ID GRIA2_HUMAN Reviewed; 883 AA. AC P42262; Q96FP6; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 3. DT 25-NOV-2008, entry version 93. DE RecName: Full=Glutamate receptor 2; DE Short=GluR-2; DE AltName: Full=GluR-B; DE AltName: Full=GluR-K2; DE AltName: Full=Glutamate receptor ionotropic, AMPA 2; DE AltName: Full=AMPA-selective glutamate receptor 2; DE Flags: Precursor; GN Name=GRIA2; Synonyms=GLUR2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), AND VARIANT ARG-607. RC TISSUE=Brain; RX MEDLINE=94271981; PubMed=8003671; RA Sun W., Ferrer-Montiel A.V., Montal M.; RT "Primary structure and functional expression of the AMPA/kainate RT receptor subunit 2 from human brain."; RL NeuroReport 5:441-444(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FLOP), AND VARIANTS RP ARG-607 AND ARG-608. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP RNA EDITING OF POSITION 607. RX MEDLINE=95016699; PubMed=7523595; RA Paschen W., Hedreen J.C., Ross C.A.; RT "RNA editing of the glutamate receptor subunits GluR2 and GluR6 in RT human brain tissue."; RL J. Neurochem. 63:1596-1602(1994). RN [4] RP IDENTIFICATION OF ISOFORM 3. RX PubMed=14687553; DOI=10.1016/S0896-6273(03)00722-0; RA Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T., RA Koehr G., Malinow R., Seeburg P.H., Osten P.; RT "Glutamatergic plasticity by synaptic delivery of GluR-B(long)- RT containing AMPA receptors."; RL Neuron 40:1199-1212(2003). CC -!- FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an CC excitatory neurotransmitter at many synapses in the central CC nervous system. Binding of the excitatory neurotransmitter L- CC glutamate induces a conformation change, leading to the opening of CC the cation channel, and thereby converts the chemical signal to an CC electrical impulse. The receptor then desensitizes rapidly and CC enters a transient inactive state, characterized by the presence CC of bound agonist. CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate CC receptor subunits. Tetramers may be formed by the dimerization of CC dimers. May interact with MPP4. Forms a ternary complex with GRIP1 CC and CSPG4. Interacts with PRKCABP, GRIP1 and GRIP2 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC Cell junction, synapse, postsynaptic cell membrane; Multi-pass CC membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Flop; CC IsoId=P42262-1; Sequence=Displayed; CC Name=Flip; CC IsoId=P42262-2; Sequence=VSP_000102, VSP_000103, VSP_000104, CC VSP_000105; CC Name=3; Synonyms=Long; CC IsoId=P42262-3; Sequence=VSP_029309; CC -!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. CC Cys-610 palmitoylation leads to Golgi retention and decreased cell CC surface expression. In contrast, Cys-836 palmitoylation does not CC affect cell surface expression but regulates stimulation-dependent CC endocytosis (By similarity). CC -!- RNA EDITING: Modified_positions=607; Note=Partially edited. Fully CC edited in the brain. Heteromerically expressed edited GLUR2 (R) CC receptor complexes are impermeable to calcium, whereas the CC unedited (Q) forms are highly permeable to divalent ions. 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 > CC kainate. CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10) CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L20814; AAA58631.1; -; mRNA. DR EMBL; BC010574; AAH10574.1; -; mRNA. DR PIR; I58181; I58181. DR RefSeq; NP_000817.2; -. DR RefSeq; NP_001077088.1; -. DR RefSeq; NP_001077089.1; -. DR UniGene; Hs.32763; -. DR HSSP; P19491; 1FTK. DR SMR; P42262; 413-527, 652-795. DR PhosphoSite; P42262; -. DR Ensembl; ENSG00000120251; Homo sapiens. DR GeneID; 2891; -. DR KEGG; hsa:2891; -. DR HGNC; HGNC:4572; GRIA2. DR HPA; CAB007812; -. DR HPA; HPA008441; -. DR MIM; 138247; gene. DR PharmGKB; PA28967; -. DR HOGENOM; P42262; -. DR HOVERGEN; P42262; -. DR DrugBank; DB00142; L-Glutamic Acid. DR NextBio; 11429; -. DR ArrayExpress; P42262; -. DR CleanEx; HS_GRIA2; -. DR GermOnline; ENSG00000120251; Homo sapiens. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW. DR GO; GO:0004971; F:alpha-amino-3-hydroxy-5-methyl-4-isoxazole ...; TAS:ProtInc. DR GO; GO:0005234; F:extracellular-glutamate-gated ion channel a...; IEA:InterPro. DR GO; GO:0015277; F:kainate selective glutamate receptor activity; TAS:ProtInc. DR GO; GO:0006811; P:ion transport; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR InterPro; IPR001828; ANF_lig_bd_rcpt. DR InterPro; IPR015683; Glutamate_receptor-rel. DR InterPro; IPR001320; Iontro_glu_rcpt. DR InterPro; IPR001508; NMDA_rcpt. DR PANTHER; PTHR18966; Glut_Rec_Related; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF00060; Lig_chan; 1. DR PRINTS; PR00177; NMDARECEPTOR. DR SMART; SM00079; PBPe; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Cell membrane; Glycoprotein; KW Ion transport; Ionic channel; Lipoprotein; Membrane; Palmitate; KW Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Receptor; KW RNA editing; Signal; Synapse; Transmembrane; Transport. FT SIGNAL 1 24 Potential. FT CHAIN 25 883 Glutamate receptor 2. FT /FTId=PRO_0000011532. FT TOPO_DOM 25 543 Extracellular (Potential). FT TRANSMEM 544 564 Potential. FT TOPO_DOM 565 624 Cytoplasmic (Potential). FT TRANSMEM 625 645 Potential. FT TOPO_DOM 646 812 Extracellular (Potential). FT TRANSMEM 813 833 Potential. FT TOPO_DOM 834 883 Cytoplasmic (Potential). FT REGION 499 501 Glutamate binding (By similarity). FT REGION 675 676 Glutamate binding (By similarity). FT BINDING 506 506 Glutamate (By similarity). FT BINDING 726 726 Glutamate (By similarity). FT MOD_RES 683 683 Phosphoserine; by PKC (By similarity). FT MOD_RES 717 717 Phosphoserine; by PKG (By similarity). FT MOD_RES 869 869 Phosphotyrosine (By similarity). FT MOD_RES 876 876 Phosphotyrosine (By similarity). FT MOD_RES 880 880 Phosphoserine (By similarity). FT LIPID 610 610 S-palmitoyl cysteine (By similarity). FT LIPID 836 836 S-palmitoyl cysteine (By similarity). FT CARBOHYD 256 256 N-linked (GlcNAc...) (Potential). FT CARBOHYD 370 370 N-linked (GlcNAc...) (Potential). FT CARBOHYD 406 406 N-linked (GlcNAc...) (Potential). FT CARBOHYD 413 413 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 765 766 NA -> TP (in isoform Flip). FT /FTId=VSP_000102. FT VAR_SEQ 775 775 N -> S (in isoform Flip). FT /FTId=VSP_000103. FT VAR_SEQ 779 779 L -> V (in isoform Flip). FT /FTId=VSP_000104. FT VAR_SEQ 796 800 SGGGD -> AKDSG (in isoform Flip). FT /FTId=VSP_000105. FT VAR_SEQ 848 883 VAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI -> M FT TLNDAMRNKARLSITGSTGENGRVMTPEFPKAVHAVPYVSP FT GMGMNVSVTDLS (in isoform 3). FT /FTId=VSP_029309. FT VARIANT 607 607 Q -> R (in RNA edited version). FT /FTId=VAR_000303. FT VARIANT 608 608 Q -> R (in dbSNP:rs17850675). FT /FTId=VAR_037055. FT CONFLICT 140 140 I -> V (in Ref. 2; AAH10574). FT CONFLICT 241 241 G -> E (in Ref. 1; AAA58631). FT CONFLICT 764 764 R -> G (in Ref. 1; AAA58631). SQ SEQUENCE 883 AA; 98821 MW; 6DAB96C76D1D8448 CRC64; MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE MYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT TTIKYTSALT 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 SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLRNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI //