P19490 (GRIA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate receptor 1
Short name=GluR-1

Alternative name(s):
AMPA-selective glutamate receptor 1
GluR-A
GluR-K1
Glutamate receptor ionotropic, AMPA 1
Short name=GluA1

Gene names

Name:	Gria1
Synonyms:	Glur1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	907 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Ionotropic glutamate receptor. 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. Ref.12 Ref.17
Subunit structure	Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with DLG1 via its C-terminus. Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with HIP1, RASGRF2, SYNDIG1 and LRFN1. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes. Interacts (via PDZ-binding motif) with SHANK3 (via PDZ domain). Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20
Subcellular location	Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density By similarity. Cell projection › dendrite By similarity. Cell projection › dendritic spine By similarity. Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression. Ref.11 Ref.12 Ref.17
Tissue specificity	Detected in cerebellum (at protein level). Ref.11
Domain	The M4 transmembrane segment mediates tetramerization and is required for cell surface expression By similarity.
Post-translational modification	Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-603 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-829 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis By similarity.
Polymorphism	Both variants Ser-710 and Thr-710 are phosphorylated at this position.
Miscellaneous	The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.
Sequence similarities	Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIA1 subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Cell projection Endoplasmic reticulum Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to amine stimulus Inferred from expression pattern PubMed 19674091. Source: RGD cellular response to amino acid stimulus Inferred from expression pattern PubMed 19913087. Source: RGD cellular response to dsRNA Inferred from expression pattern PubMed 19958814. Source: RGD cellular response to growth factor stimulus Inferred from expression pattern PubMed 19958814. Source: RGD cellular response to organic cyclic compound Inferred from expression pattern PubMed 20025928. Source: RGD cellular response to peptide hormone stimulus Inferred from expression pattern PubMed 20237279. Source: RGD ion transmembrane transport Inferred from Biological aspect of Ancestor. Source: GOC ionotropic glutamate receptor signaling pathway Inferred from direct assay PubMed 17409242Ref.17. Source: GOC long-term memory Inferred from mutant phenotype PubMed 19547753. Source: RGD neuronal action potential Inferred from mutant phenotype PubMed 12536214. Source: UniProtKB positive regulation of membrane potential Inferred from mutant phenotype PubMed 20165912. Source: RGD positive regulation of synaptic transmission Inferred from mutant phenotype PubMed 11348590. Source: UniProtKB receptor internalization Inferred from direct assay PubMed 11100149. Source: UniProtKB regulation of receptor recycling Inferred from mutant phenotype PubMed 11348590. Source: UniProtKB regulation of synaptic plasticity Inferred from mutant phenotype PubMed 12536214. Source: UniProtKB regulation of synaptic transmission Inferred from direct assay PubMed 11348590. Source: UniProtKB response to arsenic-containing substance Inferred from expression pattern PubMed 19761793. Source: RGD response to cocaine Inferred from expression pattern PubMed 20600170. Source: RGD response to drug Inferred from expression pattern PubMed 19940171. Source: RGD response to electrical stimulus Inferred from expression pattern PubMed 20554014. Source: RGD response to estradiol Inferred from expression pattern PubMed 19596275. Source: RGD response to fungicide Inferred from expression pattern PubMed 19591855. Source: RGD response to lithium ion Inferred from expression pattern PubMed 15269270. Source: UniProtKB response to organic cyclic compound Inferred from expression pattern PubMed 19940171. Source: RGD response to peptide hormone Inferred from expression pattern PubMed 20554878. Source: RGD response to toxic substance Inferred from mutant phenotype PubMed 20165912. Source: RGD spinal cord development Inferred from expression pattern PubMed 19446017. Source: RGD synaptic transmission, glutamatergic Non-traceable author statement PubMed 15269270. Source: UniProtKB
Cellular_component	alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Inferred from direct assay Ref.17. Source: UniProtKB asymmetric synapse Inferred from direct assay PubMed 12077196. Source: RGD cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from direct assay PubMed 19321442. Source: RGD cytosol Inferred from direct assay PubMed 20165912. Source: RGD dendrite Inferred from sequence or structural similarity. Source: UniProtKB dendritic shaft Inferred from direct assay PubMed 11100149. Source: UniProtKB dendritic spine Inferred from direct assay PubMed 12077196PubMed 16338934. Source: RGD early endosome Inferred from direct assay PubMed 11100149. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell excitatory synapse Inferred from direct assay PubMed 19730411. Source: BHF-UCL ionotropic glutamate receptor complex Traceable author statement PubMed 11836517. Source: UniProtKB neuromuscular junction Inferred from direct assay PubMed 19918122. Source: RGD neuron projection Inferred from direct assay PubMed 16338934. Source: RGD neuron spine Inferred from direct assay PubMed 20083202. Source: RGD neuronal cell body Inferred from direct assay PubMed 11100149. Source: UniProtKB plasma membrane Inferred from direct assay PubMed 20165912. Source: RGD postsynaptic density Inferred from direct assay PubMed 12077196. Source: RGD postsynaptic membrane Inferred from Biological aspect of Ancestor. Source: RefGenome protein complex Inferred from direct assay PubMed 17329210. Source: RGD synapse Inferred from mutant phenotype PubMed 12536214. Source: UniProtKB
Molecular_function	G-protein alpha-subunit binding Inferred from physical interaction PubMed 19942860. Source: RGD G-protein beta-subunit binding Inferred from direct assay PubMed 19942860. Source: RGD PDZ domain binding Inferred from physical interaction PubMed 16634638. Source: RGD adenylate cyclase binding Inferred from direct assay PubMed 19942860. Source: RGD alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Inferred from direct assay Ref.17. Source: UniProtKB beta-2 adrenergic receptor binding Inferred from physical interaction PubMed 19942860. Source: RGD extracellular-glutamate-gated ion channel activity Inferred from Biological aspect of Ancestor. Source: RefGenome identical protein binding Inferred from physical interaction PubMed 19461580PubMed 21317873. Source: IntAct ionotropic glutamate receptor activity Inferred from direct assay PubMed 17409242. Source: RGD myosin V binding Inferred from physical interaction PubMed 16338934. Source: RGD protein binding Inferred from physical interaction PubMed 11348590Ref.14Ref.15Ref.18. Source: UniProtKB protein domain specific binding Inferred from physical interaction PubMed 17194442. Source: RGD protein homodimerization activity Traceable author statement PubMed 11348590. Source: UniProtKB protein kinase A binding Inferred from direct assay PubMed 19942860. Source: RGD protein kinase binding Inferred from physical interaction PubMed 17329210. Source: RGD small GTPase binding Inferred from physical interaction PubMed 17194442. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-371642,EBI-371642
Adrb2	P10608	3	EBI-371642,EBI-7090342
Gria2	P19491	3	EBI-371642,EBI-77718
Myo5b	P70569	2	EBI-371642,EBI-975940

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Flop (identifier: P19490-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Flip (identifier: P19490-2)

The sequence of this isoform differs from the canonical sequence as follows:
     758-758: N → G
     768-768: N → S
     772-772: L → V
     778-778: N → S
     790-793: GGGD → KDSG

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Chain

19 – 907

889

Glutamate receptor 1

PRO_0000011531

Regions

Topological domain

19 – 536

518

Extracellular By similarity

Transmembrane

537 – 557

21

Helical; By similarity

Topological domain

558 – 584

27

Cytoplasmic By similarity

Intramembrane

585 – 600

16

Helical; Pore-forming; By similarity

Intramembrane

601 – 603

3

By similarity

Topological domain

604 – 609

6

Cytoplasmic By similarity

Transmembrane

610 – 630

21

Helical; By similarity

Topological domain

631 – 805

175

Extracellular By similarity

Transmembrane

806 – 826

21

Helical; Name=M4; By similarity

Topological domain

827 – 907

81

Cytoplasmic By similarity

Region

492 – 494

3

Glutamate binding By similarity

Region

668 – 669

2

Glutamate binding By similarity

Motif

904 – 907

4

PDZ-binding

Sites

Binding site

464

1

Glutamate By similarity

Binding site

499

1

Glutamate By similarity

Binding site

719

1

Glutamate By similarity

Amino acid modifications

Modified residue

645

1

Phosphoserine Ref.7

Modified residue

710

1

Phosphoserine; by PKC Ref.8

Modified residue

849

1

Phosphoserine; by PKC, PKA and CAMK2 Ref.9

Modified residue

863

1

Phosphoserine; by PKC and PKA Ref.9

Lipidation

603

1

S-palmitoyl cysteine By similarity

Lipidation

829

1

S-palmitoyl cysteine By similarity

Glycosylation

63

1

N-linked (GlcNAc...)

Glycosylation

249

1

N-linked (GlcNAc...) Ref.20

Glycosylation

257

1

N-linked (GlcNAc...) Ref.20

Glycosylation

363

1

N-linked (GlcNAc...) Ref.20

Glycosylation

401

1

N-linked (GlcNAc...) Potential

Glycosylation

406

1

N-linked (GlcNAc...) Potential

Disulfide bond

75 ↔ 323

Ref.20

Disulfide bond

732 ↔ 787

By similarity

Natural variations

Alternative sequence

758

1

N → G in isoform Flip.

VSP_000097

Alternative sequence

768

1

N → S in isoform Flip.

VSP_000098

Alternative sequence

772

1

L → V in isoform Flip.

VSP_000099

Alternative sequence

778

1

N → S in isoform Flip.

VSP_000100

Alternative sequence

790 – 793

4

GGGD → KDSG in isoform Flip.

VSP_000101

Natural variant

710

1

S → T. Ref.6 Ref.8

Experimental info

Mutagenesis

645

1

S → A: No effect on phosphorylation by CaMK2. Ref.9

Mutagenesis

849

1

S → A: Abolishes phosphorylation by CaMK2. Ref.9

Mutagenesis

905

1

T → A: Loss of interaction with DLG1. Ref.11

Mutagenesis

907

1

L → A: Loss of interaction with DLG1. Ref.11

Sequence conflict

67

1

S → T in AAA63479. Ref.6

Sequence conflict

248

1

A → R in AAA63479. Ref.6

Sequence conflict

698

1

R → L in AAA63479. Ref.6

Secondary structure

1

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907

Helix Strand Turn

Details...

Beta strand

23 – 32

10

Beta strand

34 – 36

3

Helix

37 – 46

10

Beta strand

51 – 61

11

Helix

67 – 79

13

Beta strand

85 – 87

3

Helix

91 – 104

14

Beta strand

108 – 110

3

Beta strand

122 – 124

3

Helix

130 – 139

10

Beta strand

144 – 149

6

Helix

156 – 168

13

Beta strand

171 – 176

6

Helix

177 – 179

3

Helix

183 – 187

5

Turn

188 – 191

4

Beta strand

196 – 203

8

Helix

206 – 208

3

Helix

209 – 218

10

Beta strand

225 – 233

9

Helix

235 – 237

3

Helix

240 – 245

6

Beta strand

250 – 254

5

Helix

261 – 276

16

Helix

288 – 309

22

Helix

334 – 342

9

Beta strand

346 – 348

3

Beta strand

351 – 353

3

Beta strand

359 – 361

3

Beta strand

366 – 372

7

Beta strand

375 – 383

9

Turn

384 – 386

3

Beta strand

387 – 390

4

Beta strand

905 – 907

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Flop [UniParc]. Last modified May 16, 2006. Version 2. Checksum: 2D4CFA7CCD532838	FASTA	907	101,579
	10 20 30 40 50 60 MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID 70 80 90 100 110 120 IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ 130 140 150 160 170 180 FVLQLRPELQ EALISIIDHY KWQTFVYIYD ADRGLSVLQR VLDTAAEKNW QVTAVNILTT 190 200 210 220 230 240 TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL 250 260 270 280 290 300 NKFKESGANV TGFQLVNYTD TIPARIMQQW RTSDSRDHTR VDWKRPKYTS ALTYDGVKVM 310 320 330 340 350 360 AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR 370 380 390 400 410 420 RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV 430 440 450 460 470 480 MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE 490 500 510 520 530 540 LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW 550 560 570 580 590 600 MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ 610 620 630 640 650 660 QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA 670 680 690 700 710 720 YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES 730 740 750 760 770 780 TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW 790 800 810 820 830 840 WYDKGECGSG GGDSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK 850 860 870 880 890 900 GFCLIPQQSI NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM PLGATGL
	Isoform Flip [UniParc]. Checksum: 5FA3091114C0BA6B	FASTA	907	101,555
	10 20 30 40 50 60 MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID 70 80 90 100 110 120 IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ 130 140 150 160 170 180 FVLQLRPELQ EALISIIDHY KWQTFVYIYD ADRGLSVLQR VLDTAAEKNW QVTAVNILTT 190 200 210 220 230 240 TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL 250 260 270 280 290 300 NKFKESGANV TGFQLVNYTD TIPARIMQQW RTSDSRDHTR VDWKRPKYTS ALTYDGVKVM 310 320 330 340 350 360 AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR 370 380 390 400 410 420 RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV 430 440 450 460 470 480 MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE 490 500 510 520 530 540 LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW 550 560 570 580 590 600 MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ 610 620 630 640 650 660 QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA 670 680 690 700 710 720 YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES 730 740 750 760 770 780 TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRGPV NLAVLKLSEQ GVLDKLKSKW 790 800 810 820 830 840 WYDKGECGSK DSGSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK 850 860 870 880 890 900 GFCLIPQQSI NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM PLGATGL

