P22756 (GRIK1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate receptor ionotropic, kainate 1
Short name=GluK1

Alternative name(s):
Glutamate receptor 5
Short name=GluR-5
Short name=GluR5

Gene names

Name:	Grik1
Synonyms:	Glur5

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	949 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. May be involved in the transmission of light information from the retina to the hypothalamus. Ref.7
Subunit structure	Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers Probable. The unedited version (Q) assembles into a functional kainate-gated homomeric channel, whereas the edited version (R) is unable to produce channel activity when expressed alone. Both edited and unedited versions can form functional channels with GRIK4 and GRIK5. Interacts with KLHL17. Ref.3 Ref.5 Ref.7
Subcellular location	Cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in subsets of neurons throughout the developing and adult central and peripheral nervous systems. In the CNS principally in the medial amygdaloid nuclei, medial habenulae, pyriform and cingulate cortices, and Purkinje cell layer. Also highly expressed in embryonic and adult dorsal root ganglia.
Miscellaneous	The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate > L-glutamate = quisqualate > CNQX = DNQX > AMPA > dihydrokainate > NMDA.
Sequence similarities	Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK1 subfamily. [View classification]
RNA editing	Edited at position 636. Partially edited.

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing RNA editing
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of synaptic transmission, GABAergic Inferred from direct assay PubMed 12533604. Source: RGD negative regulation of synaptic transmission, glutamatergic Inferred from direct assay PubMed 17395219. Source: RGD nervous system development Inferred from mutant phenotype Ref.2. Source: RGD positive regulation of synaptic transmission, GABAergic Inferred from direct assay PubMed 12533604. Source: RGD regulation of short-term neuronal synaptic plasticity Inferred from direct assay PubMed 17395219. Source: RGD synaptic transmission Traceable author statement PubMed 12533604. Source: UniProtKB
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW dendrite Inferred from direct assay PubMed 15844209. Source: RGD ionotropic glutamate receptor complex Inferred from direct assay Ref.7. Source: RGD neuronal cell body Inferred from direct assay PubMed 15844209. Source: RGD postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell terminal bouton Inferred from direct assay PubMed 15844209PubMed 16360275. Source: RGD
Molecular_function	drug binding Inferred from direct assay PubMed 12904467. Source: RGD extracellular-glutamate-gated ion channel activity Inferred from direct assay Ref.2. Source: RGD glutamate binding Inferred from direct assay PubMed 12533604Ref.7. Source: RGD kainate selective glutamate receptor activity Inferred from direct assay PubMed 17395219. Source: RGD protein homodimerization activity Inferred from direct assay Ref.7. Source: RGD voltage-gated cation channel activity Inferred from mutant phenotype PubMed 12904467. Source: RGD
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform Glur5-2C (identifier: P22756-1)

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 Glur5-2 (identifier: P22756-2)

The sequence of this isoform differs from the canonical sequence as follows:
     402-416: Missing.
     870-898: Missing.

Isoform Glur5-2A (identifier: P22756-3)

The sequence of this isoform differs from the canonical sequence as follows:
     870-871: KG → HY
     872-949: Missing.

Isoform Glur5-2B (identifier: P22756-4)

Also known as: Glur5-1;

The sequence of this isoform differs from the canonical sequence as follows:
     870-898: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Potential

