P35439 (NMDZ1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate receptor ionotropic, NMDA 1
Short name=GluN1

Alternative name(s):
Glutamate [NMDA] receptor subunit zeta-1
N-methyl-D-aspartate receptor subunit NR1
Short name=NMD-R1

Gene names

Name:	Grin1
Synonyms:	Nmdar1

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	938 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	NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. Plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors. Ref.18
Subunit structure	Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A or GRIN3B); disulfide-linked By similarity. Found in a complex with GRIN2A or GRIN2B, GRIN3A and PPP2CB. Found in a complex with GRIN2A or GRIN2B and GRIN3B By similarity. Interacts with DLG4 and MPDZ. Interacts with LRFN1 and LRFN2. Interacts with MYZAP. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity. Cell junction › synapse › postsynaptic cell membrane By similarity. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density By similarity. Note: Enriched in postsynaptic plasma membrane and postsynaptic densities By similarity.
Post-translational modification	NMDA is probably regulated by C-terminal phosphorylation of an isoform of NR1 by PKC. Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB). Its phosphorylated state is influenced by the formation of the NMDAR-PPP2CB complex and the NMDAR channel activity. Ref.7 Ref.12
Sequence similarities	Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR1/GRIN1 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
Ligand	Calcium Magnesium
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult locomotory behavior Inferred from electronic annotation. Source: Compara cellular calcium ion homeostasis Inferred from electronic annotation. Source: Compara cellular response to manganese ion Inferred from expression pattern PubMed 19643132. Source: RGD cerebral cortex development Inferred from electronic annotation. Source: Compara conditioned taste aversion Inferred from electronic annotation. Source: Compara learning or memory Traceable author statement PubMed 12535174. Source: RGD long-term memory Inferred from electronic annotation. Source: Compara male mating behavior Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara olfactory learning Inferred from electronic annotation. Source: Compara pons maturation Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell death Inferred from direct assay PubMed 20168047. Source: RGD positive regulation of excitatory postsynaptic membrane potential Inferred from direct assay PubMed 12930820. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara prepulse inhibition Inferred from electronic annotation. Source: Compara propylene metabolic process Inferred from electronic annotation. Source: Compara protein tetramerization Inferred from direct assay PubMed 22493736. Source: RGD regulation of axonogenesis Inferred from electronic annotation. Source: Compara regulation of dendrite morphogenesis Inferred from electronic annotation. Source: Compara regulation of long-term neuronal synaptic plasticity Inferred from electronic annotation. Source: Compara regulation of respiratory gaseous exchange Inferred from electronic annotation. Source: Compara regulation of synapse assembly Inferred from electronic annotation. Source: Compara respiratory gaseous exchange Inferred from electronic annotation. Source: Compara response to amine stimulus Inferred from expression pattern PubMed 19918184. Source: RGD response to amphetamine Inferred from electronic annotation. Source: Compara response to calcium ion Inferred from expression pattern PubMed 19761817. Source: RGD response to fungicide Inferred from expression pattern PubMed 19591855. Source: RGD response to morphine Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from expression pattern PubMed 19322657. Source: RGD rhythmic process Inferred from direct assay PubMed 16477151. Source: RGD sensory perception of pain Inferred from electronic annotation. Source: Compara social behavior Inferred from electronic annotation. Source: Compara suckling behavior Inferred from electronic annotation. Source: Compara synaptic transmission, glutamatergic Inferred from electronic annotation. Source: Compara visual learning Inferred from electronic annotation. Source: Compara
Cellular_component	N-methyl-D-aspartate selective glutamate receptor complex Inferred from direct assay PubMed 16477151PubMed 17050728PubMed 22493736. Source: RGD cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from electronic annotation. Source: Compara dendrite membrane Inferred from direct assay PubMed 15620359. Source: BHF-UCL excitatory synapse Inferred from direct assay PubMed 19730411. Source: BHF-UCL outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro postsynaptic density Inferred from direct assay PubMed 17207780PubMed 21314939. Source: RGD postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synaptic cleft Inferred from direct assay PubMed 17207780. Source: RGD synaptic vesicle Inferred from electronic annotation. Source: Compara terminal bouton Inferred from direct assay PubMed 19666514. Source: RGD
Molecular_function	N-methyl-D-aspartate selective glutamate receptor activity Inferred from direct assay PubMed 16477151PubMed 22098737. Source: RGD calcium channel activity Inferred from electronic annotation. Source: Compara calcium ion binding Inferred from electronic annotation. Source: Compara extracellular-glutamate-gated ion channel activity Inferred from electronic annotation. Source: InterPro glutamate binding Inferred from direct assay PubMed 8011339. Source: UniProtKB glycine binding Inferred from direct assay PubMed 8011339. Source: UniProtKB neurotransmitter binding Inferred from direct assay PubMed 16477151. Source: RGD protein heterodimerization activity Inferred from direct assay PubMed 21544205. Source: RGD voltage-gated cation channel activity Inferred from mutant phenotype PubMed 17050728. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Lrfn2	Q460M5	2	EBI-877897,EBI-877185
Lrfn2	Q80TG9	2	EBI-877923,EBI-877092	From a different organism.

