GLR1_CAEEL
ID GLR1_CAEEL Reviewed; 962 AA.
AC P34299; Q17363;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Glutamate receptor 1 {ECO:0000312|WormBase:C06E1.4};
DE Flags: Precursor;
GN Name=glr-1 {ECO:0000312|WormBase:C06E1.4};
GN ORFNames=C06E1.4 {ECO:0000312|WormBase:C06E1.4};
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=7477293; DOI=10.1038/378078a0;
RA Maricq A.V., Peckol E., Driscoll M., Bargmann C.I.;
RT "Mechanosensory signalling in C. elegans mediated by the GLR-1 glutamate
RT receptor.";
RL Nature 378:78-81(1995).
RN [2]
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 [3]
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=11222641; DOI=10.1523/jneurosci.21-05-01510.2001;
RA Brockie P.J., Madsen D.M., Zheng Y., Mellem J., Maricq A.V.;
RT "Differential expression of glutamate receptor subunits in the nervous
RT system of Caenorhabditis elegans and their regulation by the homeodomain
RT protein UNC-42.";
RL J. Neurosci. 21:1510-1522(2001).
RN [5]
RP SUBCELLULAR LOCATION, UBIQUITINATION, AND MUTAGENESIS OF LYS-888.
RX PubMed=12123612; DOI=10.1016/s0896-6273(02)00749-3;
RA Burbea M., Dreier L., Dittman J.S., Grunwald M.E., Kaplan J.M.;
RT "Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at
RT postsynaptic elements in C. elegans.";
RL Neuron 35:107-120(2002).
RN [6]
RP INTERACTION WITH SOL-1.
RX PubMed=14749834; DOI=10.1038/nature02244;
RA Zheng Y., Mellem J.E., Brockie P.J., Madsen D.M., Maricq A.V.;
RT "SOL-1 is a CUB-domain protein required for GLR-1 glutamate receptor
RT function in C. elegans.";
RL Nature 427:451-457(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=17671168; DOI=10.1091/mbc.e06-09-0818;
RA Juo P., Harbaugh T., Garriga G., Kaplan J.M.;
RT "CDK-5 regulates the abundance of GLR-1 glutamate receptors in the ventral
RT cord of Caenorhabditis elegans.";
RL Mol. Biol. Cell 18:3883-3893(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22252129; DOI=10.1038/emboj.2011.499;
RA Park E.C., Ghose P., Shao Z., Ye Q., Kang L., Xu X.Z., Powell-Coffman J.A.,
RA Rongo C.;
RT "Hypoxia regulates glutamate receptor trafficking through an HIF-
RT independent mechanism.";
RL EMBO J. 31:1379-1393(2012).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=22213799; DOI=10.1083/jcb.201104141;
RA Zhang D., Isack N.R., Glodowski D.R., Liu J., Chen C.C., Xu X.Z.,
RA Grant B.D., Rongo C.;
RT "RAB-6.2 and the retromer regulate glutamate receptor recycling through a
RT retrograde pathway.";
RL J. Cell Biol. 196:85-101(2012).
RN [10]
RP INTERACTION WITH CNI-1, SUBCELLULAR LOCATION, GLYCOSYLATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24094107; DOI=10.1016/j.neuron.2013.07.028;
RA Brockie P.J., Jensen M., Mellem J.E., Jensen E., Yamasaki T., Wang R.,
RA Maxfield D., Thacker C., Hoerndli F., Dunn P.J., Tomita S., Madsen D.M.,
RA Maricq A.V.;
RT "Cornichons control ER export of AMPA receptors to regulate synaptic
RT excitability.";
RL Neuron 80:129-142(2013).
RN [11]
RP INTERACTION WITH USP-46, SUBCELLULAR LOCATION, AND DEUBIQUITINATION BY
RP USP46.
RX PubMed=24356955; DOI=10.1074/jbc.m113.507541;
RA Dahlberg C.L., Juo P.;
RT "The WD40-repeat proteins WDR-20 and WDR-48 bind and activate the
RT deubiquitinating enzyme USP-46 to promote the abundance of the glutamate
RT receptor GLR-1 in the ventral nerve cord of Caenorhabditis elegans.";
RL J. Biol. Chem. 289:3444-3456(2014).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27223098; DOI=10.1371/journal.pgen.1006050;
RA Campbell J.C., Polan-Couillard L.F., Chin-Sang I.D., Bendena W.G.;
RT "NPR-9, a galanin-like G-protein coupled receptor, and GLR-1 regulate
RT interneuronal circuitry underlying multisensory integration of
RT environmental cues in Caenorhabditis elegans.";
RL PLoS Genet. 12:E1006050-E1006050(2016).
