NMDZ1_CANLF
ID NMDZ1_CANLF Reviewed; 943 AA.
AC Q5R1P0; Q5R1P1; Q5R1P2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 1;
DE Short=GluN1;
DE AltName: Full=Glutamate [NMDA] receptor subunit zeta-1;
DE AltName: Full=N-methyl-D-aspartate receptor 1;
DE AltName: Full=N-methyl-D-aspartate receptor subunit NR1;
DE Short=NMD-R1;
DE Flags: Precursor;
GN Name=GRIN1; Synonyms=NMDAR1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Brain cortex;
RA Taki K., Shinjo K.;
RT "Canis familiaris glutamate receptor, ionotropic, N-methyl D-aspartate 1
RT (GRIN1), transcript variant NR1-4, mRNA, complete cds.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of NMDA receptor complexes that function as
CC heterotetrameric, ligand-gated ion channels with high calcium
CC permeability and voltage-dependent sensitivity to magnesium. Channel
CC activation requires binding of the neurotransmitter glutamate to the
CC epsilon subunit, glycine binding to the zeta subunit, plus membrane
CC depolarization to eliminate channel inhibition by Mg(2+). Sensitivity
CC to glutamate and channel kinetics depend on the subunit composition.
CC {ECO:0000250|UniProtKB:P35438}.
CC -!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon
CC subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A
CC or GRIN3B). Found in a complex with GRIN2A or GRIN2B and GRIN3B (By
CC similarity). Found in a complex with GRIN2A or GRIN2B, GRIN3A and
CC PPP2CB (By similarity). Interacts with DLG4 and MPDZ (By similarity).
CC Interacts with LRFN1 and LRFN2 (By similarity). Interacts with MYZAP.
CC Interacts with SNX27 (via PDZ domain); the interaction is required for
CC recycling to the plasma membrane when endocytosed and prevent
CC degradation in lysosomes (By similarity). Found in a complex with DLG4
CC and PRR7 (By similarity). Found in a complex with GRIN2B and PRR7 (By
CC similarity). Interacts with PRR7; the interaction is reduced following
CC NMDA receptor activity (By similarity). {ECO:0000250|UniProtKB:P35438,
CC ECO:0000250|UniProtKB:P35439}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35439};
CC Multi-pass membrane protein {ECO:0000305}. Postsynaptic cell membrane
CC {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Enriched in
CC postsynaptic plasma membrane and postsynaptic densities. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5R1P0-1; Sequence=Displayed;
CC Name=2; Synonyms=NR1-4;
CC IsoId=Q5R1P0-2; Sequence=VSP_014220;
CC Name=3; Synonyms=NR1-3b;
CC IsoId=Q5R1P0-3; Sequence=VSP_014221;
CC Name=4; Synonyms=NR1-1;
CC IsoId=Q5R1P0-4; Sequence=VSP_014220, VSP_014221;
CC -!- DOMAIN: A hydrophobic region that gives rise to the prediction of a
CC transmembrane span does not cross the membrane, but is part of a
CC discontinuously helical region that dips into the membrane and is
CC probably part of the pore and of the selectivity filter.
CC {ECO:0000250|UniProtKB:A0A1L8F5J9}.
CC -!- PTM: NMDA is probably regulated by C-terminal phosphorylation of an
CC isoform of NR1 by PKC. Dephosphorylated on Ser-918 probably by protein
CC phosphatase 2A (PPP2CB). Its phosphorylated state is influenced by the
CC formation of the NMDAR-PPP2CB complex and the NMDAR channel activity
CC (By similarity). {ECO:0000250|UniProtKB:P35439}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR1/GRIN1 subfamily. {ECO:0000305}.
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DR EMBL; AB195993; BAD74216.1; -; mRNA.
DR EMBL; AB195994; BAD74217.1; -; mRNA.
DR EMBL; AB195995; BAD74218.1; -; mRNA.
DR RefSeq; NP_001008717.1; NM_001008717.1. [Q5R1P0-2]
DR AlphaFoldDB; Q5R1P0; -.