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: P35439-1)

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 B (identifier: P35439-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK

Isoform C (identifier: P35439-3)

Also known as: NMDAR1-2a subunit;

The sequence of this isoform differs from the canonical sequence as follows:
     864-900: Missing.

Isoform D (identifier: P35439-4)

The sequence of this isoform differs from the canonical sequence as follows:
     901-938: STGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES → QYHPTDITGPLNLSDPSVSTVV

Isoform E (identifier: P35439-5)

The sequence of this isoform differs from the canonical sequence as follows:
     864-885: DRKSGRAEPDPKKKATFRAITS → QYHPTDITGPLNLSDPSVSTVV
     886-938: Missing.

Isoform F (identifier: P35439-6)

Also known as: NMDAR1-2b subunit;

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
     864-900: Missing.

Isoform G (identifier: P35439-7)

Also known as: NMDAR1-4b subunit;

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
     864-885: DRKSGRAEPDPKKKATFRAITS → QYHPTDITGPLNLSDPSVSTVV
     886-938: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Chain

19 – 938

920

Glutamate receptor ionotropic, NMDA 1

PRO_0000011589

Regions

Topological domain

19 – 559

541

Extracellular Potential

Transmembrane

560 – 580

21

Helical; Potential

Topological domain

581 – 636

56

Cytoplasmic Potential

Transmembrane

637 – 657

21

Helical; Potential

Topological domain

658 – 812

155

Extracellular Potential

Transmembrane

813 – 833

21

Helical; Potential

Topological domain

834 – 938

105

Cytoplasmic Potential

Region

516 – 518

3

Glycine binding

Sites

Binding site

523

1

Glycine

Binding site

688

1

Glycine

Binding site

732

1

Glycine

Amino acid modifications

Modified residue

889

1

Phosphoserine; by PKC By similarity

Modified residue

890

1

Phosphoserine; by PKC Ref.12

Modified residue

896

1

Phosphoserine; by PKC By similarity

Modified residue

897

1

Phosphoserine; by PKC

Glycosylation

61

1

N-linked (GlcNAc...) Potential

Glycosylation

203

1

N-linked (GlcNAc...) Potential

Glycosylation

239

1

N-linked (GlcNAc...) Potential

Glycosylation

276

1

N-linked (GlcNAc...) Potential

Glycosylation

300

1

N-linked (GlcNAc...) Potential

Glycosylation

350

1

N-linked (GlcNAc...) Potential

Glycosylation

368

1

N-linked (GlcNAc...) Potential

Glycosylation

440

1

N-linked (GlcNAc...) Potential

Glycosylation

471

1

N-linked (GlcNAc...) Potential

Glycosylation

491

1

N-linked (GlcNAc...) Potential

Disulfide bond

79

Interchain By similarity

Natural variations

Alternative sequence

190

1

K → KSKKRNYENLDQLSYDNKRG PK in isoform B, isoform F and isoform G.

VSP_000140

Alternative sequence

864 – 900

37

Missing in isoform F and isoform C.

VSP_000141

Alternative sequence

864 – 885

22

DRKSG…RAITS → QYHPTDITGPLNLSDPSVST VV in isoform E and isoform G.

VSP_000142

Alternative sequence

886 – 938

53

Missing in isoform E and isoform G.

VSP_000143

Alternative sequence

901 – 938

38

STGGG…RHRES → QYHPTDITGPLNLSDPSVST VV in isoform D.

VSP_000144

Secondary structure

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938

Helix Strand Turn

Details...