References

[1]	"Cloning by functional expression of a member of the glutamate receptor family." Hollmann M., O'Shea-Greenfield A., Rogers S.W., Heinemann S.F. Nature 342:643-648(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP). Tissue: Forebrain.
[2]	Hartley M. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"A family of AMPA-selective glutamate receptors." Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A., Sakmann B., Seeburg P.H. Science 249:556-560(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP). Tissue: Brain.
[4]	Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A., Sakmann B., Seeburg P.H. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 67; 248; 698; 710; 789 AND 893.
[5]	"Molecular cloning and functional expression of glutamate receptor subunit genes." Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E.S., Maron C., Heinemann S.F. Science 249:1033-1037(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
[6]	"Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS." Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A., Koehler M., Takagi T., Sakmann B., Seeburg P.H. Science 249:1580-1585(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), VARIANT THR-710. Tissue: Brain.
[7]	"Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors." Yakel J.L., Vissavajjhala P., Derkach V.A., Brickey D.A., Soderling T.R. Proc. Natl. Acad. Sci. U.S.A. 92:1376-1380(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-645.
[8]	"Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696." Nakazawa K., Tadakuma T., Nokihara K., Ito M. Neurosci. Res. 24:75-86(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THR-710, PHOSPHORYLATION AT SER-710.
[9]	"Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II." Mammen A.L., Kameyama K., Roche K.W., Huganir R.L. J. Biol. Chem. 272:32528-32533(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-849 AND SER-863, MUTAGENESIS OF SER-645 AND SER-849.
[10]	"SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit." Leonard A.S., Davare M.A., Horne M.C., Garner C.C., Hell J.W. J. Biol. Chem. 273:19518-19524(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DLG1.
[11]	"Selective binding of synapse-associated protein 97 to GluR-A alpha-amino-5-hydroxy-3-methyl-4-isoxazole propionate receptor subunit is determined by a novel sequence motif." Cai C., Coleman S.K., Niemi K., Keinaenen K. J. Biol. Chem. 277:31484-31490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DLG1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF THR-905 AND LEU-907.
[12]	"Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics." Bedoukian M.A., Weeks A.M., Partin K.M. J. Biol. Chem. 281:23908-23921(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH CACNG2.
[13]	"SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses." Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E. Neuron 50:233-245(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LRFN1.
[14]	"AMPA receptor subunit-specific regulation by a distinct family of type II TARPs." Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S. Neuron 59:986-996(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CACNG5.
[15]	"Selective regulation of long-form calcium-permeable AMPA receptors by an atypical TARP, gamma-5." Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G. Nat. Neurosci. 12:277-285(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CACNG5.
[16]	Erratum Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G. Nat. Neurosci. 12:808-808(2009)
[17]	"Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors." Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B., Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N. Science 323:1313-1319(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[18]	"Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating." Shi Y., Suh Y.H., Milstein A.D., Isozaki K., Schmid S.M., Roche K.W., Nicoll R.A. Proc. Natl. Acad. Sci. U.S.A. 107:16315-16319(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CNIH2 AND CACNG2.
[19]	"Crystal structure of the second PDZ domain of SAP97 in complex with a GluR-A C-terminal peptide." von Ossowski I., Oksanen E., von Ossowski L., Cai C., Sundberg M., Goldman A., Keinanen K. FEBS J. 273:5219-5229(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 890-907 IN COMPLEX WITH DLG1, INTERACTION WITH DLG1.
[20]	"Crystal structure of the glutamate receptor GluA1 N-terminal domain." Yao G., Zong Y., Gu S., Zhou J., Xu H., Mathews I.I., Jin R. Biochem. J. 438:255-263(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-392, SUBUNIT, GLYCOSYLATION AT ASN-249; ASN-257 AND ASN-363, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X17184 mRNA. Translation: CAA35050.1.
M36418 mRNA. Translation: AAA41243.2.
M38060 mRNA. Translation: AAA63479.1.

PIR

A40170.
ACRTK1. S07059.

RefSeq

NP_113796.1. NM_031608.1. [P19490-1]

UniGene

Rn.29971.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AWW	X-ray	2.21	C	890-907	[»]
3SAJ	X-ray	2.50	A/B/C/D	22-392	[»]

ProteinModelPortal

P19490.

SMR

P19490. Positions 406-520, 645-788.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

248399. 5 interactions.

DIP

DIP-30929N.

IntAct

P19490. 17 interactions.

MINT

MINT-726538.

Chemistry

BindingDB

P19490.

ChEMBL

CHEMBL3753.

GuidetoPHARMACOLOGY

444.

Protein family/group databases

TCDB

1.A.10.1.1. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSite

P19490.

Proteomic databases

PRIDE

P19490.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

50592.

KEGG

rno:50592.

UCSC

RGD:621531. rat. [P19490-1]

Organism-specific databases

CTD

2890.

RGD

621531. Gria1.

Phylogenomic databases

HOVERGEN

HBG051839.

KO

K05197.

PhylomeDB

P19490.

Gene expression databases

Genevestigator

P19490.

Family and domain databases

InterPro

IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
IPR001638. SBP_bac_3.
[Graphical view]

Pfam

PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF00497. SBP_bac_3. 1 hit.
[Graphical view]

PRINTS

PR00177. NMDARECEPTOR.

SMART

SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]

SUPFAM

SSF53822. SSF53822. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P19490.

NextBio

610434.

Entry information

Entry name

GRIA1_RAT

Accession

Primary (citable) accession number: P19490

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	May 16, 2006
Last modified:	July 9, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program