:25009271). Abnormal repetitive turning behavior during male
CC mating (PubMed:17611271). {ECO:0000269|PubMed:17611271,
CC ECO:0000269|PubMed:25009271}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter family. VGLUT subfamily. {ECO:0000305}.
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DR EMBL; BX284603; CAA80150.1; -; Genomic_DNA.
DR EMBL; AF095787; AAC64972.1; -; mRNA.
DR PIR; H88548; H88548.
DR PIR; S40767; S40767.
DR PIR; T43650; T43650.
DR RefSeq; NP_499023.3; NM_066622.4.
DR AlphaFoldDB; P34644; -.
DR SMR; P34644; -.
DR STRING; 6239.ZK512.6a; -.
DR TCDB; 2.A.1.14.42; the major facilitator superfamily (mfs).
DR PaxDb; P34644; -.
DR PeptideAtlas; P34644; -.
DR EnsemblMetazoa; ZK512.6a.1; ZK512.6a.1; WBGene00001135.
DR GeneID; 176291; -.
DR KEGG; cel:CELE_ZK512.6; -.
DR UCSC; ZK512.6; c. elegans.
DR CTD; 176291; -.
DR WormBase; ZK512.6a; CE01109; WBGene00001135; eat-4.
DR eggNOG; KOG2532; Eukaryota.
DR InParanoid; P34644; -.
DR OMA; YNEQSQM; -.
DR OrthoDB; 497052at2759; -.
DR PhylomeDB; P34644; -.
DR Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-CEL-428643; Organic anion transporters.
DR PRO; PR:P34644; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001135; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; P34644; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060076; C:excitatory synapse; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISS:WormBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; ISS:WormBase.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:UniProtKB.
DR GO; GO:0006820; P:anion transport; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IMP:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISS:WormBase.
DR GO; GO:0061096; P:negative regulation of turning behavior involved in mating; IMP:WormBase.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IBA:GO_Central.
DR GO; GO:1905852; P:positive regulation of backward locomotion; IMP:UniProtKB.
DR GO; GO:1902437; P:positive regulation of male mating behavior; IMP:UniProtKB.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
DR GO; GO:0010035; P:response to inorganic substance; IMP:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:WormBase.
DR Gene3D; 1.20.1250.20; -; 2.
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 Cell membrane; Glycoprotein; Ion transport; Membrane;
KW Neurotransmitter transport; Reference proteome; Sodium; Sodium transport;
KW Symport; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..576
FT /note="Probable vesicular glutamate transporter eat-4"
FT /id="PRO_0000220944"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..344
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..471
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 25..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 576 AA; 63109 MW; 71F3A9EFBE5F84CC CRC64;
MSSWNEAWDR GKQMVGEPLA KMTAAAASAT GAAPPQQMQE EGNENPMQMH SNKVLQVMEQ
TWIGKCRKRW LLAILANMGF MISFGIRCNF GAAKTHMYKN YTDPYGKVHM HEFNWTIDEL
SVMESSYFYG YLVTQIPAGF LAAKFPPNKL FGFGIGVGAF LNILLPYGFK VKSDYLVAFI
QITQGLVQGV CYPAMHGVWR YWAPPMERSK LATTAFTGSY AGAVLGLPLS AFLVSYVSWA
APFYLYGVCG VIWAILWFCV TFEKPAFHPT ISQEEKIFIE DAIGHVSNTH PTIRSIPWKA
IVTSKPVWAI IVANFARSWT FYLLLQNQLT YMKEALGMKI ADSGLLAAIP HLVMGCVVLM
GGQLADYLRS NKILSTTAVR KIFNCGGFGG EAAFMLIVAY TTSDTTAIMA LIAAVGMSGF
AISGFNVNHL DIAPRYAAIL MGFSNGIGTL AGLTCPFVTE AFTAHSKHGW TSVFLLASLI
HFTGVTFYAV YASGELQEWA EPKEEEEWSN KELVNKTGIN GTGYGAAETT FTQLPAGVDS
SYQAQAAPAP GTNPFASAWD EHGSSGVVEN PHYQQW
