GRID1_RAT
ID GRID1_RAT Reviewed; 1009 AA.
AC Q62640; Q63225;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glutamate receptor ionotropic, delta-1;
DE Short=GluD1;
DE Short=GluR delta-1 subunit;
DE Flags: Precursor;
GN Name=Grid1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Boulter J., Pecht G.;
RT "Nucleotide sequence of rat glutamate receptor subunit gene delta1.";
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 83-1009, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8422924; DOI=10.1016/0014-5793(93)81186-4;
RA Lomeli H., Sprengel R., Laurie D., Khr G., Herb A., Seeburg P., Wisden W.;
RT "The rat delta-1 and delta-2 subunits extend the excitatory amino acid
RT receptor family.";
RL FEBS Lett. 315:318-322(1993).
CC -!- FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory
CC neurotransmitter at many synapses in the central nervous system. The
CC postsynaptic actions of Glu are mediated by a variety of receptors that
CC are named according to their selective agonists.
CC -!- SUBUNIT: Dimer. Interacts (via extracellular N-terminal domain) with
CC CBLN1 (via C1q domain), and more weakly with CBLN2.
CC {ECO:0000250|UniProtKB:Q61627}.
CC -!- INTERACTION:
CC Q62640; Q62640: Grid1; NbExp=4; IntAct=EBI-6988856, EBI-6988856;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest in the pyramidal and dentate granule cell
CC layers of the hippocampus. {ECO:0000269|PubMed:8422924}.
CC -!- DEVELOPMENTAL STAGE: Low in adult brain, much higher in younger
CC animals.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRID1 subfamily. {ECO:0000305}.
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DR EMBL; U08255; AAA17828.1; -; mRNA.
DR EMBL; Z17238; CAA78936.1; -; mRNA.
DR RefSeq; NP_077354.1; NM_024378.1.
DR PDB; 6KSP; EM; 8.10 A; A/B/C/D=21-873.
DR PDB; 6KSS; EM; 8.10 A; A/B/C/D=21-873.
DR PDBsum; 6KSP; -.
DR PDBsum; 6KSS; -.
DR AlphaFoldDB; Q62640; -.
DR SMR; Q62640; -.
DR IntAct; Q62640; 1.
DR MINT; Q62640; -.
DR STRING; 10116.ENSRNOP00000031478; -.
DR ChEMBL; CHEMBL1681629; -.
DR GlyGen; Q62640; 5 sites.
DR iPTMnet; Q62640; -.
DR PhosphoSitePlus; Q62640; -.
DR PaxDb; Q62640; -.
DR PRIDE; Q62640; -.
DR Ensembl; ENSRNOT00000079833; ENSRNOP00000073010; ENSRNOG00000055499.
DR GeneID; 79219; -.
DR KEGG; rno:79219; -.
DR UCSC; RGD:68366; rat.
DR CTD; 2894; -.
DR RGD; 68366; Grid1.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000155910; -.
DR InParanoid; Q62640; -.
DR OrthoDB; 122304at2759; -.
DR PhylomeDB; Q62640; -.
DR PRO; PR:Q62640; -.
DR Proteomes; UP000002494; Chromosome 16.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0035176; P:social behavior; ISS:CAFA.
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 3D-structure; Cell membrane; Disulfide bond; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1009
FT /note="Glutamate receptor ionotropic, delta-1"
FT /id="PRO_0000011563"
FT TOPO_DOM 21..562
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..830
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 852..1009
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 21..436
FT /note="Interaction with CBLN1"
FT /evidence="ECO:0000250|UniProtKB:Q61627"
FT REGION 931..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 73
FT /note="Essential for dimerization"
FT /evidence="ECO:0000250|UniProtKB:Q61627"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..351
FT /evidence="ECO:0000250|UniProtKB:Q61627"
FT DISULFID 96..128
FT /evidence="ECO:0000250|UniProtKB:Q61627"
FT DISULFID 294..306
FT /evidence="ECO:0000250|UniProtKB:Q61627"
FT CONFLICT 917
FT /note="T -> S (in Ref. 2; CAA78936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1009 AA; 112125 MW; ACE950B8B335B4E2 CRC64;
MEALTLWLLP WICQCVTVRA DSIIHIGAIF EENAAKDDRV FQLAVSDLSL NDDILQSEKI
TYSIKVIEAN NPFQAVQEAC DLMTQGILAL VTSTGCASAN ALQSLTDAMH IPHLFVQRNP
GGSPRTACHL NPSPDGEAYT LASRPPVRLN DVMLRLVTEL RWQKFVMFYD SEYDIRGLQS
FLDQASRLGL DVSLQKVDKN ISHVFTSLFT TMKTEELNRY RDTLRRAILL LSPQGAHSFI
NEAVETNLAS KDSHWVFVNE EISDPEILDL VHSALGRMTV VRQIFPSAKD NQKCMRNNHR
ISSLLCDPQE GYLQMLQISN LYLYDSVLML ANAFHRKLED RKWHSMASLN CIRKSTKPWN
GGRSMLDTIK KGHITGLTGV MEFREDSSNP YVQFEILGTT YSETFGKDMR KLATWDSEKG
LNGSLQERPM GSRLQGLTLK VVTVLEEPFV MVAENILGQP KRYKGFSIDV LDALAKALGF
KYEIYQAPDG RYGHQLHNTS WNGMIGELIS KRADLAISAI TITPERESVV DFSKRYMDYS
VGILIKKPEE KISIFSLFAP FDFAVWACIA AAIPVVGVLI FVLNRIQAVR SQSATQPRPS
ASATLHSAIW IVYGAFVQQG GESSVNSVAM RIVMGSWWLF TLIVCSSYTA NLAAFLTVSR
MDSPVRTFQD LSKQLEMSYG TVRDSAVYEY FRAKGTNPLE QDSTFAELWR TISKNGGADN
CVSNPSEGIR KAKKGNYAFL WDVAVVEYAA LTDDDCSVTV IGNSISSKGY GIALQHGSPY
RDLFSQRILE LQDTGDLDVL KQKWWPHTGR CDLTSHSSAQ TDGKSLKLHS FAGVFCILAI
GLLLACLVAA LELWWNSNRC HQETPKEDKE VNLEQVHRRI NSLMDEDIAH KQISPASIEL
SALEMGGLAP SQALEPTREY QNTQLSVSTF LPEQSSHGTS RTLSSGPSSN LPLPLSSSAT
MPSIQCKHRS PNGGLFRQSP VKTPIPMSFQ PVPGGVLPEA LDTSHGTSI