Beta strand

26 – 35

10

Helix

36 – 50

15

Beta strand

59 – 66

8

Helix

71 – 80

10

Helix

83 – 85

3

Beta strand

87 – 92

6

Turn

98 – 103

6

Helix

104 – 112

9

Turn

113 – 115

3

Beta strand

118 – 122

5

Helix

126 – 129

4

Turn

131 – 133

3

Beta strand

137 – 141

5

Helix

144 – 146

3

Helix

147 – 156

10

Helix

157 – 159

3

Beta strand

163 – 170

8

Helix

171 – 185

15

Turn

186 – 188

3

Beta strand

192 – 197

6

Helix

205 – 212

8

Beta strand

218 – 222

5

Helix

225 – 237

13

Beta strand

246 – 248

3

Turn

251 – 254

4

Turn

256 – 260

5

Beta strand

267 – 271

5

Helix

277 – 296

20

Beta strand

298 – 300

3

Helix

317 – 326

10

Beta strand

334 – 336

3

Beta strand

338 – 340

3

Beta strand

342 – 344

3

Beta strand

351 – 357

7

Beta strand

360 – 363

4

Beta strand

365 – 367

3

Beta strand

372 – 374

3

Beta strand

398 – 402

5

Turn

406 – 408

3

Beta strand

409 – 413

5

Beta strand

434 – 439

6

Beta strand

450 – 457

8

Helix

458 – 470

13

Beta strand

474 – 478

5

Beta strand

487 – 489

3

Beta strand

491 – 494

4

Beta strand

496 – 498

3

Helix

500 – 506

7

Beta strand

511 – 513

3

Helix

521 – 524

4

Beta strand

527 – 529

3

Beta strand

533 – 543

11

Helix

670 – 673

4

Beta strand

684 – 687

4

Helix

688 – 694

7

Helix

697 – 699

3

Helix

700 – 706

7

Turn

707 – 709

3

Beta strand

711 – 713

3

Helix

714 – 722

9

Beta strand

727 – 732

6

Helix

733 – 742

10

Beta strand

746 – 748

3

Beta strand

753 – 758

6

Beta strand

761 – 763

3

Helix

769 – 781

13

Helix

784 – 792

9

Beta strand

794 – 796

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 613D36E38F05BC73	FASTA	938	105,509
	10 20 30 40 50 60 MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL 70 80 90 100 110 120 NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG 130 140 150 160 170 180 LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL 190 200 210 220 230 240 ETLLEERESK AEKVLQFDPG TKNVTALLME ARELEARVII LSASEDDAAT VYRAAAMLNM 250 260 270 280 290 300 TGSGYVWLVG EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN 310 320 330 340 350 360 ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK 370 380 390 400 410 420 LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTMSDGTC 430 440 450 460 470 480 KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCI DLLIKLARTM NFTYEVHLVA 490 500 510 520 530 540 DGKFGTQERV NNSNKKEWNG MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI 550 560 570 580 590 600 LVKKEIPRST LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA 610 620 630 640 650 660 LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVLDRP 670 680 690 700 710 720 EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS TMYRHMEKHN YESAAEAIQA 730 740 750 760 770 780 VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH 790 800 810 820 830 840 ENGFMEDLDK TWVRYQECDS RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH 850 860 870 880 890 900 KDARRKQMQL AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT 910 920 930 STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES
	Isoform B [UniParc]. Checksum: D965531F6C38EDDD	FASTA	959	108,045
	10 20 30 40 50 60 MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL 70 80 90 100 110 120 NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG 130 140 150 160 170 180 LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL 190 200 210 220 230 240 ETLLEERESK SKKRNYENLD QLSYDNKRGP KAEKVLQFDP GTKNVTALLM EARELEARVI 250 260 270 280 290 300 ILSASEDDAA TVYRAAAMLN MTGSGYVWLV GEREISGNAL RYAPDGIIGL QLINGKNESA 310 320 330 340 350 360 HISDAVGVVA QAVHELLEKE NITDPPRGCV GNTNIWKTGP LFKRVLMSSK YADGVTGRVE 370 380 390 400 410 420 FNEDGDRKFA NYSIMNLQNR KLVQVGIYNG THVIPNDRKI IWPGGETEKP RGYQMSTRLK 430 440 450 460 470 480 IVTIHQEPFV YVKPTMSDGT CKEEFTVNGD PVKKVICTGP NDTSPGSPRH TVPQCCYGFC 490 500 510 