ID GRIA1_RAT Reviewed; 907 AA. AC P19490; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 2. DT 27-MAR-2024, entry version 221. DE RecName: Full=Glutamate receptor 1; DE Short=GluR-1; DE AltName: Full=AMPA-selective glutamate receptor 1; DE AltName: Full=GluR-A; DE AltName: Full=GluR-K1; DE AltName: Full=Glutamate receptor ionotropic, AMPA 1; DE Short=GluA1; DE Flags: Precursor; GN Name=Gria1; Synonyms=Glur1; 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] (ISOFORM FLOP). RC TISSUE=Forebrain; RX PubMed=2480522; DOI=10.1038/342643a0; RA Hollmann M., O'Shea-Greenfield A., Rogers S.W., Heinemann S.F.; RT "Cloning by functional expression of a member of the glutamate receptor RT family."; RL Nature 342:643-648(1989). RN [2] RP SEQUENCE REVISION. RA Hartley M.; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP). RC TISSUE=Brain; RX PubMed=2166337; DOI=10.1126/science.2166337; RA Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A., RA Sakmann B., Seeburg P.H.; RT "A family of AMPA-selective glutamate receptors."; RL Science 249:556-560(1990). RN [4] RP SEQUENCE REVISION TO 67; 248; 698; 710; 789 AND 893. RA Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A., RA Sakmann B., Seeburg P.H.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP). RX PubMed=2168579; DOI=10.1126/science.2168579; RA Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E.S., RA Maron C., Heinemann S.F.; RT "Molecular cloning and functional expression of glutamate receptor subunit RT genes."; RL Science 249:1033-1037(1990). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), AND VARIANT THR-710. RC TISSUE=Brain; RX PubMed=1699275; DOI=10.1126/science.1699275; RA Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A., RA Koehler M., Takagi T., Sakmann B., Seeburg P.H.; RT "Flip and flop: a cell-specific functional switch in glutamate-operated RT channels of the CNS."; RL Science 249:1580-1585(1990). RN [7] RP PHOSPHORYLATION AT SER-645. RX PubMed=7877986; DOI=10.1073/pnas.92.5.1376; RA Yakel J.L., Vissavajjhala P., Derkach V.A., Brickey D.A., Soderling T.R.; RT "Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory RT phosphorylation site in non-N-methyl-D-aspartate glutamate receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 92:1376-1380(1995). RN [8] RP VARIANT THR-710, AND PHOSPHORYLATION AT SER-710. RX PubMed=8848293; DOI=10.1016/0168-0102(95)00977-9; RA Nakazawa K., Tadakuma T., Nokihara K., Ito M.; RT "Antibody specific for phosphorylated AMPA-type glutamate receptors at RT GluR2 Ser-696."; RL Neurosci. Res. 24:75-86(1995). RN [9] RP PHOSPHORYLATION AT SER-849 AND SER-863, AND MUTAGENESIS OF SER-645 AND RP SER-849. RX PubMed=9405465; DOI=10.1074/jbc.272.51.32528; RA Mammen A.L., Kameyama K., Roche K.W., Huganir R.L.; RT "Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic RT acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II."; RL J. Biol. Chem. 272:32528-32533(1997). RN [10] RP INTERACTION WITH DLG1. RX PubMed=9677374; DOI=10.1074/jbc.273.31.19518; RA Leonard A.S., Davare M.A., Horne M.C., Garner C.C., Hell J.W.; RT "SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4- RT propionic acid receptor GluR1 subunit."; RL J. Biol. Chem. 273:19518-19524(1998). RN [11] RP INTERACTION WITH DLG1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP MUTAGENESIS OF THR-905 AND LEU-907. RX PubMed=12070168; DOI=10.1074/jbc.m204354200; RA Cai C., Coleman S.K., Niemi K., Keinaenen K.; RT "Selective binding of synapse-associated protein 97 to GluR-A alpha-amino- RT 5-hydroxy-3-methyl-4-isoxazole propionate receptor subunit is determined by RT a novel sequence motif."; RL J. Biol. Chem. 277:31484-31490(2002). RN [12] RP INTERACTION WITH PDLIM4, AND SUBCELLULAR LOCATION. RX PubMed=15456832; DOI=10.1523/jneurosci.2100-04.2004; RA Schulz T.W., Nakagawa T., Licznerski P., Pawlak V., Kolleker A., Rozov A., RA Kim J., Dittgen T., Koehr G., Sheng M., Seeburg P.H., Osten P.; RT "Actin/alpha-actinin-dependent transport of AMPA receptors in dendritic RT spines: role of the PDZ-LIM protein RIL."; RL J. Neurosci. 