GLR2_CAEEL
ID GLR2_CAEEL Reviewed; 977 AA.
AC Q10914; Q86GT2; Q9BK24;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Glutamate receptor 2;
DE Flags: Precursor;
GN Name=glr-2; ORFNames=B0280.12/K04G7.2;
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] (ISOFORM B), AND FUNCTION.
RX PubMed=12467596; DOI=10.1016/s0896-6273(02)01088-7;
RA Mellem J.E., Brockie P.J., Zheng Y., Madsen D.M., Maricq A.V.;
RT "Decoding of polymodal sensory stimuli by postsynaptic glutamate receptors
RT in C. elegans.";
RL Neuron 36:933-944(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 491-920 (ISOFORMS A AND B), AND TISSUE
RP 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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-566, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: L-glutamate acts as an excitatory neurotransmitter at many
CC synapses in the central nervous system. The postsynaptic actions of
CC glutamate are mediated by a variety of receptors that are named
CC according to their selective agonists. Required for response to
CC mechanical and osmotic stimuli. {ECO:0000269|PubMed:12467596}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q10914-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q10914-2; Sequence=VSP_008031;
CC -!- TISSUE SPECIFICITY: Command interneurons of the locomotory control
CC circuit (AIA, AIB, AVA, AVD, AVE, PVC, RIA, RIG and RIR) and motor
CC neurons (AVG, M1, RMDD and RMDV). {ECO:0000269|PubMed:11222641}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF318606; AAK01094.2; -; mRNA.
DR EMBL; FO080148; CCD61608.1; -; Genomic_DNA.
DR EMBL; FO080148; CCD61609.1; -; Genomic_DNA.
DR PIR; T15306; T15306.
DR RefSeq; NP_001021113.1; NM_001025942.1. [Q10914-2]
DR RefSeq; NP_001021114.1; NM_001025943.1. [Q10914-1]
DR AlphaFoldDB; Q10914; -.
DR SMR; Q10914; -.
DR BioGRID; 41211; 3.
DR STRING; 6239.B0280.12b; -.
DR iPTMnet; Q10914; -.
DR PaxDb; Q10914; -.
DR PRIDE; Q10914; -.
DR EnsemblMetazoa; B0280.12a.1; B0280.12a.1; WBGene00001613. [Q10914-2]
DR EnsemblMetazoa; B0280.12b.1; B0280.12b.1; WBGene00001613. [Q10914-1]
DR GeneID; 175999; -.
DR KEGG; cel:CELE_B0280.12; -.
DR UCSC; B0280.12b; c. elegans. [Q10914-1]
DR CTD; 175999; -.
DR WormBase; B0280.12a; CE31400; WBGene00001613; glr-2.
DR WormBase; B0280.12b; CE33547; WBGene00001613; glr-2.
DR eggNOG; KOG1054; Eukaryota.
DR InParanoid; Q10914; -.
DR OMA; RIASSCW; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q10914; -.
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:Q10914; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001613; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
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 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 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; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..977
FT /note="Glutamate receptor 2"
FT /id="PRO_0000011591"
FT TOPO_DOM 20..621
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..898
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 899..919
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 920..977
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 954..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 238..306
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:11222641"
FT /id="VSP_008031"
SQ SEQUENCE 977 AA; 111789 MW; 8D7A373BC70A8A42 CRC64;
MNKNLLVFGF LIFVKIGETS KKFPLRAFVA STDIDNDTAH AIIEMLRLAE MTFNALSDVD
FDVLLGTRDL PPMEMATMMW NLNRIICDEM KLGYMLMLAG TNFKNYGIYE DIANHMKMPL
IDWEPSKSEN IGKTTENNPM IFSVAPSAEQ LLIDYIQYKG WRDVVYIHDG KNADRTLRTM
FSYLHEKSPK YQLFVDNYVA PSDEEMFKEF LNEFHRRIST QHTLKSNDSS EEIDEPIPVN
VIVDLEGSYR TRAFLRALEE SVLVKKEYHY VFSNFDVDET DLSGFHFSLI NITIFRIFDK
NNKKFLKTRA EFHDVYRGGF SNTDSIPTAA AFAHDAILVA GKALQIAMNE HGKGIFDKSF
VRHQLFNRGR KGLYCRPHED QTESRQFETF EHGKKIAEAI KKVVLTDKDG TLTGRIQFDK
VTGKRTNFSA EIVEIKPGVN SLNSIWERFQ WAEGEGFLLG GERYVQEKKK DSSQTRKGIL
PSKPWQLRFN VVTVLVKPFV MLKRRNPGEP ELKGNDRFEG YCIDLLNLLA KNITGFEYDV
FISDGNKYGS RQADGSWDGM IGYLLNETAD VAVAPLTITQ ERERAVDFSK PFMTTGISIM
IKKPEKQEFN IFSFMEPLGM TIWIFTLSSY FGVSLTIFLV SWFSPYEKRI EFKRGEFTVT
NEFTLYNSLW FTLAAFMQQG TDILPRAVSG RIASSCWWFF TLIIVSSYTA NLAAFLTLER
MTPPIESVED LANQNKILYG VNEGGSTAAF FEDSIVPLYK KMWNFMVSTT QKQIELEKQS
ITNSTSNRIF VSSYADGIEK VRTSKGKYAF LLEETTNNYE SGRRPCDTMK VGQNLNTLGY
GIATKIGNPL RVSLNLAILY LSEKGELKKL ENKWWYDRGQ CDTGTSDGGT SSSLNLSKVA
GIFYILLAGM VLSMCTALVE FLFRKNKENR EKERNRMRSS RPLKPGILAS CERAKQKQLQ
NRRTKSEEVS TPRSTLF