P19492 (GRIA3_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate receptor 3
Short name=GluR-3

Alternative name(s):
AMPA-selective glutamate receptor 3
GluR-C
GluR-K3
Glutamate receptor ionotropic, AMPA 3
Short name=GluA3

Gene names

Name:	Gria3
Synonyms:	Glur3

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	888 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	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.
Subunit structure	Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with PRKCABP, GRIP1 and GRIP2. Found in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.12
Subcellular location	Cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Note: Interaction with CNIH2 and CNIH3 promotes cell surface expression. Ref.9
Post-translational modification	Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-615 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-841 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis By similarity.
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. GRIA3 subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
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	regulation of receptor recycling Inferred from mutant phenotype PubMed 11348590. Source: UniProtKB response to fungicide Inferred from expression pattern PubMed 19591855. Source: RGD response to lithium ion Inferred from expression pattern PubMed 15269270. Source: UniProtKB
Cellular_component	alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Inferred from direct assay Ref.9. Source: UniProtKB asymmetric synapse Inferred from direct assay PubMed 12077196. Source: RGD cell junction Inferred from electronic annotation. Source: UniProtKB-KW dendritic shaft Inferred from direct assay PubMed 12077196. Source: RGD perikaryon Inferred from direct assay PubMed 15844209. Source: RGD postsynaptic density Inferred from direct assay Ref.5. Source: UniProtKB postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synaptic cleft Inferred from direct assay PubMed 17207780. Source: RGD terminal bouton Inferred from direct assay PubMed 15844209. Source: RGD
Molecular_function	alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Inferred from direct assay PubMed 11834304. Source: RGD extracellular-glutamate-gated ion channel activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Pick1	Q9EP80	5	EBI-77764,EBI-77728

Alternative products

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

Isoform Flop (identifier: P19492-1)

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: P19492-2)

The sequence of this isoform differs from the canonical sequence as follows:
     770-771: NA → TP
     780-780: N → S
     784-784: L → I
     801-805: SGGGD → AKDSG

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Chain

23 – 888

866

Glutamate receptor 3

PRO_0000011537

Regions

Topological domain

23 – 546

524

Extracellular By similarity

Transmembrane

547 – 567

21

Helical; By similarity

Topological domain

568 – 596

29

Cytoplasmic By similarity

Intramembrane

597 – 612

16

Helical; Pore-forming; By similarity

Intramembrane

613 – 615

3

By similarity

Topological domain

616 – 621

6

Cytoplasmic By similarity

Transmembrane

622 – 642

21

Helical; By similarity

Topological domain

643 – 817

175

Extracellular By similarity

Transmembrane

818 – 838

21

Helical; By similarity

Topological domain

839 – 888

50

Cytoplasmic By similarity

Region

502 – 504

3

Glutamate binding

Region

680 – 681

2

Glutamate binding

Sites

Binding site

474

1

Glutamate

Binding site

509

1

Glutamate

Binding site

731

1

Glutamate

Amino acid modifications

Modified residue

871

1

Phosphotyrosine By similarity

Modified residue

881

1

Phosphotyrosine By similarity

Lipidation

615

1

S-palmitoyl cysteine By similarity

Lipidation

841

1

S-palmitoyl cysteine By similarity

Glycosylation

57

1

N-linked (GlcNAc...) Potential

Glycosylation

260

1

N-linked (GlcNAc...) Ref.12

Glycosylation

374

1

N-linked (GlcNAc...) Ref.12

Glycosylation

409

1

N-linked (GlcNAc...) Potential

Glycosylation

416

1

N-linked (GlcNAc...) Potential

Disulfide bond

85 ↔ 334

Ref.10 Ref.11 Ref.12

Disulfide bond

744 ↔ 799

Ref.10 Ref.11 Ref.12

Natural variations

Alternative sequence

770 – 771

2

NA → TP in isoform Flip.

VSP_000119

Alternative sequence

780

1

N → S in isoform Flip.

VSP_000120

Alternative sequence

784

1

L → I in isoform Flip.

