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P35439

- NMDZ1_RAT

UniProt

P35439 - NMDZ1_RAT

Protein

Glutamate receptor ionotropic, NMDA 1

Gene

Grin1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei523 – 5231Glycine1 Publication
    Binding sitei688 – 6881Glycine1 Publication
    Binding sitei732 – 7321Glycine1 Publication

    GO - Molecular functioni

    1. calcium channel activity Source: Ensembl
    2. calcium ion binding Source: Ensembl
    3. enzyme binding Source: RGD
    4. extracellular-glutamate-gated ion channel activity Source: RefGenome
    5. glutamate binding Source: UniProtKB
    6. glutamate receptor binding Source: RGD
    7. glycine binding Source: UniProtKB
    8. ionotropic glutamate receptor activity Source: RGD
    9. neurotransmitter binding Source: RGD
    10. N-methyl-D-aspartate selective glutamate receptor activity Source: RGD
    11. protein binding Source: IntAct
    12. protein dimerization activity Source: RGD
    13. protein heterodimerization activity Source: RGD
    14. receptor binding Source: RGD
    15. voltage-gated cation channel activity Source: RGD

    GO - Biological processi

    1. adult locomotory behavior Source: Ensembl
    2. cellular calcium ion homeostasis Source: Ensembl
    3. cellular response to manganese ion Source: RGD
    4. cerebral cortex development Source: Ensembl
    5. conditioned taste aversion Source: Ensembl
    6. ionotropic glutamate receptor signaling pathway Source: RGD
    7. learning or memory Source: RGD
    8. long-term memory Source: Ensembl
    9. male mating behavior Source: Ensembl
    10. negative regulation of neuron apoptotic process Source: Ensembl
    11. olfactory learning Source: Ensembl
    12. pons maturation Source: Ensembl
    13. positive regulation of apoptotic process Source: Ensembl
    14. positive regulation of cell death Source: RGD
    15. positive regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
    16. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    17. prepulse inhibition Source: Ensembl
    18. propylene metabolic process Source: Ensembl
    19. protein tetramerization Source: RGD
    20. regulation of axonogenesis Source: Ensembl
    21. regulation of dendrite morphogenesis Source: Ensembl
    22. regulation of ion transmembrane transport Source: GOC
    23. regulation of long-term neuronal synaptic plasticity Source: Ensembl
    24. regulation of respiratory gaseous exchange Source: Ensembl
    25. regulation of synapse assembly Source: Ensembl
    26. respiratory gaseous exchange Source: Ensembl
    27. response to amine Source: RGD
    28. response to amphetamine Source: Ensembl
    29. response to calcium ion Source: RGD
    30. response to ethanol Source: Ensembl
    31. response to fungicide Source: RGD
    32. response to morphine Source: Ensembl
    33. response to organic cyclic compound Source: RGD
    34. rhythmic process Source: RGD
    35. sensory perception of pain Source: Ensembl
    36. social behavior Source: Ensembl
    37. suckling behavior Source: Ensembl
    38. synaptic transmission, glutamatergic Source: RefGenome
    39. visual learning Source: Ensembl

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Keywords - Ligandi

    Calcium, Magnesium

    Enzyme and pathway databases

    ReactomeiREACT_196389. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_196392. CREB phosphorylation through the activation of CaMKII.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:Grin1
    Synonyms:Nmdar1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi2736. Grin1.

    Subcellular locationi

    Cell membrane By similarity; Multi-pass membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membrane By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity
    Note: Enriched in postsynaptic plasma membrane and postsynaptic densities.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell surface Source: Ensembl
    3. dendrite membrane Source: BHF-UCL
    4. dendritic spine Source: RGD
    5. endoplasmic reticulum Source: Ensembl
    6. excitatory synapse Source: BHF-UCL
    7. N-methyl-D-aspartate selective glutamate receptor complex Source: RGD
    8. postsynaptic density Source: RGD
    9. postsynaptic membrane Source: RefGenome
    10. synapse Source: MGI
    11. synaptic cleft Source: RGD
    12. synaptic vesicle Source: Ensembl
    13. terminal bouton Source: RGD

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 938920Glutamate receptor ionotropic, NMDA 1PRO_0000011589Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi79 – 79InterchainBy similarity
    Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
    Modified residuei889 – 8891Phosphoserine; by PKCBy similarity
    Modified residuei890 – 8901Phosphoserine; by PKC1 Publication
    Modified residuei896 – 8961Phosphoserine; by PKCBy similarity
    Modified residuei897 – 8971Phosphoserine; by PKC1 Publication

    Post-translational modificationi

    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.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP35439.
    PRIDEiP35439.

    PTM databases

    PhosphoSiteiP35439.

    Expressioni

    Gene expression databases

    ArrayExpressiP35439.
    GenevestigatoriP35439.