520 530 540 IDLLIKLART MNFTYEVHLV ADGKFGTQER VNNSNKKEWN GMMGELLSGQ ADMIVAPLTI 550 560 570 580 590 600 NNERAQYIEF SKPFKYQGLT ILVKKEIPRS TLDSFMQPFQ STLWLLVGLS VHVVAVMLYL 610 620 630 640 650 660 LDRFSPFGRF KVNSEEEEED ALTLSSAMWF SWGVLLNSGI GEGAPRSFSA RILGMVWAGF 670 680 690 700 710 720 AMIIVASYTA NLAAFLVLDR PEERITGIND PRLRNPSDKF IYATVKQSSV DIYFRRQVEL 730 740 750 760 770 780 STMYRHMEKH NYESAAEAIQ AVRDNKLHAF IWDSAVLEFE ASQKCDLVTT GELFFRSGFG 790 800 810 820 830 840 IGMRKDSPWK QNVSLSILKS HENGFMEDLD KTWVRYQECD SRSNAPATLT FENMAGVFML 850 860 870 880 890 900 VAGGIVAGIF LIFIEIAYKR HKDARRKQMQ LAFAAVNVWR KNLQDRKSGR AEPDPKKKAT 910 920 930 940 950 FRAITSTLAS SFKRRRSSKD TSTGGGRGAL QNQKDTVLPR RAIEREEGQL QLCSRHRES
	Isoform C (NMDAR1-2a subunit) [UniParc]. Checksum: A320F3585664F652	FASTA	901	101,345
	10 20 30 40 50 60 MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL 70 80 90 100 110 120 NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG 130 140 150 160 170 180 LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL 190 200 210 220 230 240 ETLLEERESK AEKVLQFDPG TKNVTALLME ARELEARVII LSASEDDAAT VYRAAAMLNM 250 260 270 280 290 300 TGSGYVWLVG EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN 310 320 330 340 350 360 ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK 370 380 390 400 410 420 LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTMSDGTC 430 440 450 460 470 480 KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCI DLLIKLARTM NFTYEVHLVA 490 500 510 520 530 540 DGKFGTQERV NNSNKKEWNG MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI 550 560 570 580 590 600 LVKKEIPRST LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA 610 620 630 640 650 660 LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVLDRP 670 680 690 700 710 720 EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS TMYRHMEKHN YESAAEAIQA 730 740 750 760 770 780 VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH 790 800 810 820 830 840 ENGFMEDLDK TWVRYQECDS RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH 850 860 870 880 890 900 KDARRKQMQL AFAAVNVWRK NLQSTGGGRG ALQNQKDTVL PRRAIEREEG QLQLCSRHRE S
	Isoform D [UniParc]. Checksum: E31E00296E49D08D	FASTA	922	103,615
	10 20 30 40 50 60 MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL 70 80 90 100 110 120 NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG 130 140 150 160 170 180 LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL 190 200 210 220 230 240 ETLLEERESK AEKVLQFDPG TKNVTALLME ARELEARVII LSASEDDAAT VYRAAAMLNM 250 260 270 280 290 300 TGSGYVWLVG EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN 310 320 330 340 350 360 ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK 370 380 390 400 410 420 LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTMSDGTC 430 440 450 460 470 480 KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCI DLLIKLARTM NFTYEVHLVA 490 500 510 520 530 540 DGKFGTQERV NNSNKKEWNG MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI 550 560 570 580 590 600 LVKKEIPRST LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA 610 620 630 640 650 660 LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVLDRP 670 680 690 700 710 720 EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS TMYRHMEKHN YESAAEAIQA 730 740 750 760 770 780 VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH 790 800 810 820 830 840 ENGFMEDLDK TWVRYQECDS RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH 850 860 870 880 890 900 KDARRKQMQL AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT 910 920 QYHPTDITGP LNLSDPSVST VV
	Isoform E [UniParc]. Checksum: 6DAA83EFC08C30D8	FASTA	885	99,451
