ID GLR1_DROME Reviewed; 991 AA. AC Q03445; B6IDJ5; Q86PC2; Q9VRX9; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 05-JUL-2017, entry version 146. DE RecName: Full=Glutamate receptor 1; DE AltName: Full=Glutamate receptor I; DE Short=dGLUR-I; DE AltName: Full=Kainate-selective glutamate receptor; DE Flags: Precursor; GN Name=GluRIA; Synonyms=Glu-RI; ORFNames=CG8442; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Embryo; RX PubMed=1359540; DOI=10.1073/pnas.89.21.10484; RA Ultsch A., Schuster C.M., Laube B., Schloss P., Schmitt B., Betz H.; RT "Glutamate receptors of Drosophila melanogaster: cloning of a kainate- RT selective subunit expressed in the central nervous system."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10484-10488(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Booth B., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., RA Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., RA Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., RA Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., RA Rubin G.M., Celniker S.E.; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Receptor for glutamate. L-glutamate acts as an CC excitatory neurotransmitter at many synapses in the central CC nervous system. The postsynaptic actions of Glu are mediated by a CC variety of receptors that are named according to their selective CC agonists (By similarity). Forms ligand-gated ion channels which CC are activated by kainate. {ECO:0000250, CC ECO:0000269|PubMed:1359540}. CC -!- SUBUNIT: Homooligomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1359540}; CC Multi-pass membrane protein {ECO:0000269|PubMed:1359540}. Cell CC junction, synapse, postsynaptic cell membrane {ECO:0000250}; CC Multi-pass membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=A; CC IsoId=Q03445-1; Sequence=Displayed; CC Name=2; CC IsoId=Q03445-2; Sequence=VSP_014219; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Central nervous system. CC {ECO:0000269|PubMed:1359540}. CC -!- DEVELOPMENTAL STAGE: No expression is seen in early embryogenesis, CC whereas high expression occurs in late embryos. During larval CC development, expression decreases to undetectable levels in late CC larvae, resumes at the early pupal stage and gradually increases CC in late pupae and early adult flies. High levels of expression CC coincide with major stages of neurogenesis. CC {ECO:0000269|PubMed:1359540}. CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel CC (TC 1.A.10.1) 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; M97192; AAA28575.1; -; mRNA. DR EMBL; AE014296; AAF50652.2; -; Genomic_DNA. DR EMBL; BT003218; AAO24973.1; -; mRNA. DR EMBL; BT050435; ACJ13142.1; -; mRNA. DR PIR; A46421; A46421. DR RefSeq; NP_476855.1; NM_057507.4. [Q03445-1] DR UniGene; Dm.6460; -. DR PDB; 5DT6; X-ray; 1.60 A; A=474-594, A=739-880. DR PDB; 5ICT; X-ray; 1.68 A; A=474-594, A=739-880. DR PDBsum; 5DT6; -. DR PDBsum; 5ICT; -. DR ProteinModelPortal; Q03445; -. DR SMR; Q03445; -. DR IntAct; Q03445; 1. DR STRING; 7227.FBpp0076691; -. DR PaxDb; Q03445; -. DR PRIDE; Q03445; -. DR EnsemblMetazoa; FBtr0076982; FBpp0076691; FBgn0004619. [Q03445-1] DR GeneID; 38742; -. DR KEGG; dme:Dmel_CG8442; -. DR CTD; 38742; -. DR FlyBase; FBgn0004619; GluRIA. DR eggNOG; KOG1054; Eukaryota. DR eggNOG; ENOG410XPSH; LUCA. DR InParanoid; Q03445; -. DR KO; K05313; -. DR OMA; VEFFCRS; -. DR OrthoDB; EOG091G11CB; -. DR PhylomeDB; Q03445; -. DR Reactome; R-DME-204005; COPII (Coat Protein 2) Mediated Vesicle Transport. DR Reactome; R-DME-399710; Activation of AMPA receptors. DR Reactome; R-DME-416993; Trafficking of GluR2-containing AMPA receptors. DR Reactome; R-DME-438066; Unblocking of NMDA receptor, glutamate binding and activation. DR Reactome; R-DME-5694530; Cargo concentration in the ER. DR Reactome; R-DME-8849932; SALM protein interactions at the synapses. DR GenomeRNAi; 38742; -. DR PRO; PR:Q03445; -. DR Proteomes; UP000000803; Chromosome 3L. DR Bgee; FBgn0004619; -. DR Genevisible; Q03445; DM. DR GO; GO:0032281; C:AMPA glutamate receptor complex; IBA:GO_Central. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0008328; C:ionotropic glutamate receptor complex; IC:FlyBase. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004971; F:AMPA glutamate receptor activity; IBA:GO_Central. DR GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro. DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:FlyBase. DR GO; GO:0006812; P:cation transport; IDA:FlyBase. DR InterPro; IPR001828; ANF_lig-bd_rcpt. DR InterPro; IPR019594; Glu/Gly-bd. 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 SMART; SM00918; Lig_chan-Glu_bd; 1. DR SMART; SM00079; PBPe; 1. DR SUPFAM; SSF53822; SSF53822; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Complete proteome; Glycoprotein; Ion channel; Ion transport; KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; KW Receptor; Reference proteome; Signal; Synapse; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 991 Glutamate receptor 1. FT /FTId=PRO_0000011555. FT TOPO_DOM 28 611 Extracellular. {ECO:0000255}. FT TRANSMEM 612 632 Helical. {ECO:0000255}. FT TOPO_DOM 633 710 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 711 731 Helical. {ECO:0000255}. FT TOPO_DOM 732 895 Extracellular. {ECO:0000255}. FT TRANSMEM 896 916 Helical. {ECO:0000255}. FT TOPO_DOM 917 991 Cytoplasmic. {ECO:0000255}. FT COMPBIAS 28 32 Poly-Gln. FT COMPBIAS 367 371 Poly-Ser. FT CARBOHYD 67 67 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 195 195 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 208 208 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 281 281 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 376 376 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 385 385 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 426 426 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 437 437 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 477 477 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 1 265 Missing (in isoform 2). