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Protein
Submitted name:

NMDA glutamate receptor subunit

Gene

grin1

Organism
Xenopus laevis (African clawed frog)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channelSAAS annotation, ReceptorSAAS annotationImported

Keywords - Biological processi

Ion transport, Transport

Protein family/group databases

TCDBi1.A.10.1.12. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

Names & Taxonomyi

Protein namesi
Submitted name:
NMDA glutamate receptor subunitImported
Gene namesi
Name:grin1Imported
Synonyms:NR1Imported
OrganismiXenopus laevis (African clawed frog)Imported
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-866327. grin1.

Subcellular locationi

  • Cell junctionsynapse SAAS annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei581 – 59919HelicalSequence analysisAdd
BLAST
Transmembranei654 – 67623HelicalSequence analysisAdd
BLAST
Transmembranei832 – 85625HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membraneSAAS annotation, Membrane, Postsynaptic cell membraneSAAS annotation, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 904884Sequence analysisPRO_5007324443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi79 ↔ 329Combined sources
Glycosylationi297 – 2971N-linked (GlcNAc...)Combined sourcesCAR_5007324439
Glycosylationi321 – 3211N-linked (GlcNAc...)Combined sourcesCAR_5007324442
Glycosylationi389 – 3891N-linked (GlcNAc...)Combined sourcesCAR_5007324441

Interactioni

Protein-protein interaction databases

DIPiDIP-59169N.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QEKX-ray2.00A/B23-405[»]
3QELX-ray2.60A/C23-405[»]
3QEMX-ray3.00A/C23-405[»]
5EWJX-ray2.77A/C23-408[»]
5EWLX-ray2.98A/C23-408[»]
5EWMX-ray2.76A/C23-408[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini454 – 814361PBPeInterPro annotationAdd
BLAST
Domaini460 – 52667Lig_chan-Glu_bdInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. [View classification]SAAS annotation

Keywords - Domaini

SignalSequence analysis, Transmembrane, Transmembrane helixSequence analysisSAAS annotation

Phylogenomic databases

HOVERGENiHBG052638.
KOiK05208.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF10562. CaM_bdg_C0. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q91977-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTMRLFLLA VLFLFSFARA GCDPKIVNIG AVLSTKKHEQ IFREAVNQAN
60 70 80 90 100
KRHFTRKIQL NATSVTHRPN AIQMALSVCE DLISSQVYAI LVSHPPAPTD
110 120 130 140 150
HLTPTPISYT AGFYRIPVIG LTTRMSIYSD KSIHLSFLRT VPPYSHQALV
160 170 180 190 200
WFEMMRLFNW NHVILIVSDD HEGRAAQKKL ETLLEGKESK SKKRNYENLD
210 220 230 240 250
QLSYDNKRGP KADKVLQFEP GTKNLTALLL EAKELEARVI ILSASEDDAT
260 270 280 290 300
AVYKSAAMLD MTGAGYVWLV GEREISGSAL RYAPDGIIGL QLINGKNESA
310 320 330 340 350
HISDAVAVVA QAIHELFEME NITDPPRGCV GNTNIWKTGP LFKRVLMSSK
360 370 380 390 400
YPDGVTGRIE FNEDGDRKFA NYSIMNLQNR KLVQVGIFNG SYIIQNDRKI
410 420 430 440 450
IWPGGETERP QGYQMSTRLK IVTIHQEPFV YVRPTTSDGT CREEYTINGD
460 470 480 490 500
PIKKVICNGP NETIPGRPTV PQCCYGFCVD LLIKLAREMN FTYEVHLVAD
510 520 530 540 550
GKFGTQERVN NSNKKEWNGM MGELLSGQAD MIVAPLTINN ERAQYIEFSK
560 570 580 590 600
PFKYQGLTIL VKKEIPRSTL DSFMQPFQST LWLLVGLSVH VVAVMLYLLD
610 620 630 640 650
RFSPFGRFKV NSEEEEEDAL TLSSAMWFSW GVLLNSGIGE GAPRSFSARI
660 670 680 690 700
LGMVWAGFAM IIVASYTANL AAFLVLDRPE ERITGINDPR LRNPSDKFIY
710 720 730 740 750
ATVKQSSVDI YFRRQVELST MYRHMEKHNY ESAAEAIQAV RDNKLHAFIW
760 770 780 790 800
DSAVLEFEAS QKCDLVTTGE LFFRSGFGIG MRKDSPWKQN VSLNILKSHE
810 820 830 840 850
NGFMEELDKT WVRYQECDSR SNAPATLTFE NMAGVFMLVA GGIVAGIFLI
860 870 880 890 900
FIEIAYKRHK DARRKQMQLA FAAVNVWRKN LQQYPPTDIT GQLNLSDPSV

STVV
Length:904
Mass (Da):101,894
Last modified:November 1, 1996 - v1
Checksum:i46D8FE0EA6D903F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94081 mRNA. Translation: CAA63825.1.
X94156 mRNA. Translation: CAA63871.1.
RefSeqiNP_001081615.1. NM_001088146.1.
UniGeneiXl.135.

Genome annotation databases

GeneIDi397953.
KEGGixla:397953.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94081 mRNA. Translation: CAA63825.1.
X94156 mRNA. Translation: CAA63871.1.
RefSeqiNP_001081615.1. NM_001088146.1.
UniGeneiXl.135.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QEKX-ray2.00A/B23-405[»]
3QELX-ray2.60A/C23-405[»]
3QEMX-ray3.00A/C23-405[»]
5EWJX-ray2.77A/C23-408[»]
5EWLX-ray2.98A/C23-408[»]
5EWMX-ray2.76A/C23-408[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59169N.

Protein family/group databases

TCDBi1.A.10.1.12. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397953.
KEGGixla:397953.

Organism-specific databases

CTDi2902.
XenbaseiXB-GENE-866327. grin1.

Phylogenomic databases

HOVERGENiHBG052638.
KOiK05208.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF10562. CaM_bdg_C0. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Heinlein U.A.O.
    Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: BrainImported.
  2. "A new type of ionotropic glutamate receptors."
    Soloviev M.M., Ishimaru H., Barnard E.A.
    Bioorg. Khim. 22:468-471(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: BrainImported.
  3. "Functional expression of a recombinant unitary glutamate receptor from Xenopus, which contains N-methyl-D-aspartate (NMDA) and non-NMDA receptor subunits."
    Soloviev M.M., Brierley M.J., Shao Z.Y., Mellor I.R., Volkova T.M., Kamboj R., Ishimaru H., Sudan H., Harris J., Foldes R.L., Grishin E.V., Usherwood P.N.R., Barnard E.A.
    J. Biol. Chem. 271:32572-32579(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: BrainImported.
  4. "Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors."
    Karakas E., Simorowski N., Furukawa H.
    Nature 475:249-253(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 23-405, GLYCOSYLATION AT ASN-297; ASN-321 AND ASN-389, DISULFIDE BONDS.
  5. "A Novel Binding Mode Reveals Two Distinct Classes of NMDA Receptor GluN2B-selective Antagonists."
    Stroebel D., Buhl D.L., Knafels J.D., Chanda P.K., Green M., Sciabola S., Mony L., Paoletti P., Pandit J.
    Mol. Pharmacol. 89:541-551(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 23-408, DISULFIDE BONDS.

Entry informationi

Entry nameiQ91977_XENLA
AccessioniPrimary (citable) accession number: Q91977
Secondary accession number(s): Q91805
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.