	10 20 30 40 50 60 MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL 70 80 90 100 110 120 NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG 130 140 150 160 170 180 LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL 190 200 210 220 230 240 ETLLEERESK AEKVLQFDPG TKNVTALLME ARELEARVII LSASEDDAAT VYRAAAMLNM 250 260 270 280 290 300 TGSGYVWLVG EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN 310 320 330 340 350 360 ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK 370 380 390 400 410 420 LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTMSDGTC 430 440 450 460 470 480 KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCI DLLIKLARTM NFTYEVHLVA 490 500 510 520 530 540 DGKFGTQERV NNSNKKEWNG MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI 550 560 570 580 590 600 LVKKEIPRST LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA 610 620 630 640 650 660 LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVLDRP 670 680 690 700 710 720 EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS TMYRHMEKHN YESAAEAIQA 730 740 750 760 770 780 VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH 790 800 810 820 830 840 ENGFMEDLDK TWVRYQECDS RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH 850 860 870 880 KDARRKQMQL AFAAVNVWRK NLQQYHPTDI TGPLNLSDPS VSTVV
	Isoform F (NMDAR1-2b subunit) [UniParc]. Checksum: 847CEED410182B5C	FASTA	922	103,881
	10 20 30 40 50 60 MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL 70 80 90 100 110 120 NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG 130 140 150 160 170 180 LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL 190 200 210 220 230 240 ETLLEERESK SKKRNYENLD QLSYDNKRGP KAEKVLQFDP GTKNVTALLM EARELEARVI 250 260 270 280 290 300 ILSASEDDAA TVYRAAAMLN MTGSGYVWLV GEREISGNAL RYAPDGIIGL QLINGKNESA 310 320 330 340 350 360 HISDAVGVVA QAVHELLEKE NITDPPRGCV GNTNIWKTGP LFKRVLMSSK YADGVTGRVE 370 380 390 400 410 420 FNEDGDRKFA NYSIMNLQNR KLVQVGIYNG THVIPNDRKI IWPGGETEKP RGYQMSTRLK 430 440 450 460 470 480 IVTIHQEPFV YVKPTMSDGT CKEEFTVNGD PVKKVICTGP NDTSPGSPRH TVPQCCYGFC 490 500 510 520 530 540 IDLLIKLART MNFTYEVHLV ADGKFGTQER VNNSNKKEWN GMMGELLSGQ ADMIVAPLTI 550 560 570 580 590 600 NNERAQYIEF SKPFKYQGLT ILVKKEIPRS TLDSFMQPFQ STLWLLVGLS VHVVAVMLYL 610 620 630 640 650 660 LDRFSPFGRF KVNSEEEEED ALTLSSAMWF SWGVLLNSGI GEGAPRSFSA RILGMVWAGF 670 680 690 700 710 720 AMIIVASYTA NLAAFLVLDR PEERITGIND PRLRNPSDKF IYATVKQSSV DIYFRRQVEL 730 740 750 760 770 780 STMYRHMEKH NYESAAEAIQ AVRDNKLHAF IWDSAVLEFE ASQKCDLVTT GELFFRSGFG 790 800 810 820 830 840 IGMRKDSPWK QNVSLSILKS HENGFMEDLD KTWVRYQECD SRSNAPATLT FENMAGVFML 850 860 870 880 890 900 VAGGIVAGIF LIFIEIAYKR HKDARRKQMQ LAFAAVNVWR KNLQSTGGGR GALQNQKDTV 910 920 LPRRAIEREE GQLQLCSRHR ES
	Isoform G (NMDAR1-4b subunit) [UniParc]. Checksum: 1872055038F790FF	FASTA	906	101,987
	10 20 30 40 50 60 MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL 70 80 90 100 110 120 NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG 130 140 150 160 170 180 LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL 190 200 210 220 230 240 ETLLEERESK SKKRNYENLD QLSYDNKRGP KAEKVLQFDP GTKNVTALLM EARELEARVI 250 260 270 280 290 300 ILSASEDDAA TVYRAAAMLN MTGSGYVWLV GEREISGNAL RYAPDGIIGL QLINGKNESA 310 320 330 340 350 360 HISDAVGVVA QAVHELLEKE NITDPPRGCV GNTNIWKTGP LFKRVLMSSK YADGVTGRVE 370 380 390 400 410 420 FNEDGDRKFA NYSIMNLQNR KLVQVGIYNG THVIPNDRKI IWPGGETEKP RGYQMSTRLK 430 440 450 460 470 480 IVTIHQEPFV YVKPTMSDGT CKEEFTVNGD PVKKVICTGP NDTSPGSPRH TVPQCCYGFC 490 500 510 520 530 540 IDLLIKLART MNFTYEVHLV ADGKFGTQER VNNSNKKEWN GMMGELLSGQ ADMIVAPLTI 550 560 570 580 590 600 NNERAQYIEF SKPFKYQGLT ILVKKEIPRS TLDSFMQPFQ STLWLLVGLS VHVVAVMLYL 610 620 630 640 650 660 LDRFSPFGRF KVNSEEEEED ALTLSSAMWF SWGVLLNSGI GEGAPRSFSA RILGMVWAGF 670 680 690 700 710 720 AMIIVASYTA NLAAFLVLDR PEERITGIND PRLRNPSDKF IYATVKQSSV DIYFRRQVEL 730 740 750 760 770 780 STMYRHMEKH NYESAAEAIQ AVRDNKLHAF IWDSAVLEFE ASQKCDLVTT GELFFRSGFG 790 800 810 820 830 840 IGMRKDSPWK QNVSLSILKS HENGFMEDLD KTWVRYQECD SRSNAPATLT FENMAGVFML 850 860 870 880 890 900 VAGGIVAGIF LIFIEIAYKR HKDARRKQMQ LAFAAVNVWR KNLQQYHPTD ITGPLNLSDP SVSTVV