    Interactioni

    Subunit structurei

    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. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes By similarity. Interacts with DLG4 and MPDZ. Interacts with LRFN1 and LRFN2. Interacts with MYZAP.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dlg4P310164EBI-877897,EBI-375655
    Lrfn2Q460M52EBI-877897,EBI-877185
    Lrfn2Q80TG92EBI-877935,EBI-877092From a different organism.
    Pdzk1Q9JJ403EBI-877897,EBI-7713572

    Protein-protein interaction databases

    BioGridi246573. 7 interactions.
    DIPiDIP-674N.
    IntActiP35439. 11 interactions.
    MINTiMINT-101336.

    Structurei

    Secondary structure

    1
    938
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 3510
    Helixi36 – 5015
    Beta strandi59 – 668
    Helixi71 – 8010
    Helixi83 – 853
    Beta strandi87 – 926
    Turni98 – 1036
    Helixi104 – 1129
    Turni113 – 1153
    Beta strandi118 – 1225
    Helixi126 – 1294
    Turni131 – 1333
    Beta strandi137 – 1415
    Helixi144 – 1463
    Helixi147 – 15610
    Helixi157 – 1593
    Beta strandi163 – 1708
    Helixi171 – 18515
    Turni186 – 1883
    Beta strandi192 – 1976
    Helixi205 – 2128
    Beta strandi218 – 2225
    Helixi225 – 23713
    Beta strandi246 – 2483
    Turni251 – 2544
    Turni256 – 2605
    Beta strandi267 – 2715
    Helixi277 – 29620
    Beta strandi298 – 3003
    Helixi317 – 32610
    Beta strandi334 – 3363
    Beta strandi338 – 3403
    Beta strandi342 – 3443
    Beta strandi351 – 3577
    Beta strandi360 – 3634
    Beta strandi365 – 3673
    Beta strandi372 – 3743
    Beta strandi398 – 4025
    Turni406 – 4083
    Beta strandi409 – 4135
    Beta strandi426 – 4283
    Beta strandi434 – 4396
    Beta strandi450 – 4578
    Helixi458 – 47013
    Beta strandi474 – 4785
    Beta strandi487 – 4893
    Beta strandi491 – 4944
    Beta strandi496 – 4983
    Helixi500 – 5067
    Beta strandi511 – 5133
    Helixi521 – 5244
    Beta strandi527 – 5293
    Beta strandi533 – 54311
    Helixi670 – 6734
    Beta strandi684 – 6874
    Helixi688 – 6947
    Helixi697 – 6993
    Helixi700 – 7067
    Turni707 – 7093
    Beta strandi711 – 7133
    Helixi714 – 7229
    Beta strandi727 – 7326
    Helixi733 – 74210
    Beta strandi746 – 7483
    Beta strandi753 – 7586
    Beta strandi761 – 7633
    Helixi769 – 78113
    Helixi784 – 7929
    Beta strandi794 – 7963

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PB7X-ray1.35A394-544[»]
    A663-800[»]
    1PB8X-ray1.45A394-544[»]
    A663-800[»]
    1PB9X-ray1.60A394-544[»]
    A663-800[»]
    1PBQX-ray1.90A/B394-800[»]
    1Y1MX-ray1.80A/B394-544[»]
    A/B663-800[»]
    1Y1ZX-ray1.50A394-544[»]
    A663-800[»]
    1Y20X-ray1.40A394-544[»]
    A663-800[»]
    2A5TX-ray2.00A394-544[»]
    3Q41X-ray3.40A/B/C21-393[»]
    4KCCX-ray1.89A394-544[»]
    A663-800[»]
    4KFQX-ray2.20A/B394-544[»]
    A/B663-800[»]
    4NF4X-ray2.00A394-544[»]
    A663-800[»]
    4NF5X-ray1.90A394-544[»]
    A663-800[»]
    4NF6X-ray2.10A394-544[»]
    A663-800[»]
    4NF8X-ray1.86A394-544[»]
    A663-800[»]
    4PE5X-ray3.96A/C23-847[»]
    ProteinModelPortaliP35439.
    SMRiP35439. Positions 396-800.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35439.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 559541ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini581 – 63656CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini658 – 812155ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini834 – 938105CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei560 – 58021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei637 – 65721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei813 – 83321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni516 – 5183Glycine binding

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG282132.
    GeneTreeiENSGT00740000115410.
    HOGENOMiHOG000231491.
    HOVERGENiHBG052638.
    KOiK05208.
    OMAiWNHVILL.
    OrthoDBiEOG79GT5V.
    PhylomeDBiP35439.
    TreeFamiTF351405.