24:8584-8594(2004). RN [13] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH CACNG2. RX PubMed=16793768; DOI=10.1074/jbc.m600679200; RA Bedoukian M.A., Weeks A.M., Partin K.M.; RT "Different domains of the AMPA receptor direct stargazin-mediated RT trafficking and stargazin-mediated modulation of kinetics."; RL J. Biol. Chem. 281:23908-23921(2006). RN [14] RP INTERACTION WITH LRFN1. RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005; RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., RA Kim E.; RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of RT excitatory synapses."; RL Neuron 50:233-245(2006). RN [15] RP INTERACTION WITH PRKG2, PHOSPHORYLATION AT SER-863, AND MUTAGENESIS OF RP ARG-855 AND SER-863. RX PubMed=18031684; DOI=10.1016/j.neuron.2007.09.016; RA Serulle Y., Zhang S., Ninan I., Puzzo D., McCarthy M., Khatri L., RA Arancio O., Ziff E.B.; RT "A GluR1-cGKII interaction regulates AMPA receptor trafficking."; RL Neuron 56:670-688(2007). RN [16] RP INTERACTION WITH CACNG5. RX PubMed=18817736; DOI=10.1016/j.neuron.2008.07.034; RA Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.; RT "AMPA receptor subunit-specific regulation by a distinct family of type II RT TARPs."; RL Neuron 59:986-996(2008). RN [17] RP INTERACTION WITH CACNG5. RX PubMed=19234459; DOI=10.1038/nn.2266; RA Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.; RT "Selective regulation of long-form calcium-permeable AMPA receptors by an RT atypical TARP, gamma-5."; RL Nat. Neurosci. 12:277-285(2009). RN [18] RP ERRATUM OF PUBMED:19234459. RX DOI=10.1038/nn0609-808c; RA Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.; RL Nat. Neurosci. 12:808-808(2009). RN [19] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=19265014; DOI=10.1126/science.1167852; RA Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B., RA Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.; RT "Functional proteomics identify cornichon proteins as auxiliary subunits of RT AMPA receptors."; RL Science 323:1313-1319(2009). RN [20] RP INTERACTION WITH CNIH2 AND CACNG2. RX PubMed=20805473; DOI=10.1073/pnas.1011706107; RA Shi Y., Suh Y.H., Milstein A.D., Isozaki K., Schmid S.M., Roche K.W., RA Nicoll R.A.; RT "Functional comparison of the effects of TARPs and cornichons on AMPA RT receptor trafficking and gating."; RL Proc. Natl. Acad. Sci. U.S.A. 107:16315-16319(2010). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 890-907 IN COMPLEX WITH DLG1, AND RP INTERACTION WITH DLG1. RX PubMed=17069616; DOI=10.1111/j.1742-4658.2006.05521.x; RA von Ossowski I., Oksanen E., von Ossowski L., Cai C., Sundberg M., RA Goldman A., Keinanen K.; RT "Crystal structure of the second PDZ domain of SAP97 in complex with a RT GluR-A C-terminal peptide."; RL FEBS J. 273:5219-5229(2006). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-392, SUBUNIT, GLYCOSYLATION AT RP ASN-63; ASN-249; ASN-257 AND ASN-363, AND DISULFIDE BOND. RX PubMed=21639859; DOI=10.1042/bj20110801; RA Yao G., Zong Y., Gu S., Zhou J., Xu H., Mathews I.I., Jin R.; RT "Crystal structure of the glutamate receptor GluA1 N-terminal domain."; RL Biochem. J. 438:255-263(2011). CC -!- FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an CC excitatory neurotransmitter at many synapses in the central nervous CC system. Binding of the excitatory neurotransmitter L-glutamate induces CC a conformation change, leading to the opening of the cation channel, CC and thereby converts the chemical signal to an electrical impulse. The CC receptor then desensitizes rapidly and enters a transient inactive CC state, characterized by the presence of bound agonist. In the presence CC of CACNG4 or CACNG7 or CACNG8, shows resensitization which is CC characterized by a delayed accumulation of current flux upon continued CC application of glutamate. {ECO:0000269|PubMed:16793768, CC ECO:0000269|PubMed:19265014}. CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate CC receptor subunits (PubMed:21639859). Tetramers may be formed by the CC dimerization of dimers (By similarity). Found in a complex with GRIA2, CC GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CC CACNG8 (PubMed:16793768, PubMed:19265014). Interacts with HIP1 and CC RASGRF2. Interacts with SYNDIG1 and GRIA2 (By similarity). Interacts CC with DLG1 (via C-terminus) (PubMed:12070168, PubMed:17069616, CC PubMed:9677374). Interacts with LRFN1 (PubMed:16630835). Interacts with CC PRKG2 (PubMed:18031684). Interacts with CNIH2 and CACNG2 CC (PubMed:20805473). Interacts with CACNG5 (PubMed:18817736, CC PubMed:19234459). Interacts (via C-terminus) with PDLIM4 (via LIM CC domain); this interaction as well as the interaction of PDLIM4 with CC alpha-actinin is required for their colocalization in early endosomes CC (PubMed:15456832). Interacts with SNX27 (via PDZ domain); the CC interaction is required for recycling to the plasma membrane when CC endocytosed and prevent degradation in lysosomes. Interacts (via PDZ- CC binding motif) with SHANK3 (via PDZ domain) (By similarity). Interacts CC with CACNG3; associates GRIA1 with the adapter protein complex 4 (AP-4) CC to target GRIA1 to the somatodendritic compartment of neurons (By CC similarity). {ECO:0000250|UniProtKB:P23818, CC ECO:0000250|UniProtKB:P42261, ECO:0000269|PubMed:12070168, CC ECO:0000269|PubMed:15456832, ECO:0000269|PubMed:16630835, CC ECO:0000269|PubMed:16793768, ECO:0000269|PubMed:17069616, CC ECO:0000269|PubMed:18031684, ECO:0000269|PubMed:18817736, CC ECO:0000269|PubMed:19234459, ECO:0000269|PubMed:19265014, CC ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:21639859, CC ECO:0000269|PubMed:9677374}. CC -!- INTERACTION: CC P19490; P10608: Adrb2; NbExp=3; IntAct=EBI-371642, EBI-7090342; CC P19490; Q5FVC2: Arhgef2; NbExp=4; IntAct=EBI-371642, EBI-15756732; CC P19490; Q71RJ2: Cacng2; NbExp=7; IntAct=EBI-371642, EBI-8538384; CC P19490; P11275: Camk2a; NbExp=3; IntAct=EBI-371642, EBI-2640645; CC P19490; Q5BJU5: Cnih2; NbExp=3; IntAct=EBI-371642, EBI-15874082; CC P19490; P31016: Dlg4; NbExp=5; IntAct=EBI-371642, EBI-375655; CC P19490; P19490: Gria1; NbExp=2; IntAct=EBI-371642, EBI-371642; CC P19490; P19491: Gria2; NbExp=3; IntAct=EBI-371642, EBI-77718; CC P19490; B2GV74: Klc2; NbExp=2; IntAct=EBI-371642, EBI-978371; CC P19490; P70569: Myo5b; NbExp=2; IntAct=EBI-371642, EBI-975940; CC P19490-2; P19491-2: Gria2; NbExp=2; IntAct=EBI-26900830, EBI-15817825; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23818}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P23818}. Endoplasmic CC reticulum membrane {ECO:0000269|PubMed:15456832}; Multi-pass membrane CC protein {ECO:0000305}. Postsynaptic cell membrane CC {ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P23818}. Postsynaptic density membrane CC {ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein CC {ECO:0000305}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:P23818}. Cell projection, dendritic spine CC {ECO:0000250|UniProtKB:P23818}. Early endosome membrane CC {ECO:0000269|PubMed:15456832}; Multi-pass membrane protein CC {ECO:0000305}. Recycling endosome membrane CC {ECO:0000269|PubMed:15456832}; Multi-pass membrane protein CC {ECO:0000305}. Presynapse {ECO:0000250|UniProtKB:P23818}. Synapse CC {ECO:0000250|UniProtKB:P23818}. Note=Interaction with CACNG2, CNIH2 and CC CNIH3 promotes cell surface expression (PubMed:19265014). Colocalizes CC with PDLIM4 in early endosomes (PubMed:15456832). Displays a CC somatodendritic localization and is excluded from axons in neurons (By CC similarity). Localized to cone photoreceptor pedicles (By similarity). CC {ECO:0000250|UniProtKB:P23818, ECO:0000269|PubMed:15456832, CC ECO:0000269|PubMed:19265014}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Flop; CC IsoId=P19490-1; Sequence=Displayed; CC Name=Flip; CC IsoId=P19490-2; Sequence=VSP_000097, VSP_000098, VSP_000099, CC VSP_000100, VSP_000101; CC -!- TISSUE SPECIFICITY: Detected in cerebellum (at protein level). CC {ECO:0000269|PubMed:12070168}. CC -!- DOMAIN: The M4 transmembrane segment mediates tetramerization and is CC required for cell surface expression. {ECO:0000250|UniProtKB:P42261}. CC -!- PTM: Phosphorylated at Ser-645 (PubMed:7877986). Phosphorylated at Ser- CC 710 by PKC (PubMed:8848293). Phosphorylated at Ser-849 by PKC, PKA and CC CAMK2 (PubMed:9405465). Phosphorylated at Ser-863 by PKC, PKA and PRKG2 CC (PubMed:18031684, PubMed:9405465). Phosphorylation of Ser-863 is CC reduced by induction of long-term depression and increased by induction CC of long-term potentiation (By similarity). CC {ECO:0000250|UniProtKB:P23818, ECO:0000269|PubMed:18031684, CC ECO:0000269|PubMed:7877986, ECO:0000269|PubMed:8848293, CC ECO:0000269|PubMed:9405465}. CC -!- PTM: Palmitoylated. Depalmitoylated by CPT1C and upon glutamate CC stimulation. ZDHHC3/GODZ specifically palmitoylates Cys-603, which CC leads to Golgi retention and decreased cell surface expression (By CC similarity). In contrast, Cys-829 palmitoylation does not affect cell CC surface expression but regulates stimulation-dependent endocytosis (By CC similarity). {ECO:0000250|UniProtKB:P23818, CC ECO:0000250|UniProtKB:P42261}. CC -!- POLYMORPHISM: Both variants Ser-710 and Thr-710 are phosphorylated at CC this position. CC -!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a CC variety of receptors that are named according to their selective CC agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate. CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) CC family. GRIA1 subfamily. {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; X17184; CAA35050.1; -; mRNA. DR EMBL; M36418; AAA41243.2; -; mRNA. DR EMBL; M38060; AAA63479.1; -; mRNA. DR PIR; A40170; A40170. DR PIR; S07059; ACRTK1. DR RefSeq; NP_113796.1; NM_031608.1. [P19490-1] DR PDB; 2AWW; X-ray; 2.21 A; C=890-907. DR PDB; 2G2L; X-ray; 2.35 A; C/D=890-907. DR PDB; 3SAJ; X-ray; 2.50 A; A/B/C/D=22-392. DR PDB; 6NJL; EM; 6.70 A; A/C=1-907. DR PDB; 6NJN; EM; 6.50 A; A=1-907. DR PDB; 6QKC; EM; 4.10 A; A/C=1-907. DR PDB; 6QKZ; EM; 6.30 A; A/C=20-907. DR PDB; 7OCA; EM; 3.40 A; A/C=1-907. DR PDB; 7OCC; EM; 3.40 A; A/C=1-907. DR PDB; 7OCD; EM; 3.50 A; A/C=1-907. DR PDB; 7OCE; EM; 3.10 A; A/C=1-907. DR PDB; 7OCF; EM; 3.60 A; A/C=1-907. DR PDB; 7QHB; EM; 3.50 A; A/C=1-907. DR PDB; 7QHH; EM; 3.60 A; A/C=1-907. DR PDB; 8AYL; EM; 3.20 A; A/C=1-907. DR PDB; 8AYM; EM; 3.30 A; A/C=1-907. DR PDB; 8AYN; EM; 2.80 A; A/C=1-907. DR PDB; 8AYO; EM; 3.30 A; A/C=1-907. DR PDB; 8C1P; EM; 2.90 A; A/B/C/D=1-907. DR PDB; 8C1Q; EM; 2.82 A; A/B/C/D=1-907. DR PDB; 8C2H; EM; 2.64 A; A/B/C/D=1-907. DR PDB; 8C2I; EM; 2.70 A; A/B/C/D=1-907. DR PDB; 8P3T; EM; 3.39 A; A/B/C/D=1-907. DR PDB; 8P3U; EM; 3.77 A; A/B/C/D=1-907. DR PDB; 8P3V; EM; 3.53 A; A/B/C/D=1-907. DR PDB; 8P3W; EM; 3.53 A; A/B/C/D=1-907. DR PDBsum; 2AWW; -. DR PDBsum; 2G2L; -. DR PDBsum; 3SAJ; -. DR PDBsum; 6NJL; -. DR PDBsum; 6NJN; -. DR PDBsum; 6QKC; -. DR PDBsum; 6QKZ; -. DR PDBsum; 7OCA; -. DR PDBsum; 7OCC; -. DR PDBsum; 7OCD; -. DR PDBsum; 7OCE; -. DR PDBsum; 7OCF; -. DR PDBsum; 7QHB; -. DR PDBsum; 7QHH; -. DR PDBsum; 8AYL; -. DR PDBsum; 8AYM; -. DR PDBsum; 8AYN; -. DR PDBsum; 8AYO; -. DR PDBsum; 8C1P; -. DR PDBsum; 8C1Q; -. DR PDBsum; 8C2H; -. DR PDBsum; 8C2I; -. DR PDBsum; 8P3T; -. DR PDBsum; 8P3U; -. DR PDBsum; 8P3V; -. DR PDBsum; 8P3W; -. DR AlphaFoldDB; P19490; -. DR EMDB; EMD-12802; -. DR EMDB; EMD-12803; -. DR EMDB; EMD-12805; -. DR EMDB; EMD-16379; -. DR EMDB; EMD-16380; -. DR EMDB; EMD-16390; -. DR EMDB; EMD-16391; -. DR EMDB; EMD-17394; -. DR EMDB; EMD-17395; -. DR EMDB; EMD-17396; -. DR EMDB; EMD-17397; -. DR EMDB; EMD-4572; -. DR EMDB; EMD-4575; -. DR EMDB; EMD-9387; -. DR EMDB; EMD-9389; -. DR SMR; P19490; -. DR BioGRID; 248399; 15. DR CORUM; P19490; -. DR DIP; DIP-30929N; -. DR ELM; P19490; -. DR IntAct; P19490; 27. DR MINT; P19490; -. DR