ID C9K0Z0_MOUSE Unreviewed; 883 AA. AC C9K0Z0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 29-MAY-2024, entry version 75. DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118}; GN Name=Gria2 {ECO:0000313|MGI:MGI:95809}; GN Synonyms=glur-2 {ECO:0000313|EMBL:BAI44626.1}; 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 {ECO:0000313|EMBL:BAI44626.1}; RN [1] {ECO:0000313|EMBL:BAI44626.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DdY {ECO:0000313|EMBL:BAI44626.1}; RC TISSUE=Spinal cord {ECO:0000313|EMBL:BAI44626.1}; RA Nishizawa M., Ito S.; RT "Expression of AMPA receptor subtypes in mouse spinal cord."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Receptor for glutamate that functions as a ligand-gated ion CC channel in the central nervous system and plays an important role in CC excitatory synaptic transmission. L-glutamate acts as an excitatory CC neurotransmitter at many synapses in the central nervous system. CC {ECO:0000256|RuleBase:RU367118}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367118}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}. CC Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118}. Endoplasmic CC reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004477}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic density membrane CC {ECO:0000256|ARBA:ARBA00037872}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00037872}. CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) CC family. GRIA2 subfamily. {ECO:0000256|ARBA:ARBA00037989}. 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; AB109210; BAI44626.1; -; mRNA. DR AlphaFoldDB; C9K0Z0; -. DR PeptideAtlas; C9K0Z0; -. DR AGR; MGI:95809; -. DR MGI; MGI:95809; Gria2. DR ChiTaRS; Gria2; mouse. DR GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:TreeGrafter. DR GO; GO:0043197; C:dendritic spine; IEA:TreeGrafter. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004971; F:AMPA glutamate receptor activity; IEA:TreeGrafter. DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IEA:TreeGrafter. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:TreeGrafter. DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:TreeGrafter. DR CDD; cd06389; PBP1_iGluR_AMPA_GluR2; 1. DR CDD; cd13715; PBP2_iGluR_AMPA; 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:SF99; GLUTAMATE RECEPTOR 2; 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 2: Evidence at transcript level; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, KW ECO:0000256|RuleBase:RU367118}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU367118}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, KW ECO:0000256|RuleBase:RU367118}; KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286, KW ECO:0000256|RuleBase:RU367118}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257, KW ECO:0000256|RuleBase:RU367118}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367118}; KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|RuleBase:RU367118}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU367118}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU367118}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367118}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|RuleBase:RU367118" FT CHAIN 25..883 FT /note="Glutamate receptor" FT /evidence="ECO:0000256|RuleBase:RU367118" FT /id="PRO_5027162428" FT TRANSMEM 542..564 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367118" FT TRANSMEM 625..647 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367118" FT TRANSMEM 815..837 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367118" FT DOMAIN 415..790 FT /note="Ionotropic glutamate receptor C-terminal" FT /evidence="ECO:0000259|SMART:SM00079" FT DOMAIN 425..490 FT /note="Ionotropic glutamate receptor L-glutamate and FT glycine-binding" FT /evidence="ECO:0000259|SMART:SM00918" SQ SEQUENCE 883 AA; 98574 MW; 9BBE632C31CB01FF CRC64; MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI QFGGANVSGF QIVVYDDSLA SKFIERWSTL EGKEYPGAHT ATIKYTSALT YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF SLGAFMRQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI //