Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00602
Entry Name
UniProt Accession
Theoretical PI
7.12
Molecular Weight
98661.84
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Glutamate receptor 2
Protein Synonyms/Alias
GluR-2; AMPA-selective glutamate receptor 2; GluR-B; GluR-K2; Glutamate receptor ionotropic, AMPA 2; GluA2;
Gene Name
Gria2
Gene Synonyms/Alias
Glur2;
Created Date
01-NOV-1991
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
610
Canonical
GAFMQQGCDISPRSL
[1]
S-Palmitoylation
836
Canonical
LVALIEFCYKSRAEA
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Hayashi T, Rumbaugh G, Huganir RL. Differential regulation of AMPA receptorsubunit trafficking by palmitoylation of two distinct sites. Neuron. 2005 Sep1;47(5):709-23.[PMID:16129400]
Functional Description
Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity).
Sequence Annotation
Topological domain: 25 543 Extracellular.
Transmembrane: 544 564 Helical.
Topological domain: 565 591 Cytoplasmic.
Topological domain: 611 616 Cytoplasmic.
Transmembrane: 617 637 Helical.
Topological domain: 638 812 Extracellular.
Transmembrane: 813 833 Helical; Name=M4.
Topological domain: 834 883 Cytoplasmic.
Binding site: 471 471 Glutamate.
Binding site: 506 506 Glutamate.
Binding site: 726 726 Glutamate.
Modified residue: 683 683 Phosphoserine; by PKC.
Modified residue: 717 717 Phosphoserine; by PKG.
Modified residue: 876 876 Phosphotyrosine.
Modified residue: 880 880 Phosphoserine.
Protein Length
883 AA.
Protein Sequence
(Canonical)
MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP  60
HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG  120
THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV  180
GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL  240
GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT  300
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI  360
KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT  420
ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI  480
WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD  540
PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF  600
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL  660
SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK  720
YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL  780
DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR  840
AEAKRMKVAK NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI                    883
FASTA
(Canonical)
>LipidDB-10090-00602|P23819
MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTP
HIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDG
THPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINV
GNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANL
GFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALT
YDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNI
KFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTT
ILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKI
WNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLD
PLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWF
SLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDL
SKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGK
YAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLL
DKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSR
AEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI
Gene Ontology
GO:0032281; C:alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex; IDA:MGI
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0030425; C:dendrite; IBA:RefGenome
GO:0005783; C:endoplasmic reticulum; IDA:MGI
GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB
GO:0016020; C:membrane; IDA:MGI
GO:0043005; C:neuron projection; IDA:BHF-UCL
GO:0045211; C:postsynaptic membrane; IDA:MGI
GO:0045202; C:synapse; IDA:MGI
GO:0008021; C:synaptic vesicle; IDA:MGI
GO:0004971; F:alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity; ISS:UniProtKB
GO:0005234; F:extracellular-glutamate-gated ion channel activity; IDA:MGI
GO:0004970; F:ionotropic glutamate receptor activity; IDA:MGI
GO:0015277; F:kainate selective glutamate receptor activity; ISS:UniProtKB
GO:0034220; P:ion transmembrane transport; IDA:GOC
GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:GOC
GO:0007268; P:synaptic transmission; IDA:MGI
GO:0035249; P:synaptic transmission, glutamatergic; IBA:RefGenome
Interpro
InterPro; IPR001828; ANF_lig-bd_rcpt
InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd
InterPro; IPR001320; Iontro_glu_rcpt
InterPro; IPR001508; NMDA_rcpt
InterPro; IPR028082; Peripla_BP_I
Pfam
Pfam; PF01094; ANF_receptor;
Pfam; PF00060; Lig_chan;
Pfam; PF10613; Lig_chan-Glu_bd;
SMART
SMART; SM00918; Lig_chan-Glu_bd;
SMART; SM00079; PBPe;
PROSITE
PRINTS
PRINTS; PR00177; NMDARECEPTOR;