VSP_000121

Alternative sequence

801 – 805

5

SGGGD → AKDSG in isoform Flip.

VSP_000122

Experimental info

Sequence conflict

517 – 518

2

KP → NA Ref.2

Secondary structure

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888

Helix Strand Turn

Details...

Beta strand

26 – 34

9

Helix

39 – 53

15

Turn

58 – 60

3

Beta strand

62 – 71

10

Helix

77 – 88

12

Turn

89 – 91

3

Beta strand

95 – 97

3

Turn

101 – 103

3

Helix

104 – 114

11

Beta strand

118 – 120

3

Beta strand

130 – 134

5

Helix

140 – 150

11

Beta strand

154 – 159

6

Helix

166 – 177

12

Beta strand

181 – 186

6

Helix

194 – 204

11

Turn

205 – 207

3

Beta strand

210 – 215

6

Helix

217 – 230

14

Beta strand

238 – 241

4

Helix

246 – 248

3

Helix

252 – 256

5

Beta strand

260 – 266

7

Helix

272 – 281

10

Turn

286 – 288

3

Beta strand

292 – 295

4

Helix

299 – 320

22

Beta strand

336 – 338

3

Turn

342 – 345

4

Helix

346 – 353

8

Beta strand

357 – 359

3

Beta strand

362 – 364

3

Beta strand

370 – 372

3

Beta strand

377 – 383

7

Beta strand

386 – 394

9

Turn

395 – 397

3

Beta strand

398 – 400

3

Beta strand

418 – 423

6

Turn

427 – 429

3

Beta strand

430 – 432

3

Helix

436 – 438

3

Helix

441 – 444

4

Beta strand

445 – 447

3

Helix

448 – 460

13

Beta strand

463 – 468

6

Turn

479 – 481

3

Helix

486 – 492

7

Beta strand

497 – 499

3

Helix

507 – 510

4

Beta strand

513 – 515

3

Beta strand

519 – 522

4

Beta strand

524 – 529

6

Helix

662 – 666

5

Beta strand

669 – 676

8

Helix

680 – 687

8

Helix

691 – 702

12

Turn

704 – 706

3

Beta strand

708 – 711

4

Helix

712 – 721

10

Turn

722 – 724

3

Beta strand

725 – 731

7

Helix

732 – 739

8

Beta strand

746 – 750

5

Beta strand

756 – 758

3

Beta strand

761 – 763

3

Helix

769 – 781

13

Helix

784 – 793

10

Turn

794 – 796

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Flop [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 2981616375661703	FASTA	888	100,373
	10 20 30 40 50 60 MGQSVLRAVF FLVLGLLGHS HGGFPNTISI GGLFMRNTVQ EHSAFRFAVQ LYNTNQNTTE 70 80 90 100 110 120 KPFHLNYHVD HLDSSNSFSV TNAFCSQFSR GVYAIFGFYD QMSMNTLTSF CGALHTSFVT 130 140 150 160 170 180 PSFPTDADVQ FVIQMRPALK GAILSLLSYY KWEKFVYLYD TERGFSVLQA IMEAAVQNNW 190 200 210 220 230 240 QVTARSVGNI KDVQEFRRII EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM 250 260 270 280 290 300 LANLGFTDIL