Chain

31 – 949

919

Glutamate receptor ionotropic, kainate 1

PRO_0000011543

Regions

Topological domain

31 – 576

546

Extracellular Potential

Transmembrane

577 – 597

21

Helical; Potential

Topological domain

598 – 653

56

Cytoplasmic Potential

Transmembrane

654 – 674

21

Helical; Potential

Topological domain

675 – 834

160

Extracellular Potential

Transmembrane

835 – 855

21

Helical; Potential

Topological domain

856 – 949

94

Cytoplasmic Potential

Region

531 – 533

3

Glutamate binding

Region

704 – 705

2

Glutamate binding

Sites

Binding site

538

1

Glutamate

Binding site

753

1

Glutamate

Amino acid modifications

Modified residue

725

1

Phosphoserine; by PKC Potential

Modified residue

761

1

Phosphothreonine; by PKC Potential

Glycosylation

68

1

N-linked (GlcNAc...) Potential

Glycosylation

74

1

N-linked (GlcNAc...) Potential

Glycosylation

276

1

N-linked (GlcNAc...) Potential

Glycosylation

379

1

N-linked (GlcNAc...) Potential

Glycosylation

428

1

N-linked (GlcNAc...) Potential

Glycosylation

439

1

N-linked (GlcNAc...) Potential

Glycosylation

446

1

N-linked (GlcNAc...) Potential

Glycosylation

561

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

402 – 416

15

Missing in isoform Glur5-2.

VSP_000129

Alternative sequence

870 – 898

29

Missing in isoform Glur5-2B and isoform Glur5-2.

VSP_000130

Alternative sequence

870 – 871

2

KG → HY in isoform Glur5-2A.

VSP_000131

Alternative sequence

872 – 949

78

Missing in isoform Glur5-2A.

VSP_000132

Natural variant

636

1

Q → R in RNA edited version.

Experimental info

Sequence conflict

282

1

K → L in AAA02874. Ref.2

Sequence conflict

354 – 355

2

CA → WR in AAA02874. Ref.2

Sequence conflict

477

1

A → G in AAA02874. Ref.2

Secondary structure

1

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949

Helix Strand Turn

Details...

Beta strand

449 – 453

5

Turn

457 – 459

3

Beta strand

460 – 462

3

Helix

471 – 474

4

Beta strand

475 – 477

3

Helix

478 – 490

13

Beta strand

494 – 498

5

Helix

515 – 521

7

Beta strand

526 – 528

3

Helix

536 – 539

4

Beta strand

542 – 544

3

Beta strand

548 – 551

4

Beta strand

553 – 559

7

Beta strand

680 – 682

3

Helix

686 – 690

5

Beta strand

693 – 698

6

Helix

704 – 711

8

Helix

715 – 724

10

Beta strand

727 – 729

3

Beta strand

731 – 735

5

Helix

736 – 745

10

Beta strand

746 – 753

8

Helix

754 – 763

10

Beta strand

767 – 771

5

Beta strand

777 – 779

3

Beta strand

782 – 784

3

Helix

789 – 802

14

Helix

805 – 813

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform Glur5-2C [UniParc]. Last modified November 1, 1995. Version 3. Checksum: 020660BDD00054E0	FASTA	949	107,840
	10 20 30 40 50 60 MERSTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP VNVEELAFKF 70 80 90 100 110 120 AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL ALGVAALFGP SHSSSVSAVQ 130 140 150 160 170 180 SICNALEVPH IQTRWKHPSV DSRDLFYINL YPDYAAISRA VLDLVLYYNW KTVTVVYEDS 190 200 210 220 230 240 TGLIRLQELI KAPSRYNIKI KIRQLPPANK DAKPLLKEMK KSKEFYVIFD CSHETAAEIL 250 260 270 280 290 300 KQILFMGMMT EYYHYFFTTL DLFALDLELY RYSGVNMTGF RKLNIDNPHV SSIIEKWSME 310 320 330 340 350 360 RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR HKPCALGPRF 370 380 390 400 410 420 MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT EKASGEVSKH LYKVWKKIGI 430 440 450 460 470 480 WNSNSGLNMT DGNRDRSNNI TDSLANRTLI VTTILEEPYV MYRKSDKPLY GNDRFEAYCL 490 500 510 520 530 540 DLLKELSNIL GFLYDVKLVP DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK 550 560 570 580 590 600 VIDFSKPFMT LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT 610 620 630 640 650 660 PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI VGGIWWFFTL 670 680 690 700 710 720 IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV RDGSTMTFFK KSKISTYEKM 730 740 750 760 770 780 WAFMSSRQQS ALVKNSDEGI QRVLTTDYAL LMESTSIEYV TQRNCNLTQI GGLIDSKGYG 790 800 810 820 830 840 VGTPIGSPYR DKITIAILQL QEEGKLHMMK EKWWRGNGCP EEDSKEASAL GVENIGGIFI 850 860 870 880 890 900 VLAAGLVLSV FVAIGEFLYK SRKNNDVEQK GKSSRLRFYF RNKVRFHGSK KESLGVEKCL 910 920 930 940 SFNAIMEELG ISLKNQKKLK KKSRTKGKSS FTSILTCHQR RTQRKETVA
	Isoform Glur5-2 [UniParc]. Checksum: B674CECB3FB60F47	FASTA	905	102,646
	10 20 30 40 50 60 MERSTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP VNVEELAFKF 70 80 90 100 110 120 AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL ALGVAALFGP SHSSSVSAVQ 130 140 150 160 170 180 SICNALEVPH IQTRWKHPSV DSRDLFYINL YPDYAAISRA VLDLVLYYNW KTVTVVYEDS 190 200 210 220 230 240 TGLIRLQELI KAPSRYNIKI KIRQLPPANK DAKPLLKEMK KSKEFYVIFD CSHETAAEIL 250 260 270 280 290 300 KQILFMGMMT EYYHYFFTTL DLFALDLELY RYSGVNMTGF RKLNIDNPHV SSIIEKWSME 310 320 330 340 350 360 RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR HKPCALGPRF 370 380 390 400 410 420 MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT EKIGIWNSNS GLNMTDGNRD 430 440 450 460 470 480 RSNNITDSLA NRTLIVTTIL EEPYVMYRKS DKPLYGNDRF EAYCLDLLKE LSNILGFLYD 490 500 510 520 530 540 VKLVPDGKYG AQNDKGEWNG MVKELIDHRA DLAVAPLTIT YVREKVIDFS KPFMTLGISI 550 560 570 580 590 600 LYRKPNGTNP GVFSFLNPLS PDIWMYVLLA CLGVSCVLFV IARFTPYEWY NPHPCNPDSD 610 620 630 640 650 660 VVENNFTLLN SFWFGVGALM QQGSELMPKA LSTRIVGGIW WFFTLIIISS YTANLAAFLT 670 680 690 700 710 720 VERMESPIDS ADDLAKQTKI EYGAVRDGST MTFFKKSKIS TYEKMWAFMS SRQQSALVKN 730 740 750 760 770 780 SDEGIQRVLT TDYALLMEST SIEYVTQRNC NLTQIGGLID SKGYGVGTPI GSPYRDKITI 790 800 810 820 830 840 AILQLQEEGK LHMMKEKWWR GNGCPEEDSK EASALGVENI GGIFIVLAAG LVLSVFVAIG 850 860 870 880 890 900 EFLYKSRKNN DVEQCLSFNA IMEELGISLK NQKKLKKKSR TKGKSSFTSI LTCHQRRTQR KETVA
	Isoform Glur5-2A [UniParc]. Checksum: CC3EEB35068FDB54	FASTA	871	98,853
	10 20 30 40 50 60 MERSTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP VNVEELAFKF 70 80 90 100 110 120 AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL ALGVAALFGP SHSSSVSAVQ 130 140 150 160 170 180 SICNALEVPH IQTRWKHPSV DSRDLFYINL YPDYAAISRA VLDLVLYYNW KTVTVVYEDS 190 200 210 220 230 240 TGLIRLQELI KAPSRYNIKI KIRQLPPANK DAKPLLKEMK KSKEFYVIFD CSHETAAEIL 250 260 270 280 290 300 KQILFMGMMT EYYHYFFTTL DLFALDLELY RYSGVNMTGF RKLNIDNPHV SSIIEKWSME 310 320 330 340 350 360 RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR HKPCALGPRF 370 380 390 400 410 420 MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT EKASGEVSKH LYKVWKKIGI 430 440 450 460 470 480 WNSNSGLNMT DGNRDRSNNI TDSLANRTLI VTTILEEPYV MYRKSDKPLY GNDRFEAYCL 490 500 510 520 530 540 DLLKELSNIL GFLYDVKLVP DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK 550 560 570 580 590 600 VIDFSKPFMT LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT 610 620 630 640 650 660 PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI VGGIWWFFTL 670 680 690 700 710 720 IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV RDGSTMTFFK KSKISTYEKM 730 740 750 760 770 780 WAFMSSRQQS ALVKNSDEGI QRVLTTDYAL LMESTSIEYV TQRNCNLTQI GGLIDSKGYG 790 800 810 820 830 840 VGTPIGSPYR DKITIAILQL QEEGKLHMMK EKWWRGNGCP EEDSKEASAL GVENIGGIFI 850 860 870 VLAAGLVLSV FVAIGEFLYK SRKNNDVEQH Y
	Isoform Glur5-2B (Glur5-1) [UniParc]. Checksum: 4609F0CDF337B3D1	FASTA	920	104,388
	10 20 30 40 50 60 MERSTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP VNVEELAFKF 70 80 90 100 110 120 AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL ALGVAALFGP SHSSSVSAVQ 130 140 150 160 170 180 SICNALEVPH IQTRWKHPSV DSRDLFYINL YPDYAAISRA VLDLVLYYNW KTVTVVYEDS 190 200 210 220 230 240 TGLIRLQELI KAPSRYNIKI KIRQLPPANK DAKPLLKEMK KSKEFYVIFD CSHETAAEIL 250 260 270 280 290 300 KQILFMGMMT EYYHYFFTTL DLFALDLELY RYSGVNMTGF RKLNIDNPHV SSIIEKWSME 310 320 330 340 350 360 RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR HKPCALGPRF 370 380 390 400 410 420 MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT EKASGEVSKH LYKVWKKIGI 430 440 450 460 470 480 WNSNSGLNMT DGNRDRSNNI TDSLANRTLI VTTILEEPYV MYRKSDKPLY GNDRFEAYCL 490 500 510 520 530 540 DLLKELSNIL GFLYDVKLVP DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK 550 560 570 580 590 600 VIDFSKPFMT LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT 610 620 630 640 650 660 PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI VGGIWWFFTL 670 680 690 700 710 720 IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV RDGSTMTFFK KSKISTYEKM 730 740 750 760 770 780 WAFMSSRQQS ALVKNSDEGI QRVLTTDYAL LMESTSIEYV TQRNCNLTQI GGLIDSKGYG 790 800 810 820 830 840 VGTPIGSPYR DKITIAILQL QEEGKLHMMK EKWWRGNGCP EEDSKEASAL GVENIGGIFI 850 860 870 880 890 900 VLAAGLVLSV FVAIGEFLYK SRKNNDVEQC LSFNAIMEEL GISLKNQKKL KKKSRTKGKS 910 920 SFTSILTCHQ RRTQRKETVA

