GRID1_HUMAN
ID GRID1_HUMAN Reviewed; 1009 AA.
AC Q9ULK0; B3KXD5; B7Z7L0; Q8IXT3;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Glutamate receptor ionotropic, delta-1;
DE Short=GluD1;
DE Short=GluR delta-1 subunit;
DE Flags: Precursor;
GN Name=GRID1; Synonyms=KIAA1220;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Caudate nucleus, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-609 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-1009 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULK0-2; Sequence=VSP_057019;
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; AK127168; BAG54447.1; -; mRNA.
DR EMBL; AK302192; BAH13646.1; -; mRNA.
DR EMBL; AC022028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL683834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471142; EAW80340.1; -; Genomic_DNA.
DR EMBL; BC039263; AAH39263.1; -; mRNA.
DR EMBL; AB033046; BAA86534.1; -; mRNA.
DR CCDS; CCDS31236.1; -. [Q9ULK0-1]
DR RefSeq; NP_060021.1; NM_017551.2. [Q9ULK0-1]
DR AlphaFoldDB; Q9ULK0; -.
DR SMR; Q9ULK0; -.
DR BioGRID; 109151; 18.
DR IntAct; Q9ULK0; 4.
DR STRING; 9606.ENSP00000330148; -.
DR ChEMBL; CHEMBL4524129; -.
DR TCDB; 1.A.10.1.34; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; Q9ULK0; 4 sites.
DR iPTMnet; Q9ULK0; -.
DR PhosphoSitePlus; Q9ULK0; -.
DR BioMuta; GRID1; -.
DR DMDM; 38372397; -.
DR jPOST; Q9ULK0; -.
DR MassIVE; Q9ULK0; -.
DR MaxQB; Q9ULK0; -.
DR PaxDb; Q9ULK0; -.
DR PeptideAtlas; Q9ULK0; -.
DR PRIDE; Q9ULK0; -.
DR ProteomicsDB; 6880; -.
DR ProteomicsDB; 85053; -. [Q9ULK0-1]
DR Antibodypedia; 30060; 242 antibodies from 29 providers.
DR DNASU; 2894; -.
DR Ensembl; ENST00000327946.12; ENSP00000330148.7; ENSG00000182771.19. [Q9ULK0-1]
DR GeneID; 2894; -.
DR KEGG; hsa:2894; -.
DR MANE-Select; ENST00000327946.12; ENSP00000330148.7; NM_017551.3; NP_060021.1.
DR UCSC; uc001kdl.2; human. [Q9ULK0-1]
DR CTD; 2894; -.
DR DisGeNET; 2894; -.
DR GeneCards; GRID1; -.
DR HGNC; HGNC:4575; GRID1.
DR HPA; ENSG00000182771; Tissue enhanced (brain).
DR MIM; 610659; gene.
DR neXtProt; NX_Q9ULK0; -.
DR OpenTargets; ENSG00000182771; -.
DR PharmGKB; PA28970; -.
DR VEuPathDB; HostDB:ENSG00000182771; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000155910; -.
DR HOGENOM; CLU_007257_9_0_1; -.
DR InParanoid; Q9ULK0; -.
DR OMA; IMFYDSE; -.
DR PhylomeDB; Q9ULK0; -.
DR TreeFam; TF352434; -.
DR PathwayCommons; Q9ULK0; -.
DR SignaLink; Q9ULK0; -.
DR SIGNOR; Q9ULK0; -.
DR BioGRID-ORCS; 2894; 14 hits in 1078 CRISPR screens.
DR ChiTaRS; GRID1; human.
DR GeneWiki; GRID1; -.
DR GenomeRNAi; 2894; -.
DR Pharos; Q9ULK0; Tbio.
DR PRO; PR:Q9ULK0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9ULK0; protein.
DR Bgee; ENSG00000182771; Expressed in prefrontal cortex and 127 other tissues.
DR ExpressionAtlas; Q9ULK0; baseline and differential.
DR Genevisible; Q9ULK0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; 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_0000011561"
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 930..954
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 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 VAR_SEQ 1..429
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057019"
FT VARIANT 529
FT /note="V -> I (in dbSNP:rs2306265)"
FT /id="VAR_022011"
SQ SEQUENCE 1009 AA; 112131 MW; 201DA12ECC8E1F1A CRC64;
MEALTLWLLP WICQCVSVRA 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 NQKCTRNNHR
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 AQSAAQPRPS
ASATLHSAIW IVYGAFVQQG GESSVNSMAM RIVMGSWWLF TLIVCSSYTA NLAAFLTVSR
MDNPIRTFQD LSKQVEMSYG TVRDSAVYEY FRAKGTNPLE QDSTFAELWR TISKNGGADN
CVSSPSEGIR KAKKGNYAFL WDVAVVEYAA LTDDDCSVTV IGNSISSKGY GIALQHGSPY
RDLFSQRILE LQDTGDLDVL KQKWWPHMGR CDLTSHASAQ ADGKSLKLHS FAGVFCILAI
GLLLACLVAA LELWWNSNRC HQETPKEDKE VNLEQVHRRM NSLMDEDIAH KQISPASIEL
SALEMGGLAP TQTLEPTREY QNTQLSVSTF LPEQSSHGTS RTLSSGPSSN LPLPLSSSAT
MPSMQCKHRS PNGGLFRQSP VKTPIPMSFQ PVPGGVLPEA LDTSHGTSI