    Family and domain databases

    InterProiIPR001828. ANF_lig-bd_rcpt.
    IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
    IPR019594. Glu_rcpt_Glu/Gly-bd.
    IPR001320. Iontro_glu_rcpt.
    IPR001508. NMDA_rcpt.
    IPR028082. Peripla_BP_I.
    IPR001638. SBP_bac_3.
    [Graphical view]
    PfamiPF01094. ANF_receptor. 1 hit.
    PF10562. CaM_bdg_C0. 1 hit.
    PF00060. Lig_chan. 1 hit.
    PF00497. SBP_bac_3. 1 hit.
    [Graphical view]
    PRINTSiPR00177. NMDARECEPTOR.
    SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
    SM00079. PBPe. 1 hit.
    [Graphical view]
    SUPFAMiSSF53822. SSF53822. 1 hit.

    Sequences (7)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: P35439-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN    50
    KRHGSWKIQL NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND 100
    HFTPTPVSYT AGFYRIPVLG LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV 150
    WFEMMRVYNW NHIILLVSDD HEGRAAQKRL ETLLEERESK AEKVLQFDPG 200
    TKNVTALLME ARELEARVII LSASEDDAAT VYRAAAMLNM TGSGYVWLVG 250
    EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN 300
    ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN 350
    YSIMNLQNRK LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI 400
    VTIHQEPFVY VKPTMSDGTC KEEFTVNGDP VKKVICTGPN DTSPGSPRHT 450
    VPQCCYGFCI DLLIKLARTM NFTYEVHLVA DGKFGTQERV NNSNKKEWNG 500
    MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI LVKKEIPRST 550
    LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA 600
    LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN 650
    LAAFLVLDRP EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS 700
    TMYRHMEKHN YESAAEAIQA VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG 750
    ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH ENGFMEDLDK TWVRYQECDS 800
    RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH KDARRKQMQL 850
    AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT 900
    STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES 938
    Length:938
    Mass (Da):105,509
    Last modified:June 1, 1994 - v1
    Checksum:i613D36E38F05BC73
    GO
    Isoform B (identifier: P35439-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:959
    Mass (Da):108,045
    Checksum:iD965531F6C38EDDD
    GO
    Isoform C (identifier: P35439-3) [UniParc]FASTAAdd to Basket

    Also known as: NMDAR1-2a subunit

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

    Show »
    Length:901
    Mass (Da):101,345
    Checksum:iA320F3585664F652
    GO
    Isoform D (identifier: P35439-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:922
    Mass (Da):103,615
    Checksum:iE31E00296E49D08D
    GO
    Isoform E (identifier: P35439-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:885
    Mass (Da):99,451
    Checksum:i6DAA83EFC08C30D8
    GO
    Isoform F (identifier: P35439-6) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:922
    Mass (Da):103,881
    Checksum:i847CEED410182B5C
    GO
    Isoform G (identifier: P35439-7) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:906
    Mass (Da):101,987
    Checksum:i1872055038F790FF
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei190 – 1901K → KSKKRNYENLDQLSYDNKRG PK in isoform B, isoform F and isoform G. CuratedVSP_000140
    Alternative sequencei864 – 90037Missing in isoform F and isoform C. CuratedVSP_000141Add
    BLAST
    Alternative sequencei864 – 88522DRKSG…RAITS → QYHPTDITGPLNLSDPSVST VV in isoform E and isoform G. CuratedVSP_000142Add
    BLAST
    Alternative sequencei886 – 93853Missing in isoform E and isoform G. CuratedVSP_000143Add
    BLAST
    Alternative sequencei901 – 93838STGGG…RHRES → QYHPTDITGPLNLSDPSVST VV in isoform D. CuratedVSP_000144Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiJN0336.
    JN0337.
    JN0338.
    JN0339.
    JN0340.
    JN0341.
    JN0342.
    S19710.
    RefSeqiNP_001257531.1. NM_001270602.1. [P35439-2]
    NP_001257532.1. NM_001270603.1. [P35439-6]
    NP_001257534.1. NM_001270605.1. [P35439-3]
    NP_001257537.1. NM_001270608.1. [P35439-7]
    NP_001257539.1. NM_001270610.1. [P35439-5]
    NP_001274352.1. NM_001287423.1. [P35439-4]
    NP_058706.1. NM_017010.2. [P35439-1]
    UniGeneiRn.9840.