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_014219. FT CONFLICT 61 61 M -> L (in Ref. 1; AAA28575). FT {ECO:0000305}. FT CONFLICT 301 301 S -> N (in Ref. 1; AAA28575). FT {ECO:0000305}. FT CONFLICT 309 316 GQSQSQNA -> AKAKARTQ (in Ref. 1; FT AAA28575). {ECO:0000305}. FT CONFLICT 324 324 A -> P (in Ref. 1; AAA28575). FT {ECO:0000305}. FT CONFLICT 747 747 T -> A (in Ref. 1; AAA28575). FT {ECO:0000305}. FT CONFLICT 759 759 Y -> H (in Ref. 1; AAA28575). FT {ECO:0000305}. FT CONFLICT 916 916 M -> V (in Ref. 1; AAA28575). FT {ECO:0000305}. FT CONFLICT 944 944 A -> G (in Ref. 1; AAA28575). FT {ECO:0000305}. FT STRAND 476 484 {ECO:0000244|PDB:5DT6}. FT TURN 488 490 {ECO:0000244|PDB:5DT6}. FT STRAND 491 493 {ECO:0000244|PDB:5DT6}. FT HELIX 504 507 {ECO:0000244|PDB:5DT6}. FT STRAND 508 510 {ECO:0000244|PDB:5DT6}. FT HELIX 511 523 {ECO:0000244|PDB:5DT6}. FT STRAND 526 531 {ECO:0000244|PDB:5DT6}. FT HELIX 550 556 {ECO:0000244|PDB:5DT6}. FT STRAND 561 563 {ECO:0000244|PDB:5DT6}. FT HELIX 571 574 {ECO:0000244|PDB:5DT6}. FT STRAND 577 579 {ECO:0000244|PDB:5DT6}. FT STRAND 583 586 {ECO:0000244|PDB:5DT6}. FT STRAND 588 593 {ECO:0000244|PDB:5DT6}. FT HELIX 743 746 {ECO:0000244|PDB:5DT6}. FT STRAND 753 755 {ECO:0000244|PDB:5DT6}. FT HELIX 761 768 {ECO:0000244|PDB:5DT6}. FT HELIX 772 783 {ECO:0000244|PDB:5DT6}. FT HELIX 784 787 {ECO:0000244|PDB:5DT6}. FT STRAND 788 791 {ECO:0000244|PDB:5DT6}. FT HELIX 792 801 {ECO:0000244|PDB:5DT6}. FT TURN 802 804 {ECO:0000244|PDB:5DT6}. FT STRAND 806 811 {ECO:0000244|PDB:5DT6}. FT HELIX 812 819 {ECO:0000244|PDB:5DT6}. FT STRAND 826 830 {ECO:0000244|PDB:5DT6}. FT STRAND 836 838 {ECO:0000244|PDB:5DT6}. FT STRAND 841 843 {ECO:0000244|PDB:5DT6}. FT HELIX 849 861 {ECO:0000244|PDB:5DT6}. FT HELIX 864 872 {ECO:0000244|PDB:5DT6}. FT HELIX 874 876 {ECO:0000244|PDB:5DT6}. SQ SEQUENCE 991 AA; 111668 MW; C8917868ABA06F98 CRC64; MHSRLKFLAY LHFICASSIF WPEFSSAQQQ QQTVSLTEKI PLGAIFEQGT DDVQSAFKYA MLNHNLNVSS RRFELQAYVD VINTADAFKL SRLICNQFSR GVYSMLGAVS PDSFDTLHSY SNTFQMPFVT PWFPEKVLAP SSGLLDFAIS MRPDYHQAII DTIQYYGWQS IIYLYDSHDG LLRLQQIYQE LKPGNETFRV QMVKRIANVT MAIEFLHTLE DLGRFSKKRI VLDCPAEMAK EIIVQHVRDI KLGRRTYHYL LSGLVMDNHW PSDVVEFGAI NITGFRIVDS NRRAVRDFHD SRKRLEPSGQ SQSQNAGGPN SLPAISAQAA LMYDAVFVLV EAFNRILRKK PDQFRSNHLQ RRSHGGSSSS SATGTNESSA LLDCNTSKGW VTPWEQGEKI SRVLRKVEID GLSGEIRFDE DGRRINYTLH VVEMSVNSTL QQVAEWRDDA GLLPLHSHNY ASSSRSASAS TGDYDRNHTY IVSSLLEEPY LSLKQYTYGE SLVGNDRFEG YCKDLADMLA AQLGIKYEIR LVQDGNYGAE NQYAPGGWDG MVGELIRKEA DIAISAMTIT AERERVIDFS KPFMTLGISI MIKKPVKQTP GVFSFLNPLS QEIWISVILS YVGVSFVLYF VTRFPPYEWR IVRRPQADST AQQPPGIIGG ATLSEPQAHV PPVPPNEFTM LNSFWYSLAA FMQQGCDITP PSIAGRIAAA VWWFFTIILI SSYTANLAAF LTVERMVAPI KTPEDLTMQT DVNYGTLLYG STWEFFRRSQ IGLHNKMWEY MNANQHHSVH TYDEGIRRVR QSKGKYALLV ESPKNEYVNA RPPCDTMKVG RNIDTKGFGV ATPIGSPLRK RLNEAVLTLK ENGELLRIRN KWWFDKTECN LDQETSTPNE LSLSNVAGIY YILIGGLLLA VIVAIMEFFC RNKTPQLKSP GSNGSAGGVP GMLASSTYQR DSLSDAIMHS QAKLAMQASS EYDERLVGVE LASNVRYQYS M //