STRING; 10116.ENSRNOP00000074119; -. DR BindingDB; P19490; -. DR ChEMBL; CHEMBL3753; -. DR DrugCentral; P19490; -. DR TCDB; 1.A.10.1.1; the glutamate-gated ion channel (gic) family of neurotransmitter receptors. DR GlyCosmos; P19490; 6 sites, No reported glycans. DR GlyGen; P19490; 6 sites. DR iPTMnet; P19490; -. DR PhosphoSitePlus; P19490; -. DR SwissPalm; P19490; -. DR PaxDb; 10116-ENSRNOP00000064722; -. DR ABCD; P19490; 2 sequenced antibodies. DR Ensembl; ENSRNOT00000071615.4; ENSRNOP00000064722.3; ENSRNOG00000045816.4. [P19490-1] DR Ensembl; ENSRNOT00000081136.2; ENSRNOP00000074119.2; ENSRNOG00000045816.4. [P19490-2] DR Ensembl; ENSRNOT00055051536; ENSRNOP00055042480; ENSRNOG00055029717. [P19490-1] DR Ensembl; ENSRNOT00060039317; ENSRNOP00060032516; ENSRNOG00060022487. [P19490-1] DR Ensembl; ENSRNOT00065010094; ENSRNOP00065007367; ENSRNOG00065006524. [P19490-1] DR GeneID; 50592; -. DR KEGG; rno:50592; -. DR UCSC; RGD:621531; rat. [P19490-1] DR AGR; RGD:621531; -. DR CTD; 2890; -. DR RGD; 621531; Gria1. DR eggNOG; KOG1054; Eukaryota. DR GeneTree; ENSGT00940000157342; -. DR InParanoid; P19490; -. DR OMA; DSDIQHS; -. DR OrthoDB; 511851at2759; -. DR PhylomeDB; P19490; -. DR Reactome; R-RNO-204005; COPII-mediated vesicle transport. DR Reactome; R-RNO-399710; Activation of AMPA receptors. DR Reactome; R-RNO-399719; Trafficking of AMPA receptors. DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors. DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation. DR Reactome; R-RNO-5694530; Cargo concentration in the ER. DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules. DR EvolutionaryTrace; P19490; -. DR PRO; PR:P19490; -. DR Proteomes; UP000002494; Chromosome 10. DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB. DR GO; GO:0032279; C:asymmetric synapse; IDA:RGD. DR GO; GO:0044308; C:axonal spine; ISO:RGD. DR GO; GO:0044297; C:cell body; ISO:RGD. DR GO; GO:0009986; C:cell surface; IDA:RGD. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL. DR GO; GO:0032590; C:dendrite membrane; IDA:RGD. DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB. DR GO; GO:0043197; C:dendritic spine; IDA:ARUK-UCL. DR GO; GO:0032591; C:dendritic spine membrane; ISO:RGD. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0008328; C:ionotropic glutamate receptor complex; ISO:RGD. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD. DR GO; GO:0043005; C:neuron projection; ISO:RGD. DR GO; GO:0044309; C:neuron spine; IDA:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB. DR GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD. DR GO; GO:0099544; C:perisynaptic space; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0098794; C:postsynapse; ISO:RGD. DR GO; GO:0014069; C:postsynaptic density; ISO:RGD. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO. DR GO; GO:0098793; C:presynapse; ISS:UniProtKB. DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO. DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0055037; C:recycling endosome; ISO:RGD. DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB. DR GO; GO:0036477; C:somatodendritic compartment; ISO:RGD. DR GO; GO:0045202; C:synapse; IDA:SynGO-UCL. DR GO; GO:0097060; C:synaptic membrane; IDA:ARUK-UCL. DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD. DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD. DR GO; GO:0008179; F:adenylate cyclase binding; IDA:RGD. DR GO; GO:0004971; F:AMPA glutamate receptor activity; IDA:UniProtKB. DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL. DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:ARUK-UCL. DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD. DR GO; GO:0031681; F:G-protein beta-subunit binding; IDA:RGD. DR GO; GO:0035254; F:glutamate receptor binding; IPI:UniProtKB. DR GO; GO:0004970; F:glutamate-gated receptor activity; IDA:RGD. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0019865; F:immunoglobulin binding; IPI:UniProtKB. DR GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; ISO:RGD. DR GO; GO:0031489; F:myosin V binding; IPI:RGD. DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD. DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD. DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD. DR GO; GO:0051018; F:protein kinase A binding; IDA:RGD. DR GO; GO:0019901; F:protein kinase binding; IPI:RGD. DR GO; GO:0097110; F:scaffold protein binding; IPI:SynGO-UCL. DR GO; GO:0031267; F:small GTPase binding; IPI:RGD. DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO. DR GO; GO:0071418; P:cellular response to amine stimulus; IEP:RGD. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:RGD. DR GO; GO:0071242; P:cellular response to ammonium ion; ISO:RGD. DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IDA:RGD. DR GO; GO:0071359; P:cellular response to dsRNA; IEP:RGD. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD. DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD. DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD. DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD. DR GO; GO:0099565; P:chemical synaptic transmission, postsynaptic; ISO:RGD. DR GO; GO:0007616; P:long-term memory; IMP:RGD. DR GO; GO:0060292; P:long-term synaptic depression; ISO:RGD. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:UniProtKB. DR GO; GO:0034220; P:monoatomic ion transmembrane transport; ISO:RGD. DR GO; GO:0019228; P:neuronal action potential; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD. DR GO; GO:0045838; P:positive regulation of membrane potential; IMP:RGD. DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:UniProtKB. DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB. DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; ISO:RGD. DR GO; GO:0001919; P:regulation of receptor recycling; IMP:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB. DR GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD. DR GO; GO:0042220; P:response to cocaine; IEP:RGD. DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:0060992; P:response to fungicide; IEP:RGD. DR GO; GO:0010226; P:response to lithium ion; IEP:UniProtKB. DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD. DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD. DR GO; GO:0009636; P:response to toxic substance; IMP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0021510; P:spinal cord development; IEP:RGD. DR GO; GO:0007416; P:synapse assembly; ISO:RGD. DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central. DR CDD; cd06390; PBP1_iGluR_AMPA_GluR1; 1. DR CDD; cd13729; PBP2_iGluR_AMPA_GluR1; 1. DR Gene3D; 1.10.287.70; -; 2. DR Gene3D; 3.40.50.2300; -; 2. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2. DR InterPro; IPR001828; ANF_lig-bd_rcpt. DR InterPro; IPR019594; Glu/Gly-bd. DR InterPro; IPR001508; Iono_Glu_rcpt_met. DR InterPro; IPR015683; Ionotropic_Glu_rcpt. DR InterPro; IPR001320; Iontro_rcpt_C. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR PANTHER; PTHR18966:SF157; GLUTAMATE RECEPTOR 1; 1. DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF00060; Lig_chan; 1. DR Pfam; PF10613; Lig_chan-Glu_bd; 1. DR Pfam; PF00497; SBP_bac_3; 1. DR PRINTS; PR00177; NMDARECEPTOR. DR SMART; SM00918; Lig_chan-Glu_bd; 1. DR SMART; SM00079; PBPe; 1. DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; KW Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel; KW Ion transport; Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate; KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome; KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..907 FT /note="Glutamate receptor 1" FT /id="PRO_0000011531" FT TOPO_DOM 19..536 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 537..557 FT /note="Helical" FT /evidence="ECO:0000250" FT TOPO_DOM 558..584 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT INTRAMEM 585..600 FT /note="Helical; Pore-forming" FT /evidence="ECO:0000250" FT INTRAMEM 601..603 FT /evidence="ECO:0000250" FT