GLR3_CAEEL
ID GLR3_CAEEL Reviewed; 836 AA.
AC Q21415; Q9BK23;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Glutamate receptor ionotropic, kainate glr-3 {ECO:0000305};
DE Flags: Precursor;
GN Name=glr-3 {ECO:0000312|WormBase:K10D3.1};
GN ORFNames=K10D3.1 {ECO:0000312|WormBase:K10D3.1};
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|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 [2] {ECO:0000312|EMBL:AAK01095.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 405-802, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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 [3] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF PRO-121; PRO-130; MET-582 AND GLN-584.
RX PubMed=31474366; DOI=10.1016/j.cell.2019.07.034;
RA Gong J., Liu J., Ronan E.A., He F., Cai W., Fatima M., Zhang W., Lee H.,
RA Li Z., Kim G.H., Pipe K.P., Duan B., Liu J., Xu X.Z.S.;
RT "A Cold-Sensing Receptor Encoded by a Glutamate Receptor Gene.";
RL Cell 178:1375-1386.e11(2019).
CC -!- FUNCTION: Ionotropic glutamate receptor (By similarity). Activation by
CC glutamate requires additional verification (PubMed:31474366). L-
CC glutamate acts as an excitatory neurotransmitter at many synapses in
CC the central nervous system. Binding of the excitatory neurotransmitter
CC L-glutamate induces a conformation change, leading to the opening of
CC the cation channel, and thereby converts the chemical signal to an
CC electrical impulse. The receptor then desensitizes rapidly and enters a
CC transient inactive state, characterized by the presence of bound
CC agonist (By similarity). {ECO:0000250|UniProtKB:P39087,
CC ECO:0000269|PubMed:31474366}.
CC -!- FUNCTION: Independent of its ionotropic glutamate receptor activity,
CC acts as a thermoreceptor in the ASER neuron where it triggers a calcium
CC response to activate cold avoidance behavior in response to
CC temperatures below 19 degrees Celsius (PubMed:31474366). Possibly
CC functions as a metabotropic cold receptor and acts upstream of the G(o)
CC G protein goa-1 in the ASER neuron (PubMed:31474366). Also functions in
CC cold sensing in the intestine (PubMed:31474366).
CC {ECO:0000269|PubMed:31474366}.
CC -!- ACTIVITY REGULATION: Activated by low temperature of 18 degrees Celsius
CC in ASER neuron. {ECO:0000269|PubMed:31474366}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P42260};
CC Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P42260}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestine and in the ASER neuron
CC (PubMed:31474366). Also expressed in the thermosensitive RIA
CC interneuron (PubMed:11222641). {ECO:0000269|PubMed:11222641,
CC ECO:0000269|PubMed:31474366}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, expressed just before
CC hatching at low levels. {ECO:0000269|PubMed:11222641}.
CC -!- DISRUPTION PHENOTYPE: Abolishes signal transduction during cold
CC signaling in intestine and ASER neuron. {ECO:0000269|PubMed:31474366}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000255}.
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DR EMBL; BX284601; CAA99883.3; -; Genomic_DNA.
DR EMBL; AF318607; AAK01095.1; -; mRNA.
DR PIR; T23570; T23570.
DR RefSeq; NP_492017.3; NM_059616.3.
DR AlphaFoldDB; Q21415; -.
DR SMR; Q21415; -.
DR STRING; 6239.K10D3.1; -.
DR PaxDb; Q21415; -.
DR EnsemblMetazoa; K10D3.1.1; K10D3.1.1; WBGene00001614.
DR GeneID; 172449; -.
DR KEGG; cel:CELE_K10D3.1; -.
DR UCSC; K10D3.1; c. elegans.
DR CTD; 172449; -.
DR WormBase; K10D3.1; CE36553; WBGene00001614; glr-3.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000167320; -.
DR HOGENOM; CLU_007257_1_1_1; -.
DR InParanoid; Q21415; -.
DR OMA; CKEMRGF; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q21415; -.
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:Q21415; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001614; Expressed in pharyngeal muscle cell (C elegans) and 1 other tissue.
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; IBA:GO_Central.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
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 GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0120169; P:detection of cold stimulus involved in thermoception; IDA:UniProtKB.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; 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 Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Sensory transduction; Signal; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..836
FT /note="Glutamate receptor ionotropic, kainate glr-3"
FT /evidence="ECO:0000255"
FT /id="PRO_5004199558"
FT TOPO_DOM 20..523
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 622..780
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 781..801
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 802..836
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 478..480
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 485
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 651..652
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 699
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT CARBOHYD 225
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 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 76..320
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT MUTAGEN 121
FT /note="P->L: In xu261; abolishes cold receptor function.
FT Decreases signal transduction during cold thermoreception
FT signaling in intestine and ASER neuron."
FT /evidence="ECO:0000269|PubMed:31474366"
FT MUTAGEN 130
FT /note="P->L: Abolishes cold receptor function."
FT /evidence="ECO:0000269|PubMed:31474366"
FT MUTAGEN 582
FT /note="M->R: Normal cold receptor function."
FT /evidence="ECO:0000269|PubMed:31474366"
FT MUTAGEN 584
FT /note="Q->R: Normal cold receptor function."
FT /evidence="ECO:0000269|PubMed:31474366"
SQ SEQUENCE 836 AA; 94921 MW; D9DDF4661D0D3F3D CRC64;
MFWIAKTLIA FLILLKTDCY KIAIPANLID EVNPVLEFVD FRVQVIPYET KPLWRIKQES
FKIVGISIEN GLFSVCNCLI LGASAIILPE QYDGHLAAAA IVQSIADNTN VPCVSLHLSP
PTRPSTHLHP HLNAKSLAVA AFIKREKWKD VVVVFEEPDE LLEITDMITA GHFDPDSFSS
QLVRLKHGDD YGNELKHIKN KLDRYRIVIN IPLQKALHFL EQAANMSMCG VLYHYVVMDM
DLVTVDIDSI RGIEDCNITS FGVHDVNSEY IEDIRQEIVH KSSIRLPKKG VPYTTSIWID
TLRLLIRSMK SIQIWDEPRC GSSWKSGSDI KKRFFENPLA GISGDLHWAP SGERSNYTLH
VYRRTLSFQK FAEWSSRTRR IASSEAVVIA NSSEKLTLEG KHLKISVYLE APFVMITSNG
SYEGYCIDLL HKIANILKFT YTIQKVRDNA YGSKESNGKW SGMVGELQRG DADLAVASLT
ISYGRSEVID FTVPYMHLGI SILFKKPRIR DSDWFKFMDP LSTQVWIMTF ASYFVVSVAI
WIIAKISPYE QFERDEDNGQ YKPVDNQFSL RNSFWFTVCS LMQQGSELCP RAASTRLLTG
IWWFFALILI SSYTANLAAV LTTRRMETPI ENADDLAAQT KIKYGTLGRG STMSFFNESK
IETYERMWQL MSSSPGLFVQ SSKEGIARVK SSDYAYLMES SMLEYAVERD CELMQIGGLI
DQKGYGIGLP KGSPYRELIS TAILRLQEKT ELTELKEKWW KDKSVVCEQP KRKDQDDGES
IGGIFIILVV GLVLTAVLVI FELITTRKPS PAQSQVIRHV NVIPSFKLGF FRWNVN
