GRID1_MOUSE
ID GRID1_MOUSE Reviewed; 1009 AA.
AC Q61627; Q3UUL5;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Glutamate receptor ionotropic, delta-1;
DE Short=GluD1;
DE Short=GluR delta-1 subunit;
DE Flags: Precursor;
GN Name=Grid1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Forebrain;
RX PubMed=1372507; DOI=10.1016/0006-291x(92)90566-4;
RA Yamazaki M., Araki K., Shibata A., Mishina M.;
RT "Molecular cloning of a cDNA encoding a novel member of the mouse glutamate
RT receptor channel family.";
RL Biochem. Biophys. Res. Commun. 183:886-892(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH CBLN1 AND CBLN2.
RX PubMed=22220752; DOI=10.1111/j.1471-4159.2012.07648.x;
RA Wei P., Pattarini R., Rong Y., Guo H., Bansal P.K., Kusnoor S.V.,
RA Deutch A.Y., Parris J., Morgan J.I.;
RT "The Cbln family of proteins interact with multiple signaling pathways.";
RL J. Neurochem. 121:717-729(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-436, DISULFIDE BONDS,
RP INTERACTION WITH CBLN1, MUTAGENESIS OF PHE-73, SUBUNIT, SITE, AND REGION.
RX PubMed=27418511; DOI=10.1126/science.aae0104;
RA Elegheert J., Kakegawa W., Clay J.E., Shanks N.F., Behiels E., Matsuda K.,
RA Kohda K., Miura E., Rossmann M., Mitakidis N., Motohashi J., Chang V.T.,
RA Siebold C., Greger I.H., Nakagawa T., Yuzaki M., Aricescu A.R.;
RT "Structural basis for integration of GluD receptors within synaptic
RT organizer complexes.";
RL Science 353:295-299(2016).
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 (PubMed:27418511). Interacts (via extracellular N-
CC terminal domain) with CBLN1 (via C1q domain), and more weakly with
CC CBLN2 (PubMed:22220752, PubMed:27418511). {ECO:0000269|PubMed:22220752,
CC ECO:0000269|PubMed:27418511}.
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: Equally in forebrain and cerebellum.
CC {ECO:0000269|PubMed:1372507}.
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; D10171; BAA01041.1; -; mRNA.
DR EMBL; AK138279; BAE23610.1; -; mRNA.
DR EMBL; AC114572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC169510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT030647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466573; EDL24889.1; -; Genomic_DNA.
DR CCDS; CCDS26944.1; -.
DR PIR; JH0266; JH0266.
DR RefSeq; NP_032192.2; NM_008166.2.
DR PDB; 5KC9; X-ray; 2.30 A; A/B/C=21-436.
DR PDBsum; 5KC9; -.
DR AlphaFoldDB; Q61627; -.
DR SMR; Q61627; -.
DR BioGRID; 200061; 2.
DR IntAct; Q61627; 1.
DR MINT; Q61627; -.
DR STRING; 10090.ENSMUSP00000044009; -.
DR GlyConnect; 2345; 2 N-Linked glycans (2 sites).
DR GlyGen; Q61627; 4 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q61627; -.
DR PhosphoSitePlus; Q61627; -.
DR MaxQB; Q61627; -.
DR PaxDb; Q61627; -.
DR PeptideAtlas; Q61627; -.
DR PRIDE; Q61627; -.
DR ProteomicsDB; 271164; -.
DR Antibodypedia; 30060; 242 antibodies from 29 providers.
DR DNASU; 14803; -.
DR Ensembl; ENSMUST00000043349; ENSMUSP00000044009; ENSMUSG00000041078.
DR GeneID; 14803; -.
DR KEGG; mmu:14803; -.
DR UCSC; uc007tbj.1; mouse.
DR CTD; 2894; -.
DR MGI; MGI:95812; Grid1.
DR VEuPathDB; HostDB:ENSMUSG00000041078; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000155910; -.
DR HOGENOM; CLU_007257_9_0_1; -.
DR InParanoid; Q61627; -.
DR OMA; IMFYDSE; -.
DR OrthoDB; 122304at2759; -.
DR PhylomeDB; Q61627; -.
DR TreeFam; TF352434; -.
DR BioGRID-ORCS; 14803; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Grid1; mouse.
DR PRO; PR:Q61627; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q61627; protein.
DR Bgee; ENSMUSG00000041078; Expressed in CA1 field of hippocampus and 94 other tissues.
DR Genevisible; Q61627; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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; IMP:UniProtKB.
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_0000011562"
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:0000269|PubMed:27418511"
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:0000269|PubMed:27418511"
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 DISULFID 80..351
FT /evidence="ECO:0000269|PubMed:27418511,
FT ECO:0007744|PDB:5KC9"
FT DISULFID 96..128
FT /evidence="ECO:0000269|PubMed:27418511,
FT ECO:0007744|PDB:5KC9"
FT DISULFID 294..306
FT /evidence="ECO:0000269|PubMed:27418511,
FT ECO:0007744|PDB:5KC9"
FT MUTAGEN 73
FT /note="F->D: Abolishes dimerization. Weakly interacts with
FT C1q domain of CBLN1."
FT /evidence="ECO:0000269|PubMed:27418511"
FT CONFLICT 178
FT /note="L -> F (in Ref. 1; BAA01041)"
FT /evidence="ECO:0000305"
FT STRAND 23..33
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 35..51
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:5KC9"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:5KC9"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:5KC9"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 318..339
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:5KC9"
FT HELIX 362..370
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 393..402
FT /evidence="ECO:0007829|PDB:5KC9"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 406..416
FT /evidence="ECO:0007829|PDB:5KC9"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:5KC9"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:5KC9"
SQ SEQUENCE 1009 AA; 112210 MW; 143243A1E3EBD660 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
MDNPIRTFQD LSKQLEMSYG TVRDSAVYEY FRAKGTNPLE QDSTFAELWR TISKNGGADN
CVSNPSEGIR KAKKGNYAFL WDVAVVEYAA LTDDDCSVTV IGNSISSKGY GIALQHGSPY
RDLFSQRILE LQDTGDLDVL KQKWWPHTGR CDLTSHSSTQ TEGKSLKLHS FAGVFCILAI
GLLLACLVAA LELWWNSNRC HQETPKEDKE VNLEQVHRRI NSLMDEDIAH KQISPASIEL
SALEMGGLAP SQALEPTREY QNTQLSVSTF LPEQSSHGTS RTLSSGPSSN LPLPLSSSAT
MPSIQCKHRS PNGGLFRQSP VKTPIPMSFQ PVPGGVLPEA LDTSHGTSI