LERVMHGGAN ITGFQIVNNE NPMVQQFIQR WVRLDEREFP EAKNAPLKYT 310 320 330 340 350 360 SALTHDAILV IAEAFRYLRR QRVDVSRRGS AGDCLANPAV PWSQGIDIER ALKMVQVQGM 370 380 390 400 410 420 TGNIQFDTYG RRTNYTIDVY EMKVSGSRKA GYWNEYERFV PFSDQQISND SSSSENRTIV 430 440 450 460 470 480 VTTILESPYV MYKKNHEQLE GNERYEGYCV DLAYEIAKHV RIKYKLSIVG DGKYGARDPE 490 500 510 520 530 540 TKIWNGMVGE LVYGRADIAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS 550 560 570 580 590 600 FLDPLAYEIW MCIVFAYIGV SVVLFLVSRF SPYEWHLEDN NEEPRDPQSP PDPPNEFGIF 610 620 630 640 650 660 NSLWFSLGAF MQQGCDISPR SLSGRIVGGV WWFFTLIIIS SYTANLAAFL TVERMVSPIE 670 680 690 700 710 720 SAEDLAKQTE IAYGTLDSGS TKEFFRRSKI AVYEKMWSYM KSAEPSVFTK TTADGVARVR 730 740 750 760 770 780 KSKGKFAFLL ESTMNEYIEQ RKPCDTMKVG GNLDSKGYGV ATPKGSALGN AVNLAVLKLN 790 800 810 820 830 840 EQGLLDKLKN KWWYDKGECG SGGGDSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF 850 860 870 880 CYKSRAESKR MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI
	Isoform Flip [UniParc]. Checksum: D53A3C20BFB3F620	FASTA	888	100,444
	10 20 30 40 50 60 MGQSVLRAVF FLVLGLLGHS HGGFPNTISI GGLFMRNTVQ EHSAFRFAVQ LYNTNQNTTE 70 80 90 100 110 120 KPFHLNYHVD HLDSSNSFSV TNAFCSQFSR GVYAIFGFYD QMSMNTLTSF CGALHTSFVT 130 140 150 160 170 180 PSFPTDADVQ FVIQMRPALK GAILSLLSYY KWEKFVYLYD TERGFSVLQA IMEAAVQNNW 190 200 210 220 230 240 QVTARSVGNI KDVQEFRRII EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM 250 260 270 280 290 300 LANLGFTDIL LERVMHGGAN ITGFQIVNNE NPMVQQFIQR WVRLDEREFP EAKNAPLKYT 310 320 330 340 350 360 SALTHDAILV IAEAFRYLRR QRVDVSRRGS AGDCLANPAV PWSQGIDIER ALKMVQVQGM 370 380 390 400 410 420 TGNIQFDTYG RRTNYTIDVY EMKVSGSRKA GYWNEYERFV PFSDQQISND SSSSENRTIV 430 440 450 460 470 480 VTTILESPYV MYKKNHEQLE GNERYEGYCV DLAYEIAKHV RIKYKLSIVG DGKYGARDPE 490 500 510 520 530 540 TKIWNGMVGE LVYGRADIAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS 550 560 570 580 590 600 FLDPLAYEIW MCIVFAYIGV SVVLFLVSRF SPYEWHLEDN NEEPRDPQSP PDPPNEFGIF 610 620 630 640 650 660 NSLWFSLGAF MQQGCDISPR SLSGRIVGGV WWFFTLIIIS SYTANLAAFL TVERMVSPIE 670 680 690 700 710 720 SAEDLAKQTE IAYGTLDSGS TKEFFRRSKI AVYEKMWSYM KSAEPSVFTK TTADGVARVR 730 740 750 760 770 780 KSKGKFAFLL ESTMNEYIEQ RKPCDTMKVG GNLDSKGYGV ATPKGSALGT PVNLAVLKLS 790 800 810 820 830 840 EQGILDKLKN KWWYDKGECG AKDSGSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF 850 860 870 880 CYKSRAESKR MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI

References

[1]	"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]. Tissue: Brain.
[2]	"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]. Strain: Sprague-Dawley. Tissue: Forebrain.
[3]	"A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties." Nakanishi N., Schneider N.A., Axel R. Neuron 5:569-581(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT FLIP). Tissue: Brain cortex and Hippocampus.
[4]	"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: ALTERNATIVE SPLICING (ISOFORMS FLIP AND FLOP). Tissue: Brain.
[5]	"Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1." Xia J., Zhang X., Staudinger J., Huganir R.L. Neuron 22:179-187(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRKCABP.
[6]	"GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors." Dong H., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P.F., Huganir R.L. Nature 386:279-284(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRIP1. Tissue: Hippocampus.
[7]	"Association of AMPA receptors with a subset of glutamate receptor-interacting protein in vivo." Wyszynski M., Valtschanoff J.G., Naisbitt S., Dunah A.W., Kim E., Standaert D.G., Weinberg R., Sheng M. J. Neurosci. 19:6528-6537(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRIP2.
[8]	"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.
[9]	"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: SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[10]	"Structure of the S1S2 glutamate binding domain of GLuR3." Ahmed A.H., Wang Q., Sondermann H., Oswald R.E. Proteins 75:628-637(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 407-800 IN COMPLEX WITH GLUTAMATE, DISULFIDE BOND.
[11]	"Molecular mechanism of flop selectivity and subsite recognition for an AMPA receptor allosteric modulator: structures of GluA2 and GluA3 in complexes with PEPA." Ahmed A.H., Ptak C.P., Oswald R.E. Biochemistry 49:2843-2850(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 417-799 IN COMPLEX WITH GLUTAMATE, DISULFIDE BOND.
[12]	"Dynamics and allosteric potential of the AMPA receptor N-terminal domain." Sukumaran M., Rossmann M., Shrivastava I., Dutta A., Bahar I., Greger I.H. EMBO J. 30:972-982(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 23-403, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-260 AND ASN-374.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M36420 mRNA. Translation: AAA41245.1.
X54656 mRNA. Translation: CAA38466.1.
M38062 mRNA. Translation: AAA63480.1.
M85036 mRNA. Translation: AAA41241.2.

IPI

IPI00195443.
IPI00231095.

PIR

C40170.

RefSeq

NP_001106213.1. NM_001112742.1.
NP_116785.2. NM_032990.2.

UniGene

Rn.74049.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DLN	X-ray	1.91	A	407-800	[»]
3DP4	X-ray	2.11	A	407-800	[»]
3LSW	X-ray	1.75	A	417-530	[»]
3LSX	X-ray	2.01	A	417-530	[»]
3M3F	X-ray	2.50	A	417-799	[»]
3M3K	X-ray	1.79	A/C/E	417-799	[»]
3O21	X-ray	2.20	A/B/C/D	23-403	[»]
3P3W	X-ray	4.20	A/B/C/D	23-403	[»]
3RT6	X-ray	2.84	B	417-799	[»]
3RT8	X-ray	2.43	A	417-799	[»]
4F1Y	X-ray	1.79	A/C	417-799	[»]
4F22	X-ray	2.06	A	417-799	[»]
4F29	X-ray	1.75	A	417-799	[»]
4F2O	X-ray	1.91	A	417-799	[»]
4F2Q	X-ray	2.20	A	417-799	[»]
4F31	X-ray	2.29	B/D	417-799	[»]
4F39	X-ray	1.83	A	417-799	[»]
4F3B	X-ray	1.82	A	417-799	[»]
4F3G	X-ray	2.06	A	417-799	[»]

ProteinModelPortal

P19492.

SMR

P19492. Positions 415-530, 657-800.

ModBase

Search...

Protein-protein interaction databases

IntAct

P19492. 4 interactions.

MINT

MINT-86220.

STRING

10116.ENSRNOP00000010367.

PTM databases

PhosphoSite

P19492.

Proteomic databases

PaxDb

P19492.

PRIDE

P19492.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

29628.

KEGG

rno:29628.

UCSC

RGD:70958. rat.

Organism-specific databases

CTD

2892.

RGD

70958. Gria3.

Phylogenomic databases

eggNOG

NOG316680.

HOGENOM

HOG000234372.

HOVERGEN

HBG051839.

KO

K05199.

OrthoDB

EOG4XKV68.

Gene expression databases

ArrayExpress

P19492.

Genevestigator

P19492.

GermOnline

ENSRNOG00000007682. Rattus norvegicus.

Family and domain databases

InterPro

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

Pfam

PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]

PRINTS

PR00177. NMDARECEPTOR.

SMART

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

ProtoNet

Search...

Other

BindingDB

P19492.

ChEMBL

CHEMBL3504.

EvolutionaryTrace

P19492.

NextBio

609848.

Entry information

Entry name

GRIA3_RAT

Accession

Primary (citable) accession number: P19492

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	April 3, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program