CC -!- FUNCTION: Non-NMDA (N-methyl-D-aspartate) ionotropic glutamate receptor
CC (PubMed:7477293). L-glutamate acts as an excitatory neurotransmitter at
CC many synapses in the central nervous system (PubMed:7477293). The
CC postsynaptic actions of glutamate are mediated by a variety of
CC receptors that are named according to their selective agonists
CC (PubMed:7477293). May contribute to a sensory discrimination between
CC mechanical and chemical stimuli (PubMed:7477293). Plays a role in
CC controlling movement in response to environmental cues such as food
CC availability and mechanosensory stimulation such as the nose touch
CC response (PubMed:27223098). In AIB interneurons, promotes omega turns,
CC a movement that frequently follows backwards locomotion or 'reversals'
CC in response to environmental cues while possibly playing an inhibitory
CC role in alternative neurons to inhibit omega turns (PubMed:27223098).
CC {ECO:0000269|PubMed:27223098, ECO:0000269|PubMed:7477293}.
CC -!- SUBUNIT: Interacts with sol-1 (PubMed:14749834). Interacts with cni-1;
CC the interaction negatively regulates export of glr-1 from the
CC endoplasmic reticulum to synapses (PubMed:24094107). Interacts with
CC usp-46; the interaction results in deubiquitination of glr-1
CC (PubMed:24356955). {ECO:0000269|PubMed:14749834,
CC ECO:0000269|PubMed:24094107, ECO:0000269|PubMed:24356955}.
CC -!- INTERACTION:
CC P34299; Q93212: sol-1; NbExp=2; IntAct=EBI-15564936, EBI-15564914;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:12123612, ECO:0000269|PubMed:24356955}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12123612,
CC ECO:0000269|PubMed:24356955}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:24094107}. Synapse {ECO:0000269|PubMed:17671168}.
CC Cell membrane {ECO:0000269|PubMed:17671168,
CC ECO:0000269|PubMed:22252129}. Recycling endosome
CC {ECO:0000269|PubMed:17671168, ECO:0000269|PubMed:22252129}. Cell
CC projection, dendrite {ECO:0000269|PubMed:22213799}. Perikaryon
CC {ECO:0000269|PubMed:22213799}. Note=Partially co-localizes with lin-10
CC at synapses (PubMed:17671168). Trafficking between the plasma membrane
CC and recycling endosomes in the ventral nerve cord is regulated by lin-
CC 10 (PubMed:17671168, PubMed:22252129). During hypoxia, accumulates in
CC enlarged endosome-like compartments (PubMed:22252129). Co-localizes
CC with rab-6.2 at or near punctate structures in the neuron cell body and
CC along the ventral cord dendrites (PubMed:22213799).
CC {ECO:0000269|PubMed:17671168, ECO:0000269|PubMed:22213799,
CC ECO:0000269|PubMed:22252129}.
CC -!- TISSUE SPECIFICITY: Command interneurons of the locomotory control
CC circuit (AIB, AVA, AVB, AVD, AVE and PVC) and motor neurons (RMD, RIM,
CC SMD, AVG, PVQ and URY). {ECO:0000269|PubMed:11222641,
CC ECO:0000269|PubMed:7477293}.
CC -!- PTM: Ubiquitinated. Deubiquitinated by usp-46 which prevents its
CC degradation. {ECO:0000269|PubMed:12123612,
CC ECO:0000269|PubMed:24356955}.
CC -!- PTM: Glycosylated. {ECO:0000303|PubMed:24094107}.
CC -!- DISRUPTION PHENOTYPE: Decreased frequency of reversals, suppression of
CC hyperreversal phenotype of cni-1 mutants, decreased tactile response
CC and increased osmotic avoidance (PubMed:24094107). Overall, display
CC increased omega turn frequency following reversals, however deletion in
CC AIB interneurons specifically results in decreased omega turn frequency
CC (PubMed:27223098). Decreased nose touch responses (PubMed:27223098).
CC {ECO:0000269|PubMed:24094107, ECO:0000269|PubMed:27223098}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
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DR EMBL; U34661; AAA92006.1; -; mRNA.
DR EMBL; BX284603; CCD62564.1; -; Genomic_DNA.
DR PIR; B88533; B88533.
DR PIR; S60225; S60225.
DR RefSeq; NP_498887.2; NM_066486.6.
DR AlphaFoldDB; P34299; -.
DR SMR; P34299; -.
DR BioGRID; 41408; 9.
DR IntAct; P34299; 1.
DR STRING; 6239.C06E1.4; -.
DR TCDB; 1.A.10.1.21; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR iPTMnet; P34299; -.
DR PaxDb; P34299; -.
DR EnsemblMetazoa; C06E1.4.1; C06E1.4.1; WBGene00001612.
DR GeneID; 176204; -.
DR KEGG; cel:CELE_C06E1.4; -.