    Genome annotation databases

    EnsembliENSRNOT00000037725; ENSRNOP00000029227; ENSRNOG00000011726. [P35439-2]
    ENSRNOT00000044246; ENSRNOP00000043301; ENSRNOG00000011726. [P35439-6]
    ENSRNOT00000049297; ENSRNOP00000049198; ENSRNOG00000011726. [P35439-1]
    GeneIDi24408.
    KEGGirno:24408.
    UCSCiRGD:2736. rat. [P35439-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi JN0336.
    JN0337.
    JN0338.
    JN0339.
    JN0340.
    JN0341.
    JN0342.
    S19710.
    RefSeqi NP_001257531.1. NM_001270602.1. [P35439-2 ]
    NP_001257532.1. NM_001270603.1. [P35439-6 ]
    NP_001257534.1. NM_001270605.1. [P35439-3 ]
    NP_001257537.1. NM_001270608.1. [P35439-7 ]
    NP_001257539.1. NM_001270610.1. [P35439-5 ]
    NP_001274352.1. NM_001287423.1. [P35439-4 ]
    NP_058706.1. NM_017010.2. [P35439-1 ]
    UniGenei Rn.9840.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PB7 X-ray 1.35 A 394-544 [» ]
    A 663-800 [» ]
    1PB8 X-ray 1.45 A 394-544 [» ]
    A 663-800 [» ]
    1PB9 X-ray 1.60 A 394-544 [» ]
    A 663-800 [» ]
    1PBQ X-ray 1.90 A/B 394-800 [» ]
    1Y1M X-ray 1.80 A/B 394-544 [» ]
    A/B 663-800 [» ]
    1Y1Z X-ray 1.50 A 394-544 [» ]
    A 663-800 [» ]
    1Y20 X-ray 1.40 A 394-544 [» ]
    A 663-800 [» ]
    2A5T X-ray 2.00 A 394-544 [» ]
    3Q41 X-ray 3.40 A/B/C 21-393 [» ]
    4KCC X-ray 1.89 A 394-544 [» ]
    A 663-800 [» ]
    4KFQ X-ray 2.20 A/B 394-544 [» ]
    A/B 663-800 [» ]
    4NF4 X-ray 2.00 A 394-544 [» ]
    A 663-800 [» ]
    4NF5 X-ray 1.90 A 394-544 [» ]
    A 663-800 [» ]
    4NF6 X-ray 2.10 A 394-544 [» ]
    A 663-800 [» ]
    4NF8 X-ray 1.86 A 394-544 [» ]
    A 663-800 [» ]
    4PE5 X-ray 3.96 A/C 23-847 [» ]
    ProteinModelPortali P35439.
    SMRi P35439. Positions 396-800.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246573. 7 interactions.
    DIPi DIP-674N.
    IntActi P35439. 11 interactions.
    MINTi MINT-101336.

    Chemistry

    BindingDBi P35439.
    ChEMBLi CHEMBL2096680.
    GuidetoPHARMACOLOGYi 455.

    PTM databases

    PhosphoSitei P35439.

    Proteomic databases

    PaxDbi P35439.
    PRIDEi P35439.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000037725 ; ENSRNOP00000029227 ; ENSRNOG00000011726 . [P35439-2 ]
    ENSRNOT00000044246 ; ENSRNOP00000043301 ; ENSRNOG00000011726 . [P35439-6 ]
    ENSRNOT00000049297 ; ENSRNOP00000049198 ; ENSRNOG00000011726 . [P35439-1 ]
    GeneIDi 24408.
    KEGGi rno:24408.
    UCSCi RGD:2736. rat. [P35439-1 ]

    Organism-specific databases

    CTDi 2902.
    RGDi 2736. Grin1.

    Phylogenomic databases

    eggNOGi NOG282132.
    GeneTreei ENSGT00740000115410.
    HOGENOMi HOG000231491.
    HOVERGENi HBG052638.
    KOi K05208.
    OMAi WNHVILL.
    OrthoDBi EOG79GT5V.
    PhylomeDBi P35439.
    TreeFami TF351405.

    Enzyme and pathway databases

    Reactomei REACT_196389. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_196392. CREB phosphorylation through the activation of CaMKII.

    Miscellaneous databases

    EvolutionaryTracei P35439.
    NextBioi 603223.
    PROi P35439.

    Gene expression databases

    ArrayExpressi P35439.
    Genevestigatori P35439.

    Family and domain databases

    InterProi 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.
    IPR028082. Peripla_BP_I.
    IPR001638. SBP_bac_3.
    [Graphical view ]
    Pfami PF01094. ANF_receptor. 1 hit.
    PF10562. CaM_bdg_C0. 1 hit.
    PF00060. Lig_chan. 1 hit.
    PF00497. SBP_bac_3. 1 hit.
    [Graphical view ]
    PRINTSi PR00177. NMDARECEPTOR.
    SMARTi SM00918. Lig_chan-Glu_bd. 1 hit.
    SM00079. PBPe. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53822. SSF53822. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: PHOSPHORYLATION AT SER-897, DEPHOSPHORYLATION BY PPP2CB, 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.

    Entry informationi

    Entry nameiNMDZ1_RAT
    AccessioniPrimary (citable) accession number: P35439
    Secondary accession number(s): Q62646
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 164 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3