DR SMR; Q5R1P0; -.
DR STRING; 9615.ENSCAFP00000037473; -.
DR Ensembl; ENSCAFT00030009788; ENSCAFP00030008563; ENSCAFG00030005339. [Q5R1P0-3]
DR Ensembl; ENSCAFT00030009880; ENSCAFP00030008649; ENSCAFG00030005339. [Q5R1P0-1]
DR Ensembl; ENSCAFT00040022091; ENSCAFP00040019164; ENSCAFG00040011986. [Q5R1P0-3]
DR Ensembl; ENSCAFT00040022256; ENSCAFP00040019306; ENSCAFG00040011986. [Q5R1P0-1]
DR GeneID; 494007; -.
DR KEGG; cfa:494007; -.
DR CTD; 2902; -.
DR eggNOG; KOG4440; Eukaryota.
DR InParanoid; Q5R1P0; -.
DR OrthoDB; 188544at2759; -.
DR Reactome; R-CFA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-CFA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-CFA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-CFA-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-CFA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0016594; F:glycine binding; ISS:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF10562; CaM_bdg_C0; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..943
FT /note="Glutamate receptor ionotropic, NMDA 1"
FT /id="PRO_0000011586"
FT TOPO_DOM 21..580
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT TOPO_DOM 602..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT INTRAMEM 624..645
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:A0A1L8F5J9"
FT TOPO_DOM 646..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT TRANSMEM 652..668
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT TOPO_DOM 669..833
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT TRANSMEM 834..854
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT TOPO_DOM 855..943
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT REGION 624..645
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:A0A1L8F5J9"
FT BINDING 537..539
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 544
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 709
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 753
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 695
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 79..329
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT DISULFID 441..475
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT DISULFID 457..476
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT DISULFID 765..819
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT VAR_SEQ 190..210
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014220"
FT VAR_SEQ 885..921
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014221"
SQ SEQUENCE 943 AA; 106118 MW; EC8811B090F5577C CRC64;
MSTMRLLTLA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL
NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG
LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYSW NHIILLVSDD HEGRAAQKRL
ETLLEERESK SKKRNYENLD QLSYDHKRGP KAEKVLQFDP GTKNVTALLM EARELEARVI
ILSASEDDAA TVYRAAAMLN MTGSGYVWLV GEREISGNAL RYAPDGIIGL QLINGKNESA
HISDAVGVVA QAVHELLEKE NITDPPRGCV GNTNIWKTGP LFKRVLMSSK YADGVTGRVE
FNEDGDRKFA NYSIMNLQNR KLVQVGIYNG THVIPNDRKI IWPGGETEKP RGYQMSTRLK
IVTIHQEPFV YVKPTLSDGT CKEEFTVNGD PVKKVICTGP NDTSPGSPRH TVPQCCYGFC
IDLLIKLART MNFTYEVHLV ADGKFGTQER VNNSNKKEWN GMMGELLSGQ ADMIVAPLTI
NNERAQYIEF SKPFKYQGLT ILVKKEIPRS TLDSFMQPFQ STLWLLVGLS VHVVAVMLYL
LDRFSPFGRF KVNSEEEEED ALTLSSAMWF SWGVLLNSGI GEGAPRSFSA RILGMVWAGF
AMIIVASYTA NLAAFLVLDR PEERITGIND PRLRNPSDKF IYATVKQSSV DIYFRRQVEL
STMYRHMEKH NYESAAEAIQ AVRDNKLHAF IWDSAVLEFE ASQKCDLVTT GELFFRSGFG
IGMRKDSPWK QNVSLSILKS HENGFMEDLD KTWVRYQECD SRSNAPATLT FENMAGVFML
VAGGIVAGIF LIFIEIAYKR HKDARRKQMQ LAFAAVNVWR KNLQDRKSGR AEPDPKKKAT
FRAITSTLAS SFKRRRSSKD TQYHPTDITG TLNLSDPSVS TVV