References

[1]	"A glutamate receptor channel with high affinity for domoate and kainate." Sommer B., Burnashev N., Verdoorn T.A., Keinaenen K., Sakmann B., Seeburg P.H. EMBO J. 11:1651-1656(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING. Tissue: Brain.
[2]	"Cloning of a novel glutamate receptor subunit, GluR5: expression in the nervous system during development." Bettler B., Boulter J., Hermans-Borgmeyer I., O'Shea-Greenfield A., Deneris E.S., Moll C., Borgmeyer U., Hollmann M., Heinemann S.F. Neuron 5:583-595(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathway." Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M., Singer J.D., Marshall J. J. Biol. Chem. 281:40164-40173(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KLHL17.
[4]	"High-affinity kainate and domoate receptors in rat brain." Lomeli H., Wisden W., Koehler M., Keinaenen K., Sommer B., Seeburg P.H. FEBS Lett. 307:139-143(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[5]	"Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate." Naur P., Vestergaard B., Skov L.K., Egebjerg J., Gajhede M., Kastrup J.S. FEBS Lett. 579:1154-1160(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 445-820 IN COMPLEX WITH GLUTAMATE, SUBUNIT.
[6]	"Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity." Mayer M.L. Neuron 45:539-552(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 446-821 IN COMPLEX WITH GLUTAMATE.
[7]	"Crystal structures of the kainate receptor GluR5 ligand binding core dimer with novel GluR5-selective antagonists." Mayer M.L., Ghosal A., Dolman N.P., Jane D.E. J. Neurosci. 26:2852-2861(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 446-820 IN COMPLEXES WITH UBP302 AND UBP310, FUNCTION, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M83560 mRNA. Translation: AAA02873.1.
M83561 mRNA. Translation: AAA02874.1.
Z11712 mRNA. Translation: CAA77775.1.
Z11713 mRNA. Translation: CAA77776.1.
Z11714 mRNA. Translation: CAA77777.1.