References

[1]	"Molecular cloning and characterization of the rat NMDA receptor." Moriyoshi K., Masu M., Ishii T., Shigemoto R., Mizuno N., Nakanishi S. Nature 354:31-37(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Brain.
[2]	"Alternative splicing generates functionally distinct N-methyl-D-aspartate receptors." Nakanishi N., Axel R., Shneider N.A. Proc. Natl. Acad. Sci. U.S.A. 89:8552-8556(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor." Hollmann M., Boulter J., Maron C., Beasley L., Sullivan J., Pecht G., Heinemann S.F. Neuron 10:943-954(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Forebrain.
[4]	"Cloning and analysis of the 5' flanking sequence of the rat N-methyl-D-aspartate receptor 1 (NMDAR1) gene." Bai G., Kusiak J.W. Biochim. Biophys. Acta 1152:197-200(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-86. Strain: Sprague-Dawley. Tissue: Liver.
[5]	"Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing." Sugihara H., Moriyoshi K., Ishii T., Masu M., Nakanishi S. Biochem. Biophys. Res. Commun. 185:826-832(1992) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING. Tissue: Brain.
[6]	"Combinatorial RNA splicing alters the surface charge on the NMDA receptor." Anantharam V., Panchal R., Wilson A., Koltchin V.V., Treistman S.N., Bayley H. FEBS Lett. 305:27-30(1992) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING. Tissue: Brain.
[7]	"An NMDA receptor signaling complex with protein phosphatase 2A." Chan S.F., Sucher N.J. J. Neurosci. 21:7985-7992(2001) [PubMed] [Europe PMC] [Abstract] Cited for: DEPHOSPHORYLATION, IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B; GRIN3A AND PPP2CB.
[8]	"Assembly with the NR1 subunit is required for surface expression of NR3A-containing NMDA receptors." Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A., Trimmer J.S., Sucher N.J., Heinemann S.F. J. Neurosci. 21:1228-1237(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
[9]	"Association of NR3A with the N-methyl-D-aspartate receptor NR1 and NR2 subunits." Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B., Yasuda R.P. Mol. Pharmacol. 62:1119-1127(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
[10]	"Characterization and comparison of the NR3A subunit of the NMDA receptor in recombinant systems and primary cortical neurons." Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V., Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J., Lipton S.A. J. Neurophysiol. 87:2052-2063(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
[11]	"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation." Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E. Neuron 43:563-574(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MPDZ AND DLG4.
[12]	"Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms." Sanchez-Perez A.M., Felipo V. Neurochem. Int. 47:84-91(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-890.
[13]	"A novel family of adhesion-like molecules that interacts with the NMDA receptor." Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J. J. Neurosci. 26:2174-2183(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LRFN2.
[14]	"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.
[15]	"GRINL1A colocalizes with N-methyl D-aspartate receptor NR1 subunit and reduces N-methyl D-aspartate toxicity." Roginski R.S., Goubaeva F., Mikami M., Fried-Cassorla E., Nair M.R., Yang J. NeuroReport 19:1721-1726(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYZAP.
[16]	"Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core." Furukawa H., Gouaux E. EMBO J. 22:2873-2885(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 394-800 IN COMPLEXES WITH AGONISTS AND ANTAGONIST.
[17]	"Subunit arrangement and function in NMDA receptors." Furukawa H., Singh S.K., Mancusso R., Gouaux E. Nature 438:185-192(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 394-800 IN COMPLEX WITH GRIN2A; GLYCINE AND GLUTAMATE, SUBUNIT.
[18]	"Mechanism of partial agonist action at the NR1 subunit of NMDA receptors." Inanobe A., Furukawa H., Gouaux E. Neuron 47:71-84(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 394-800 IN COMPLEXES WITH AGONISTS, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X63255 mRNA. Translation: CAA44914.1.
AY157515 Genomic DNA. Translation: AAA16366.1.
U08261 mRNA. Translation: AAB50926.1.
U08262 mRNA. Translation: AAB50927.1.
U08263 mRNA. Translation: AAB50928.1.
U08264 mRNA. Translation: AAB50929.1.
U08265 mRNA. Translation: AAB50930.1.
U08267 mRNA. Translation: AAB50932.1.
U08268 mRNA. Translation: AAB50933.1.
S39217 mRNA. Translation: AAB22431.1.
S39218 mRNA. Translation: AAB22432.1.
S39219 mRNA. Translation: AAB22433.1.
S39220 mRNA. Translation: AAB22434.1.
S39221 mRNA. Translation: AAB22435.1.
X65227 mRNA. Translation: CAA46335.1.

IPI

IPI00198625.
IPI00231254.
IPI00231255.
IPI00231256.
IPI00231257.
IPI00231259.
IPI00389747.

PIR

JN0336.
JN0337.
JN0338.
JN0339.
JN0340.
JN0341.
JN0342.
S19710.

RefSeq

NP_001257531.1. NM_001270602.1.
NP_001257532.1. NM_001270603.1.
NP_001257534.1. NM_001270605.1.
NP_001257537.1. NM_001270608.1.
NP_001257539.1. NM_001270610.1.
NP_058706.1. NM_017010.2.

UniGene

Rn.9840.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PB7	X-ray	1.35	A	394-800	[»]
1PB8	X-ray	1.45	A	394-800	[»]
1PB9	X-ray	1.60	A	394-800	[»]
1PBQ	X-ray	1.90	A/B	394-800	[»]
1Y1M	X-ray	1.80	A/B	394-800	[»]
1Y1Z	X-ray	1.50	A	394-800	[»]
1Y20	X-ray	1.40	A	394-800	[»]
2A5T	X-ray	2.00	A	394-800	[»]
3Q41	X-ray	3.40	A/B/C	21-393	[»]

ProteinModelPortal

P35439.

SMR

P35439. Positions 396-800.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-674N.

IntAct

P35439. 3 interactions.

MINT

MINT-101336.

PTM databases

PhosphoSite

P35439.

Proteomic databases

PaxDb

P35439.

PRIDE

P35439.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000037725; ENSRNOP00000029227; ENSRNOG00000011726.
ENSRNOT00000044246; ENSRNOP00000043301; ENSRNOG00000011726.
ENSRNOT00000049297; ENSRNOP00000049198; ENSRNOG00000011726.

GeneID

24408.

KEGG

rno:24408.

UCSC

RGD:2736. rat.

Organism-specific databases

CTD

2902.

RGD

2736. Grin1.

Phylogenomic databases

eggNOG

NOG282132.

GeneTree

ENSGT00700000104113.

HOGENOM

HOG000231491.

HOVERGEN

HBG052638.

KO

K05208.

OMA

VYRSAAM.

Gene expression databases

ArrayExpress

P35439.

Genevestigator

P35439.

GermOnline

ENSRNOG00000011726. Rattus norvegicus.

Family and domain databases

InterPro

IPR001828. ANF_lig-bd_rcpt.
IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR001638. SBP_bac_3.
[Graphical view]

Pfam

PF01094. ANF_receptor. 1 hit.
PF10562. CaM_bdg_C0. 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]

ProtoNet

Search...

Other

BindingDB

P35439.

ChEMBL

CHEMBL330.

EvolutionaryTrace

P35439.

NextBio

603223.

Entry information

Entry name

NMDZ1_RAT

Accession

Primary (citable) accession number: P35439
Secondary accession number(s): Q62646

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 148 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program