TOPO_DOM 604..609 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 610..630 FT /note="Helical" FT /evidence="ECO:0000250" FT TOPO_DOM 631..805 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 806..826 FT /note="Helical; Name=M4" FT /evidence="ECO:0000250" FT TOPO_DOM 827..907 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT REGION 857..881 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 904..907 FT /note="PDZ-binding" FT BINDING 464 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 492..494 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 499 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 668..669 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 719 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT MOD_RES 645 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:7877986" FT MOD_RES 710 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:8848293" FT MOD_RES 849 FT /note="Phosphoserine; by PKC, PKA and CAMK2" FT /evidence="ECO:0000269|PubMed:7877986, FT ECO:0000269|PubMed:9405465" FT MOD_RES 863 FT /note="Phosphoserine; by PKC, PKA and PKG/PRKG2" FT /evidence="ECO:0000269|PubMed:18031684, FT ECO:0000269|PubMed:9405465" FT LIPID 603 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT LIPID 829 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CARBOHYD 63 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21639859" FT CARBOHYD 249 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21639859" FT CARBOHYD 257 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21639859" FT CARBOHYD 363 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21639859" FT CARBOHYD 401 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 406 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 75..323 FT /evidence="ECO:0000269|PubMed:21639859" FT DISULFID 732..787 FT /evidence="ECO:0000250" FT VAR_SEQ 758 FT /note="N -> G (in isoform Flip)" FT /evidence="ECO:0000303|PubMed:1699275" FT /id="VSP_000097" FT VAR_SEQ 768 FT /note="N -> S (in isoform Flip)" FT /evidence="ECO:0000303|PubMed:1699275" FT /id="VSP_000098" FT VAR_SEQ 772 FT /note="L -> V (in isoform Flip)" FT /evidence="ECO:0000303|PubMed:1699275" FT /id="VSP_000099" FT VAR_SEQ 778 FT /note="N -> S (in isoform Flip)" FT /evidence="ECO:0000303|PubMed:1699275" FT /id="VSP_000100" FT VAR_SEQ 790..793 FT /note="GGGD -> KDSG (in isoform Flip)" FT /evidence="ECO:0000303|PubMed:1699275" FT /id="VSP_000101" FT VARIANT 710 FT /note="S -> T" FT /evidence="ECO:0000269|PubMed:1699275, FT ECO:0000269|PubMed:8848293" FT MUTAGEN 645 FT /note="S->A: No effect on phosphorylation by CaMK2." FT /evidence="ECO:0000269|PubMed:9405465" FT MUTAGEN 849 FT /note="S->A: Abolishes phosphorylation by CaMK2." FT /evidence="ECO:0000269|PubMed:9405465" FT MUTAGEN 855 FT /note="R->A: Decreases binding efficiency to PRKG2." FT MUTAGEN 855 FT /note="R->E: Abolishes binding to PRKG2." FT /evidence="ECO:0000269|PubMed:18031684" FT MUTAGEN 863 FT /note="S->A: Decreases synaptic insertion during FT chemical-induced long term potentiation." FT /evidence="ECO:0000269|PubMed:18031684" FT MUTAGEN 905 FT /note="T->A: Loss of interaction with DLG1." FT /evidence="ECO:0000269|PubMed:12070168" FT MUTAGEN 907 FT /note="L->A: Loss of interaction with DLG1." FT /evidence="ECO:0000269|PubMed:12070168" FT CONFLICT 67 FT /note="S -> T (in Ref. 6; AAA63479)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="A -> R (in Ref. 6; AAA63479)" FT /evidence="ECO:0000305" FT CONFLICT 698 FT /note="R -> L (in Ref. 6; AAA63479)" FT /evidence="ECO:0000305" FT STRAND 23..32 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 37..46 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 51..61 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 67..79 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 91..104 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 130..139 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 144..149 FT /evidence="ECO:0007829|PDB:3SAJ" FT