DR UCSC; C06E1.4; c. elegans.
DR CTD; 176204; -.
DR WormBase; C06E1.4; CE31407; WBGene00001612; glr-1.
DR eggNOG; KOG1054; Eukaryota.
DR GeneTree; ENSGT00940000168258; -.
DR HOGENOM; CLU_007257_1_2_1; -.
DR InParanoid; P34299; -.
DR OMA; AMLVTWH; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P34299; -.
DR Reactome; R-CEL-204005; COPII-mediated vesicle transport.
DR Reactome; R-CEL-399710; Activation of AMPA receptors.
DR Reactome; R-CEL-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-CEL-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-CEL-5694530; Cargo concentration in the ER.
DR PRO; PR:P34299; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001612; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; IPI:WormBase.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0032589; C:neuron projection membrane; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0014069; C:postsynaptic density; IDA:WormBase.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; ISS:WormBase.
DR GO; GO:0019899; F:enzyme binding; IPI:WormBase.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:WormBase.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:UniProtKB.
DR GO; GO:0008306; P:associative learning; IMP:WormBase.
DR GO; GO:0007631; P:feeding behavior; IMP:WormBase.
DR GO; GO:0043056; P:forward locomotion; IMP:UniProtKB.
DR GO; GO:0046959; P:habituation; IMP:WormBase.
DR GO; GO:0006972; P:hyperosmotic response; IMP:UniProtKB.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:WormBase.
DR GO; GO:1905852; P:positive regulation of backward locomotion; IMP:UniProtKB.
DR GO; GO:1905850; P:positive regulation of forward locomotion; IGI:UniProtKB.
DR GO; GO:0043058; P:regulation of backward locomotion; IMP:WormBase.
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:0050913; P:sensory perception of bitter taste; IMP:WormBase.
DR GO; GO:0007614; P:short-term memory; IMP:WormBase.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IDA:WormBase.
DR GO; GO:0001966; P:thigmotaxis; IMP:WormBase.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00062; PBPb; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW Synapse; Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..962
FT /note="Glutamate receptor 1"
FT /id="PRO_0000011590"
FT TOPO_DOM 26..591
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 613..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..855
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..962
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 852
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 888
FT /note="K->R: Increased levels of glr-1."
FT /evidence="ECO:0000269|PubMed:12123612"
SQ SEQUENCE 962 AA; 108142 MW; 25488406566A5583 CRC64;
MFSSFSFLNM FGVLFTVFNL TVVQPYPSHI IIKSFGNNEE VSRVALKAME YTSDHINSRD
DVPFKLAFDH RVVEEGAAVS WNMVNAVCDE LKEGAMALLS SVDGKGREGI RGVSDALEMP
LVSLTALSND DHQQQQFGNL FEVSVRPPIS ELLADFIVHK GWGEVLVLID PVHASLHLPS
LWRHLRTRTN TSVKASMFDL PADEKQFEAY LMQFNMMRNN ETNRILIDCA SPKRLKKLLI
NIRSAQFNQA NYHYVLANYD FLPYDQEMFQ NGNINISGFN IINKDGREYW SLKKHLKTSS
SLGGGDDVSV EAAVGHDAML VTWHGFAKCL QANDSLFHGT FRHRRFFNRG FPGIYCDPLS
DRSHPNRPFS SFEHGKTIGV AFRNMKIGHK EGTLTGNIEF DRFGNRKNFD VSIVDLVSNT
KATFNSKEVL AWRQGVGFFS NRTVAQHSRK SQNDHKDNQV IVLTNLVAPF VMIKRECLEM
ANLTECQGNN KFEGFCIDLL KLLADKIEEF NYEIKLGTKA GSKQADGSWD GMIGELLSGR
AHAVVASLTI NQERERVVDF SKPFMTTGIS IMIKKPDKQE FSVFSFMQPL STEIWMYIIF
AYIGVSVVIF LVSRFSPYEW RVEETSRGGF TISNDFSVYN CLWFTLAAFM QQGTDILPRS
ISGRIASSAW WFFTMIIVSS YTANLAAFLT LEKMQAPIES VEDLAKQSKI KYGIQGGGST
ASFFKYSSVQ IYQRMWRYME SQVPPVFVAS YAEGIERVRS HKGRYAFLLE ATANEYENTR
KPCDTMKVGA NLNSIGYGIA TPFGSDWKDH INLAILALQE RGELKKLENK WWYDRGQCDA
GITVDGSSAS LNLSKVAGIF YILMGGMVIS MLAALGEFLY RSRIEARKSN SNSMVANFAK
NLKSALSSQL RLSVEGGAVA QPGSQSHNAI RRQQVAAFLP ANEKEAFNNV DRPANTLYNT
AV