IPI

IPI00231402.
IPI00569872.
IPI00951061.
IPI00952320.

PIR

S19808.

RefSeq

NP_001104584.1. NM_001111114.1.
NP_001104587.1. NM_001111117.1.
NP_058937.1. NM_017241.2.

UniGene

Rn.10449.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TXF	X-ray	2.10	A	446-821	[»]
1VSO	X-ray	1.85	A	445-820	[»]
1YCJ	X-ray	1.95	A/B	445-820	[»]
2F34	X-ray	1.74	A/B	446-820	[»]
2F35	X-ray	1.87	A/B	446-820	[»]
2F36	X-ray	2.11	A/B/C/D	446-820	[»]
2OJT	X-ray	1.95	A/B	446-820	[»]
2PBW	X-ray	2.50	A/B	445-820	[»]
2QS1	X-ray	1.80	A/B	446-820	[»]
2QS2	X-ray	1.80	A/B	446-820	[»]
2QS3	X-ray	1.76	A/B	446-820	[»]
2QS4	X-ray	1.58	A/B/C/D	446-820	[»]
2WKY	X-ray	2.20	A/B	445-821	[»]
3C31	X-ray	1.49	A/B	446-821	[»]
3C32	X-ray	1.72	A/B	446-821	[»]
3C33	X-ray	1.72	A/B	446-821	[»]
3C34	X-ray	1.82	A/B	446-821	[»]
3C35	X-ray	1.97	A/B	446-821	[»]
3C36	X-ray	1.68	A/B	446-821	[»]
3GBA	X-ray	1.35	A/B/C/D	445-820	[»]
3GBB	X-ray	2.10	A/B	445-805	[»]
3S2V	X-ray	2.50	A/B	445-820	[»]
4DLD	X-ray	2.00	A/B	445-820	[»]
4E0X	X-ray	2.00	A/B	445-820	[»]

ProteinModelPortal

P22756.

SMR

P22756. Positions 445-559.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29257N.

STRING

10116.ENSRNOP00000045594.

Protein family/group databases

TCDB

1.A.10.1.5. glutamate-gated ion channel (GIC) family of neurotransmitter receptors.

PTM databases

PhosphoSite

P22756.

Proteomic databases

PaxDb

P22756.

PRIDE

P22756.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000042581; ENSRNOP00000050263; ENSRNOG00000001575.
ENSRNOT00000051060; ENSRNOP00000046164; ENSRNOG00000001575.

GeneID

29559.

KEGG

rno:29559.

UCSC

RGD:2732. rat.

Organism-specific databases

CTD

2897.

RGD

2732. Grik1.

Phylogenomic databases

eggNOG

NOG316680.

GeneTree

ENSGT00590000083056.

HOGENOM

HOG000234371.

HOVERGEN

HBG051839.

InParanoid

P22756.

KO

K05201.

Gene expression databases

ArrayExpress

P22756.

Genevestigator

P22756.

GermOnline

ENSRNOG00000001575. 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

P22756.

ChEMBL

CHEMBL2919.

EvolutionaryTrace

P22756.

NextBio

609606.

Entry information

Entry name

GRIK1_RAT

Accession

Primary (citable) accession number: P22756

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program