TURN 151..154 FT /evidence="ECO:0007829|PDB:7OCA" FT HELIX 156..168 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 171..176 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 183..187 FT /evidence="ECO:0007829|PDB:3SAJ" FT TURN 188..191 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 196..203 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 209..218 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 225..233 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 240..245 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 250..254 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:7OCA" FT HELIX 261..276 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 288..309 FT /evidence="ECO:0007829|PDB:3SAJ" FT HELIX 334..342 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 351..353 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 366..372 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 375..383 FT /evidence="ECO:0007829|PDB:3SAJ" FT TURN 384..386 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 387..390 FT /evidence="ECO:0007829|PDB:3SAJ" FT STRAND 409..412 FT /evidence="ECO:0007829|PDB:8AYN" FT TURN 417..419 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 420..422 FT /evidence="ECO:0007829|PDB:8AYN" FT TURN 424..428 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 431..434 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 438..450 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 454..456 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 465..467 FT /evidence="ECO:0007829|PDB:8C1P" FT TURN 469..471 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 476..482 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 487..494 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 497..502 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 503..505 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 509..512 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 514..518 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 530..532 FT /evidence="ECO:0007829|PDB:8C2H" FT HELIX 537..558 FT /evidence="ECO:0007829|PDB:8C2H" FT STRAND 559..561 FT /evidence="ECO:0007829|PDB:7OCE" FT TURN 562..564 FT /evidence="ECO:0007829|PDB:8C2I" FT HELIX 587..598 FT /evidence="ECO:0007829|PDB:8C2H" FT HELIX 610..638 FT /evidence="ECO:0007829|PDB:8C2H" FT TURN 641..643 FT /evidence="ECO:0007829|PDB:8C1Q" FT HELIX 650..655 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 658..662 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 664..667 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 668..674 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 679..689 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 690..693 FT /evidence="ECO:0007829|PDB:7OCE" FT STRAND 697..699 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 700..710 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 713..719 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 720..728 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 729..731 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 735..738 FT /evidence="ECO:0007829|PDB:8AYN" FT STRAND 744..751 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 757..769 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 772..781 FT /evidence="ECO:0007829|PDB:8AYN" FT TURN 782..784 FT /evidence="ECO:0007829|PDB:8AYN" FT HELIX 803..832 FT /evidence="ECO:0007829|PDB:8C2H" FT STRAND 905..907 FT /evidence="ECO:0007829|PDB:2AWW" SQ SEQUENCE 907 AA; 101579 MW; 2D4CFA7CCD532838 CRC64; MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ FVLQLRPELQ EALISIIDHY KWQTFVYIYD ADRGLSVLQR VLDTAAEKNW QVTAVNILTT TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL NKFKESGANV TGFQLVNYTD TIPARIMQQW RTSDSRDHTR VDWKRPKYTS ALTYDGVKVM AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW WYDKGECGSG GGDSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK GFCLIPQQSI NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM PLGATGL //